Membrane Proteins of Known Structure

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mpstruc is a curated database of membrane proteins of known 3D structure. To be included in the database, a structure must be available in the RSCB Protein Data Bank (PDB) and have been published in a peer reviewed journal. The database is manually curated based upon on-going literature surveys. Because of the labor involved, new structures are not posted until they are released by the PDB and the complete reference, including pagination for print journals, is available in PubMed. Our goal is to make mpstruc as accurate and complete as possible. If you find errors or omissions, please send a message to Gracie Han, or mpstruc emphasizes structures determined by diffraction and cryo-EM methods. NMR structures are also included whenever identified. A comprehensive list of NMR-determined structures has been established by Dror Warschawski and is available from the Atoine Loquet lab.

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Members of the Bridge Institute at USC join the mpstruc team: We're pleased to announce that the Ray Stevens and Vadim Cherezov labs will join us in maintaining and improving the mpstruc database. Dr. Gye Won "Gracie" Han will be the voice of the group.
Membrane-embedded structures now available!: Mark Sansom's lab at Oxford has created the MemProtMD database of all known transmembrane proteins embedded in lipid membranes, described in Stansfeld et al. (2015) Structure 23:1350-1361. Links to the structures are now included in mpstruc. Click on the icon, and you will be taken to the appropriate entry in MemProtMD.
MPtopo XML data representations now available: XML representations are now available for the MPtopo membrane protein topology database.

Latest new protein entered: 26 Apr 2024 at 10:07 PDT.
Last database update: 26 Apr 2024 at 10:07 PDT

New Structures:

YbtPQ ABC importer in occluded state:: Escherichia coli, 3.10 Å
Bitter taste receptor TAS2R14 - G_i complex with bound cholesterol and intracellular tastant cmpd28.1: Homo sapiens, 2.68 Å
Lnt apoplipoprotein N-acyltransferase in 7.10 monoacylglycerol (MAG): Escherichia coli, 2.19 Å
AlgE alginate export protein in 7.10 monoacylglycerol (MAG): Pseudomonas aeruginosa, 1.45 Å
A_2A adenosine receptor in 7.10 monoacylglycerol (MAG): Homo sapiens, 2.37 Å
Hypo-osmolality-gated calcium-permeable channel TMEM63B in digitonin detergent: Homo sapiens, 3.84 Å

Unique proteins in database = 1704

Coördinate files in database = 7711

Published reports of membrane protein structures in database = 3377

A full list of pdb codes currently in the database is available here.

Unique proteins include proteins of same type from different species. For example, photosynthetic reaction centers from R. viridis and R. sphaeroides are considered unique. Structures of mutagenized versions of proteins already in the database are excluded as unique. Proteins that differ only by substrate bound or by physiological state are also excluded. Structures 'obsoleted' by the PDB are not included.

Total number of PDB coördinate files, including those for unique proteins. This number reflects the fact that published reports of structures often include several coördinate files describing, for example, the protein in different crystal forms, or with different bound substrates.

New Pre-Publication Structures: (links to mpstruc bulletin board page):

A word about the new interface to the protein table.

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Links to the Protein Data Bank Site

Links to the Structural Biology Knowledgebase Site

Membrane Proteins of Known 3D Structure
(Table description)
Protein	PDB Code	Links	Reference (links are to PubMed)
MONOTOPIC MEMBRANE PROTEINS Reviewed by Allen et al. (2018) Database of Peripheral Membrane Proteins
Cyclooxygenases
*Ram Prostaglandin H2 synthase-1 (cyclooxygenase-1 or COX-1): Ovis aries* E Eukaryota, 3.5 Å**	1PRH	Data File Jmol Viewer prostaglandin synthase-1 (COX-1)	Picot et al. (1994). Picot D, Loll PJ, & Garavito RM (1994). The x-ray crystal structure of the membrane protein prostaglandin H₂synthase-1. Nature 367 :243-249. PubMed Id: 8121489.
*Ram Prostaglandin H2 synthase-1 (COX-1): Ovis aries* E Eukaryota, 3.4 Å** In complex with bromoaspirin.	1PTH	Data File Jmol Viewer	Loll et al. (1995). Loll PJ, Picot D, & Garavito RM (1995). The structural basis of aspirin activity inferred from the crystal structure of inactivated prostaglandin H2 synthase. Nat Struct Biol 2 :637-643. PubMed Id: 7552725.
*Ram Prostaglandin H2 synthase-1 (COX-1): Ovis aries* E Eukaryota, 3.1 Å** In complex with flurbiprofen.	1CQE	Data File Jmol Viewer	Garavito et al. (1995). Garavito RM, Picot D, & Loll PJ (1995). The 3.1 A X-ray crystal structure of the integral membrane enzyme prostaglandin H2 synthase-1. Adv Prostaglandin Thromboxane Leukot Res 23 :99-103. PubMed Id: 7732912.
*Ram Prostaglandin H2 synthase-1 (COX-1): Ovis aries* E Eukaryota, 2.61 Å** 1EQG is complex with ibuprofen. Complex with flurbiprofen, 2.70 Å: 1EQH Complex with flurbiprofen methyl ester, 2.75 Å: 1HT5 Complex with alclofenac, 2.69 Å: 1HT8	1EQG	Data File Jmol Viewer	Selinsky et al. (2001). Selinsky BS, Gupta K, Sharkey CT, Loll PJ (2001). Structural analysis of NSAID binding by prostaglandin H2 synthase: time-dependent and time-independent inhibitors elicit identical enzyme conformations. Biochemistry 40 :5172-5180. PubMed Id: 11318639.
*Ram Prostaglandin H2 synthase-1 (COX-1): Ovis aries* E Eukaryota, 3.2 Å** In complex with O-actylsalicylhydroxamic acid.	1EBV	Data File Jmol Viewer	Loll et al. (2001). Loll PJ, Sharkey CT, O'Connor SJ, Dooley CM, O'Brien E, Devocelle M, Nolan KB, Selinsky BS, & Fitzgerald DJ (2001). O-acetylsalicylhydroxamic acid, a novel acetylating inhibitor of prostaglandin H2 synthase: structural and functional characterization of enzyme-inhibitor interactions. Mol Pharmacol 60 :1407-1413. PubMed Id: 11723249.
*Ram Prostaglandin H2 synthase-1 (COX-1): Ovis aries* E Eukaryota, 2.00 Å** In complex with alpha-methyl-4-biphenyl acetic acid.	1Q4G	Data File Jmol Viewer	Gupta et al. (2004). Gupta K, Selinsky BS, Kaub CJ, Katz AK, & Loll PJ (2004). The 2.0 Å resolution crystal structure of prostaglandin H2 synthase-1: structural insights into an unusual peroxidase. J Mol Biol 335 :503-518. PubMed Id: 14672659.
*Ram Prostaglandin H2 synthase-1 (COX-1): Ovis aries* E Eukaryota, 2.00 Å** In complex with flurbiprofen + Mn(III) PPIX cofactor.	2AYL	Data File Jmol Viewer	Gupta et al. (2006). Gupta K, Selinsky BS, & Loll PJ (2006). 2.0 angstroms structure of prostaglandin H2 synthase-1 reconstituted with a manganese porphyrin cofactor. Acta Crystallogr D Biol Crystallogr 62 :151-156. PubMed Id: 16421446.
*Ram Prostaglandin H2 synthase-1 (COX-1): Ovis aries* E Eukaryota (expressed in Spodoptera frugiperda), 3.05 Å** 3N8V is the unoccupied structure. R120Q/Native Heterodimer mutant in complex with Flurbiprofen, 2.75 Å: 3N8W COX-1 in complex with Nimesulide, 2.75 Å: 3N8X Aspirin Acetylated COX-1 in Complex with Diclofenac, 2.60 Å: 3N8Y COX-1 in Complex with Flurbiprofen, 2.90 Å: 3N8Z	3N8V	Data File Jmol Viewer	Sidhu et al. (2010). Sidhu RS, Lee JY, Yuan C, & Smith WL (2010). Comparison of Cyclooxygenase-1 Crystal Structures: Cross-Talk between Monomers Comprising Cyclooxygenase-1 Homodimers. Biochemistry 49 :7069-7079. PubMed Id: 20669977.
*Ram Prostaglandin H2 synthase-1 (COX-1) in complex with the subtype-selective derivative 2a: Ovis aries* E Eukaryota (expressed in Spodoptera frugiperda), 3.35 Å**	7JXT	Data File Jmol Viewer	Friedrich et al. (2021). Friedrich L, Cingolani G, Ko YH, Iaselli M, Miciaccia M, Perrone MG, Neukirch K, Bobinger V, Merk D, Hofstetter RK, Werz O, Koeberle A, Scilimati A, & Schneider G (2021). Learning from Nature: From a Marine Natural Product to Synthetic Cyclooxygenase-1 Inhibitors by Automated De Novo Design. Adv Sci (Weinh) 8 16:2100832. PubMed Id: 34176236. doi:10.1002/advs.202100832.
*Prostaglandin H2 synthase-1 (cyclooxygenase-1 or COX-1): Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.36 Å**	6Y3C	Data File Jmol Viewer	Miciaccia et al. (2021). Miciaccia M, Belviso BD, Iaselli M, Cingolani G, Ferorelli S, Cappellari M, Loguercio Polosa P, Perrone MG, Caliandro R, & Scilimati A (2021). Three-dimensional structure of human cyclooxygenase (hCOX)-1. Sci Rep 11 1:4312. PubMed Id: 33619313. doi:10.1038/s41598-021-83438-z.
*Cyclooxygenase-2: Mus musculus* E Eukaryota, 3.0 Å**	1CX2	Data File Jmol Viewer prostaglandin synthase-2 (COX-2)	Kurumbail et al. (1996). Kurumbail RG, Stevens AM, Gierse JK, McDonald JJ, Stegeman RA, Pak JY, Gildehaus D, Miyashiro JM, Penning TD, Seibert, K et al (1996). Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents. Nature 384 :644-648. PubMed Id: 8967954.
*Cyclooxygenase-2 with bound indomethacin-ethylenediamine-dansyl conjugate: Mus musculus* E Eukaryota (expressed in S. frugiperda), 2.22 Å** with bound indomethacin-butyldiamine-dansyl conjugate, 2.22 Å: 6BL3	6BL4	Data File Jmol Viewer	Xu et al. (2019). Xu S, Uddin MJ, Banerjee S, Duggan K, Musee J, Kiefer JR, Ghebreselasie K, Rouzer CA, & Marnett LJ (2019). Fluorescent indomethacin-dansyl conjugates utilize the membrane-binding domain of cyclooxygenase-2 to block the opening to the active site. J Biol Chem 294 22:8690-8698. PubMed Id: 31000626. doi:10.1074/jbc.RA119.007405.
*Fatty acid α-dioxygenase (α-DOX): Arabidopsis thaliana* E Eukaryota (expressed in E. coli), 1.70 Å** First structure of a member of the α-DOX subfamily of cyclooxygenase-peroxidase family of heme-containing proteins. With bound imidazole, 1.51 Å: 4HHR	4HHS	Data File Jmol Viewer	Goulah et al. (2013). Goulah CC, Zhu G, Koszelak-Rosenblum M, & Malkowski MG (2013). The Crystal Structure of α-Dioxygenase Provides Insight into Diversity in the Cyclooxygenase-Peroxidase Superfamily. Biochemistry 52 :1364-1372. PubMed Id: 23373518. doi:10.1021/bi400013k.
Lipoxygenases Related to Cyclooxygenases Rather than being tethered by α-helices at the interface, they are tethered by N-terminal β-sheet C2-like domains
*Arachidonic acid 15-lipoxygenase from soybeans: Glycine max* E Eukaryota, 2.60 Å**	2SBL	Data File Jmol Viewer	Boyington et al. (1993). Boyington JC, Gaffney BJ, & Amzel LM (1993). The three-dimensional structure of an arachidonic acid 15-lipoxygenase. Science 260 5113:1482-1486. PubMed Id: 8502991. doi:10.1126/science.8502991.
*Lipoxygenase-L1 from soybeans: Glycine max* E Eukaryota, 1.40 Å**	1YGE	Data File Jmol Viewer	Minor et al. (1996). Minor W, Steczko J, Stec B, Otwinowski Z, Bolin JT, Walter R, & Axelrod B (1996). Crystal structure of soybean lipoxygenase L-1 at 1.4 A resolution. Biochemistry 35 33:10687-10701. PubMed Id: 8718858. doi:10.1021/bi960576u.
*Lipoxygenase-L3 from soybeans: Glycine max* E Eukaryota, 2.60 Å**	1LNH	Data File Jmol Viewer	Skrzypczak-Jankun et al. (1997). Skrzypczak-Jankun E, Amzel LM, Kroa BA, & Funk MO Jr (1997). Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme. Proteins 29 1:15-31. PubMed Id: 9294864. doi:10.1002/(SICI)1097-0134(199709)29:1.
*8R-Lipoxygenase from coral: Plexaura homomalla* E Eukaryota (expressed in E. coli), 3.20 Å** 2FNQ supersedes 1ZQ4	2FNQ	Data File Jmol Viewer	Oldham et al. (2005). Oldham ML, Brash AR, & Newcomer ME (2005). Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via a C2-like domain and a structural basis of product chirality. J Biol Chem 280 47:39545-39552. PubMed Id: 16162493. doi:10.1074/jbc.M506675200.
*8R-Lipoxygenase from coral. Δ413-417 I805A mutant: Plexaura homomalla* E Eukaryota (expressed in E. coli), 1.85 Å**	3FG4	Data File Jmol Viewer	Neau et al. (2009). Neau DB, Gilbert NC, Bartlett SG, Boeglin W, Brash AR, & Newcomer ME (2009). The 1.85 A structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity. Biochemistry 48 33:7906-7915. PubMed Id: 19594169. doi:10.1021/bi900084m.
*15-Lipoxygenase from rabbit reticulocytes: Oryctolagus cuniculus* E Eukaryota, 2.40 Å**	1LOX	Data File Jmol Viewer	Gillmor et al. (1997). Gillmor SA, Villaseñor A, Fletterick R, Sigal E, & Browner MF (1997). The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity. Nat Struct Mol Biol 4 12:1003-1009. PubMed Id: 9406550. doi:10.1038/nsb1297-1003 .
*5-Lipoxygenase: Homo sapiens* E Eukaryota (expressed in E. coli), 2.39 Å**	3O8Y	Data File Jmol Viewer	Gilbert et al. (2011). Gilbert NC, Bartlett SG, Waight MT, Neau DB, Boeglin WE, Brash AR, & Newcomer ME (2011). The structure of human 5-lipoxygenase. Science 331 :217-219. PubMed Id: 21233389. doi:10.1126/science.1197203.
*15-Lipoxygenase-2 (15-LOX-2) with substrate mimic: Homo sapiens* E Eukaryota (expressed in E. coli), 2.63 Å**	4NRE	Data File Jmol Viewer	Kobe et al. (2014). Kobe MJ, Neau DB, Mitchell CE, Bartlett SG, & Newcomer ME (2014). The structure of human 15-lipoxygenase-2 with a substrate mimic. J Biol Chem 289 :8562-8569. PubMed Id: 24497644. doi:10.1074/jbc.M113.543777.
Squalene-Hopene Cyclases
*Squalene-hopene cyclase: Alicyclobacillus acidocaldarius* B Bacteria, 2.0 Å** 2SQC is space group P4₃2₁2. 3SQC, 2.8 Å is P3₂21.	2SQC	Data File Jmol Viewer squalene-hopene cyclase	Wendt et al. (1999). Wendt KU, Lenhart A, & Schulz GE (1999). The structure of the membrane protein squalene-hopene cyclase at 2.0 Å resolution. J. Mol. Biol. 286 :175-187. PubMed Id: 9931258.
Oxidases
*Monoamine Oxidase B: Homo sapiens (Human) mitochondrial outer membrane* E Eukaryota (expressed in Pichia pastoris), 3.0 Å** NOTE: MAOB has a single transmembrane helix that anchors it to the outer membrane (residues 489-515). Nevertheless, we consider it monotopic because the bulk of the 520-residue protein, including the active site, is not located within the membrane core.	1GOS	Data File Jmol Viewer Monoamine oxidase B	Binda et al. (2002). Binda C, Newton-Vinson P, Hubálek F, Edmondson DE, & Mattevi A (2002). Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nature Struct Biol 9 :22-26. PubMed Id: 11753429.
*Monoamine Oxidase B with bound Isatin: Homo sapiens (Human) mitochondrial outer membrane* E Eukaryota (expressed in Pichia pastoris), 1.70 Å** with bound Tranylcypromine, 2.20 Å: 1OJB with bound N-(2-aminoethyl)-p-chlorobenamide, 2.40 Å: 1OJC with bound Lauryldimethyl-amine N-Oxide, 3.10 Å: 1OJD with bound 1.4-Diphenyl-2-butene, 2.30 Å: 1OJ9	1OJA	Data File Jmol Viewer	Binda et al. (2003). Binda C, Li M, Hubálek F, Restelli N, Edmondson DE, & Mattevi A (2003). Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures. Proc Natl Acad Sci USA 100 :9750-9755. PubMed Id: 12913124.
*Monoamine Oxidase A: Rattus norvegicus (Rat) mitochondrial outer membrane* E Eukaryota (expressed in S. cerevisiae), 3.20 Å**	1O5W	Data File Jmol Viewer	Ma et al. (2004). Ma J, Yoshimura M, Yamashita E, Nakagawa A, Ito A, & Tsukihara T (2004). Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors. J Mol Biol 338 :103-114. PubMed Id: 15050826.
*Monoamine Oxidase A with bound Clorglycine: Homo sapiens (Human) mitochondrial outer membrane* E Eukaryota (expressed in Pichia pastoris), 3.00 Å** crystal form B, 3.15 Å: 2BXS Monoamine Oxidase B with bound Deprenyl, 2.20 Å: 2BYB	2BXR	Data File Jmol Viewer	De Colibus et al. (2005). De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, & Mattevi A (2005). Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc Natl Acad Sci USA 102 :12684-12689. PubMed Id: 16129825.
*Monoamine Oxidase A with bound Harmine: Homo sapiens (Human) mitochondrial outer membrane* E Eukaryota (expressed in S. cerevisiae), 2.20 Å** G110A mutant with bound Harmine, 2.17 Å: 2Z5Y	2Z5X	Data File Jmol Viewer	Son et al. (2008). Son SY, Ma J, Kondou Y, Yoshimura M, Yamashita E, & Tsukihara T (2008). Structure of human monoamine oxidase A at 2.2-Å resolution: The control of opening the entry for substrates/inhibitors. Proc Natl Acad Sci USA 105 :5739-5744. PubMed Id: 18391214.
*Alternative oxidase (AOX), cyanide-insensitive: Trypanosoma brucei brucei* E Eukaryota (expressed in E. coli), 2.85 Å** with ascofuranone derivative, 2.59 Å: 3VVA with colletochlorin B, 2.30 Å: 3W54	3VV9	Data File Jmol Viewer	Shiba et al. (2013). Shiba T, Kido Y, Sakamoto K, Inaoka DK, Tsuge C, Tatsumi R, Takahashi G, Balogun EO, Nara T, Aoki T, Honma T, Tanaka A, Inoue M, Matsuoka S, Saimoto H, Moore AL, Harada S, & Kita K (2013). Structure of the trypanosome cyanide-insensitive alternative oxidase. Proc Natl Acad Sci USA 110 :4580-4585. PubMed Id: 23487766. doi:10.1073/pnas.1218386110.
Hydrolases
*Fatty acid amide hydrolase: Rattus norvegicus* E Eukaryota, 2.8 Å** NOTE: Like MAO, FAAH has a single TM segment. But the active site is external to the membrane, and many other residues on the protein surface contribute to membrane binding. Absence of the TM segment affects neither membrane association or function.	1MT5	Data File Jmol Viewer fatty acid amide hydrolase	Bracey et al. (2002). Bracey MH, Hanson MA, Masuda KR, Stevens RC, & Cravatt BF (2002). Structural adaptations in a membrane enzyme that terminates endo cannabinoid signaling. Science 298 :1793-1796. PubMed Id: 12459591.
*LpxH pyrophosphohydrase with bound lipid X & Mn²⁺: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 1.65 Å** complex with lipid X, P21 form, 1.72 Å: 5B4A complex with lipid X, C2 form, 1.6 Å: 5B4B H10N mutant in complex with Mn²⁺, 1.96 Å: 5B4C H10N mutant, 1.75 Å: 5B4D	5B49	Data File Jmol Viewer	Okada et al. (2016). Okada C, Wakabayashi H, Kobayashi M, Shinoda A, Tanaka I, & Yao M (2016). Crystal structures of the UDP-diacylglucosamine pyrophosphohydrase LpxH from Pseudomonas aeruginosa. Sci Rep 6 :32822. PubMed Id: 27609419. doi:10.1038/srep32822.
*LpxI phosphodiester hydrolase for lipid A biosynthesis: Caulobacter crescentus* B Bacteria (expressed in E. coli), 2.90 Å** D225A mutant, 2.52 Å: 4GGI	4GGM	Data File Jmol Viewer	Metzger et al. (2012). Metzger LE 4th, Lee JK, Finer-Moore JS, Raetz CR, & Stroud RM (2012). LpxI structures reveal how a lipid A precursor is synthesized. Nature Struc Mol Biol 19 :1132-1138. PubMed Id: 23042606. doi:10.1038/nsmb.2393.
*LpxK, the 4'-kinase of lipid A biosynthesis: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.30 Å** Apo LpxK, 1.90 Å: 4EHX ADP/Mg²⁺ LpxK, 2.20 Å: 4EHY	4EHW	Data File Jmol Viewer	Emptage et al. (2012). Emptage RP, Daughtry KD, Pemble CW 4th, & Raetz CR (2012). Crystal structure of LpxK, the 4'-kinase of lipid A biosynthesis and atypical P-loop kinase functioning at the membrane interface. Proc Natl Acad Sci USA 109 :12956-12961. PubMed Id: 22826246. doi:10.1073/pnas.1206072109.
*N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: Homo sapiens* E Eukaryota (expressed in E. coli), 2.65 Å**	4QN9	Data File Jmol Viewer	Magotti et al. (2015). Magotti P, Bauer I, Igarashi M, Babagoli M, Marotta R, Piomelli D, & Garau G (2015). Structure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of Fatty Acid ethanolamide biosynthesis by bile acids. Structure 23 3:598-604. PubMed Id: 25684574. doi:10.1016/j.str.2014.12.018.
*PulA pullulanase: Klebsiella oxytoca* B Bacteria (expressed in E. coli), 2.88 Å**	2YOC	Data File Jmol Viewer	East et al. (2016). East A, Mechaly AE, Huysmans GH, Bernarde C, Tello-Manigne D, Nadeau N, Pugsley AP, Buschiazzo A, Alzari PM, Bond PJ, & Francetic O (2016). Structural Basis of Pullulanase Membrane Binding and Secretion Revealed by X-Ray Crystallography, Molecular Dynamics and Biochemical Analysis. Structure 24 :92-104. PubMed Id: 26688215. doi:10.1016/j.str.2015.10.023.
*C2 domain of cytosolic phospholipase A₂α bound to phosphatidylcholine: Gallus gallus* E Eukaryota (expressed in E. coli), 2.21 Å**	6IEJ	Data File Jmol Viewer	Hirano et al. (2019). Hirano Y, Gao YG, Stephenson DJ, Vu NT, Malinina L, Simanshu DK, Chalfant CE, Patel DJ, & Brown RE (2019). Structural basis of phosphatidylcholine recognition by the C2-domain of cytosolic phospholipase A₂α. Elife 8 :e44760. PubMed Id: 31050338. doi:10.7554/eLife.44760.
*PlaF phospholipase A bacterial virulence factor: Pseudomonas aeruginosa* B Bacteria, 2.00 Å**	6I8W	Data File Jmol Viewer	Bleffert et al. (2022). Bleffert F, Granzin J, Caliskan M, Schott-Verdugo SN, Siebers M, Thiele B, Rahme L, Felgner S, Dörmann P, Gohlke H, Batra-Safferling R, Jaeger KE, & Kovacic F (2022). Structural, mechanistic, and physiological insights into phospholipase A-mediated membrane phospholipid degradation in Pseudomonas aeruginosa. Elife 11 :e72824. PubMed Id: 35536643. doi:10.7554/eLife.72824.
*Phospholipase Cβ3, in complex with Gγβ on lipid nanodiscs: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.30 Å** cryo-EM structure on liposomes, 3.50 Å: 8EMW in solution, 3.60 Å: 8EMV	8EMX	Data File Jmol Viewer	Falzone & MacKinnon (2023). Falzone ME, & MacKinnon R (2023). Gβγ activates PIP2 hydrolysis by recruiting and orienting PLCβ on the membrane surface. Proc Natl Acad Sci U S A 120 20:e2301121120. PubMed Id: 37172014. doi:10.1073/pnas.2301121120.
Hydroxylases
*Kdo hydroxylase KdoO, apo protein: Methylacidiphilum infernorum* B Bacteria (expressed in E. coli), 1.94 Å** in complex with cobalt(II), 1.45 Å: 5YKA in complex with alphaketoglutarate and Fe(III), 1.6 Å: 5YVZ in complex with succinate and Fe(III), 1.49 Å: 5YW0	6A2E	Data File Jmol Viewer	Joo et al. (2018). Joo SH, Pemble CW 4th, Yang EG, Raetz CRH, & Chung HS (2018). Biochemical and Structural Insights into an Fe(II)/α-Ketoglutarate/O₂-Dependent Dioxygenase, Kdo 3-Hydroxylase (KdoO). J Mol Biol 430 21:4036-4048. PubMed Id: 30092253. doi:10.1016/j.jmb.2018.07.029.
Acyltransferases
*LpxM lipid A acyltransferase: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 1.99 Å** The protein is anchored at the membrane interface by a single TM helix. E127A catalytic residue mutant, 1.9 Å: 5KNK	5KN7	Data File Jmol Viewer	Dovala et al. (2016). Dovala D, Rath CM, Hu Q, Sawyer WS, Shia S, Elling RA, Knapp MS, & Metzger LE 4th (2016). Structure-guided enzymology of the lipid A acyltransferase LpxM reveals a dual activity mechanism. Proc Natl Acad Sci USA 113 :E6064-E6071. PubMed Id: 27681620. doi:10.1073/pnas.1610746113.
*PatA membrane-associated acyltransferase, unliganded: Mycolicibacterium smegmatis* B Bacteria, 3.67 Å**	7OJT	Data File Jmol Viewer	Anso et al. (2021). Anso I, Basso LGM, Wang L, Marina A, Páez-Pérez ED, Jäger C, Gavotto F, Tersa M, Perrone S, Contreras FX, Prandi J, Gilleron M, Linster CL, Corzana F, Lowary TL, Trastoy B, & Guerin ME (2021). Molecular ruler mechanism and interfacial catalysis of the integral membrane acyltransferase PatA. Sci Adv 7 42:eabj4565. PubMed Id: 34652941. doi:10.1126/sciadv.abj4565.
Thioesterases
*acyl protein thioesterase 1 (APT 1) bound to palmitic acid: Homo sapiens* E Eukaryota (expressed in E. coli), 2.75 Å** C2S mutant bound to palmitic acid, 2.60 Å: 6QGQ S119A mutant bound to palmitic acid, 2.60 Å: 6QGO bound to 2-Bromopalmitate, 2.10 Å: 6QGN	6QGS	Data File Jmol Viewer	Abrami et al. (2021). Abrami L, Audagnotto M, Ho S, Marcaida MJ, Mesquita FS, Anwar MU, Sandoz PA, Fonti G, Pojer F, Dal Peraro M, & van der Goot FG (2021). Palmitoylated acyl protein thioesterase APT2 deforms membranes to extract substrate acyl chains. Nat Chem Biol 17 4:438-447. PubMed Id: 33707782. doi:10.1038/s41589-021-00753-2.
Nucleotidyltransferases
*Tam41 mitochondrial CDP-DAG synthase Δ74: Schizosaccharomyces pombe* E Eukaryota (expressed in E. coli), 2.26 Å** F240A mutant, 2.88 Å: 6IG2	6IG4	Data File Jmol Viewer	Jiao et al. (2019). Jiao H, Yin Y, & Liu Z (2019). Structures of the Mitochondrial CDP-DAG Synthase Tam41 Suggest a Potential Lipid Substrate Pathway from Membrane to the Active Site. Structure 27 8:1258-1269.e4. PubMed Id: 31178220. doi:10.1016/j.str.2019.04.017.
Oxidoreductases (Monotopic)
*Sulfide:quinone oxidoreductase in complex with decylubiquinone: Aquifex aeolicus* B Bacteria, 2.0 Å** "as-purified" protein, 2.30 Å: 3HYV in complex with aurachin C, 2.9 Å: 3HYX This monotopic membrane protein is thought to be buried about 12 Å in the bilayer interface. Listed under TRANSMEMBRANE PROTEINS: ALPHA-HELICAL : Oxidoreductases, MONOTOPIC MEMBRANE PROTEINS : Oxidoreductases (Monotopic).	3HYW	Data File Jmol Viewer	Marcia et al. (2009). Marcia M, Ermler U, Peng G, & Michel H (2009). The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proc Natl Acad Sci USA 106 :9625-9630. PubMed Id: 19487671.
*Sulfide:quinone oxidoreductase, selenomethionine-substituted: Homo sapiens* E Eukaryota (expressed in e. coli), 2.59 Å** native protein, 2.99 Å: 6MP5	6MO6	Data File Jmol Viewer	Jackson et al. (2019). Jackson MR, Loll PJ, & Jorns MS (2019). X-Ray Structure of Human Sulfide:Quinone Oxidoreductase: Insights into the Mechanism of Mitochondrial Hydrogen Sulfide Oxidation. Structure 27 5:794-805.e4. PubMed Id: 30905673. doi:10.1016/j.str.2019.03.002.
*Electron Transfer Flavoprotein-ubiquinone oxidoreductase (ETF-QO) with bound UQ: Sus scrofa* E Eukaryota, 2.5 Å** UQ-free structure, 2.6 Å: 2GMJ. Because this is a mitochondrial respiratory chain protein, it is listed under TRANSMEMBRANE PROTEINS: ALPHA-HELICAL : Oxidoreductases and MONOTOPIC MEMBRANE PROTEINS : Oxidoreductases (Monotopic).	2GMH	Data File Jmol Viewer	Zhang et al. (2006). Zhang J, Frerman FE, & Kim J-JP (2006). Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool. Proc Natl Acad Sci U S A 103 :16212-16217. PubMed Id: 17050691.
*mitochondrial trifunctional protein: Homo sapiens* E Eukaryota (expressed in E. coli), 3.6 Å**	6DV2	Data File Jmol Viewer	Xia et al. (2019). Xia C, Fu Z, Battaile KP, & Kim JP (2019). Crystal structure of human mitochondrial trifunctional protein, a fatty acid β-oxidation metabolon. Proc Natl Acad Sci USA 116 13:6069-6074. PubMed Id: 30850536. doi:10.1073/pnas.1816317116.
*Electron bifurcating flavoprotein Fix/EtfABCX: Thermotoga maritima* B Bacteria (expressed in Pyrococcus furiosus), 2.90 Å** cryo-EM structure	7KOE	Data File Jmol Viewer	Feng et al. (2021). Feng X, Schut GJ, Lipscomb GL, Li H, & Adams MWW (2021). Cryoelectron microscopy structure and mechanism of the membrane-associated electron-bifurcating flavoprotein Fix/EtfABCX. Proc Natl Acad Sci U S A 118 2:e2016978118. PubMed Id: 33372143. doi:10.1073/pnas.2016978118.
Dehydrogenases
*Glycerol-3-phosphate dehydrogenase (GlpD, native): Escherichia coli* B Bacteria, 1.75 Å** SeMet-GlpD, 1.95 Å: 2R4J GlpD-2-PGA, 2.3 Å: 2R45 GlpD-PEP, 2.1 Å: 2R46 GlpD-DHAP, 2.1 Å: 2R4E Listed under MONOTOPIC MEMBRANE PROTEINS : Dehydrogenases, TRANSMEMBRANE PROTEINS: ALPHA-HELICAL : Oxidoreductases.	2QCU	Data File Jmol Viewer	Yeh et al. (2008). Yeh JI, Chinte U, & Du S (2008). Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism. Proc. Natl. Acad. Sci. USA 105 :3280-3285. PubMed Id: 18296637.
*PutA proline utilization protein: Geobacter sulfurreducens* B Bacteria (expressed in E. coli), 1.90 Å** in complex with L-tetrahydro-2-furoic acid, 2.10 Å: 4NMA in complex with L-lactate, 2.2 Å: 4NMB in complex with Zwittergent 3-12, 1.90 Å: 4NMC reduced with dithionite, 1.98 Å: 4NMD inactivated by N-propargylglycine, 2.09 Å: 4NME inactivated by N-propargylglycine and complexed with menadione bisulfite, 1.95 Å: 4NMF	4NM9	Data File Jmol Viewer	Singh et al. (2014). Singh H, Arentson BW, Becker DF, & Tanner JJ (2014). Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site. Proc Natl Acad Sci USA 111 :3389-3394. PubMed Id: 24550478. doi:10.1073/pnas.1321621111.
*Ndi1 NADH Dehydrogenase: Saccharomyces cerevisiae* E Eukaryota, 2.70 Å** Ndi1-NAD⁺ complex, 2.90 Å: 4GAP Ndi1-UQ2 complex, 3.00 Å: 4GAV	4G9K	Data File Jmol Viewer	Iwata et al. (2012). Iwata M, Lee Y, Yamashita T, Yagi T, Iwata S, Cameron AD, & Maher MJ (2012). The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates. Proc Natl Acad Sci USA 109 :15247-15252. PubMed Id: 22949654. doi:10.1073/pnas.1210059109 .
*Ndi1 NADH Dehydrogenase, apo form: Saccharomyces cerevisiae* E Eukaryota (expressed in E. coli), 2.39 Å** with NADH, 2.26 Å: 4G6H with Quinone, 2.48 Å: 4G74 with NAH and Quinone, 2.52 Å: 4G73	4G6G	Data File Jmol Viewer	Feng et al. (2012). Feng Y, Li W, Li J, Wang J, Ge J, Xu D, Liu Y, Wu K, Zeng Q, Wu JW, Tian C, Zhou B, & Yang M (2012). Structural insight into the type-II mitochondrial NADH dehydrogenases. Nature 491 :478-482. PubMed Id: 23086143. doi:10.1038/nature11541.
*NDH-2 NADH dehydrogenase: Caldalkalibacillus thermarum* B Bacteria (expressed in E. coli), 2.50 Å** NDH-2 is a non-proton pumping dehydrogenase.	4NWZ	Data File Jmol Viewer	Heikal et al. (2014). Heikal A, Nakatani Y, Dunn E, Weimar MR, Day CL, Baker EN, Lott JS, Sazanov LA, & Cook GM (2014). Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation. Mol Microbiol 91 5:950-964. PubMed Id: 24444429. doi:10.1111/mmi.12507.
*(S)-Mandelate dehydrogenase (MDH): Pseudomonas putida* B Bacteria (expressed in E. coli), 2.2 Å**	6BFG	Data File Jmol Viewer	Sukumar et al. (2018). Sukumar N, Liu S, Li W, Mathews FS, Mitra B, & Kandavelu P (2018). Structure of the monotopic membrane protein (S)-mandelate dehydrogenase at 2.2Å resolution. Biochimie 154 :45-54. PubMed Id: 30071260. doi:10.1016/j.biochi.2018.07.017.
Decarboxylases (Monotopic)
*phosphatidylserine decarboxylase (PSD), apo-form: Escherichia coli* B Bacteria, 2.60 Å** PE-bond form, 3.60 Å: 6L07	6L06	Data File Jmol Viewer	Watanabe et al. (2020). Watanabe Y, Watanabe Y, & Watanabe S (2020). Structural Basis for Phosphatidylethanolamine Biosynthesis by Bacterial Phosphatidylserine Decarboxylase. Structure 28 7:799-809.e5. PubMed Id: 32402247. doi:10.1016/j.str.2020.04.006.
*phosphatidylserine decarboxylase (PSD) apo form: Escherichia coli* B Bacteria, 1.90 Å** apo form, 2.63 Å: 7CNX with 8PE bound, 2.12 Å: 7CNY with 10PE bound, 2.70 Å: 7CNZ	7CNW	Data File Jmol Viewer	Cho et al. (2021). Cho G, Lee E, & Kim J (2021). Structural insights into phosphatidylethanolamine formation in bacterial membrane biogenesis. Sci Rep 11 1:5785. PubMed Id: 33707636. doi:10.1038/s41598-021-85195-5.
Glycosyltransferases
*Peptidoglycan Glycosyltransferase: Staphylococcus aureus* B Bacteria, 2.8 Å** NOTE: The enzyme has a single TM segment, which is absent in the structure. The active site is external to the membrane, but the so-called Jaw Region contributes to membrane binding. 2OLV shows the enzyme complexed with moenomycin. 2OLU is the structure of the apoenzyme.	2OLV	Data File Jmol Viewer	Lovering et al. (2007). Lovering AL, de Castro LH, Lim D, & Strynadka NCJ (2007). Structural insight into the transglycosylation step in bacterial cell-wall biosynthesis. Science 315 :1402-1405. PubMed Id: 17347437.
*Peptidoglycan Glycosyltransferase penicillin-binding protein 1a (PBP1a): Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.1 Å** NOTE: The enzyme has a single TM segment, which is absent in the structure. The active site is external to the membrane.	2OQO	Data File Jmol Viewer	Yuan et al. (2007). Yuan Y, Barrett D, Zhang Y, Kahne D, Sliz P, & Walker S. (2007). Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis. Proc Natl Acad Sci USA 104 :5348-5353. PubMed Id: 17360321.
*Peptidoglycan Glycosyltransferase penicillin-binding protein 1b (PBP1b): Escherichia coli* B Bacteria, 2.16 Å** 3VMA supersedes the original PDB entry 3FWM. NOTE: The single TM segment is present in this structure. The active site is external to the membrane. SeMet Protein, 3.09 Å: 3FWL	3VMA	Data File Jmol Viewer	Sung et al. (2009). Sung MT, Lai YT, Huang CY, Chou LY, Shih HW, Cheng WC, Wong CH, & Ma C (2009). Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli. Proc Natl Acad Sci USA 106 :8824-8829. PubMed Id: 19458048.
*Peptidoglycan Glycosyltransferase penicillin-binding protein 1b (PBP1b): Escherichia coli* B Bacteria, 3.28 Å** cryo-EM structure	7LQ6	Data File Jmol Viewer	Caveney et al. (2021). Caveney NA, Workman SD, Yan R, Atkinson CE, Yu Z, & Strynadka NCJ (2021). CryoEM structure of the antibacterial target PBP1b at 3.3 Å resolution. Nat Commun 12 1:2775. PubMed Id: 33986273. doi:10.1038/s41467-021-23063-6.
*Monofunctional glycosyltransferase WaaA, substrate free: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.00 Å** WaaA catalyzes the transfer of Kdo to the lipid A precursor of lipopolysaccharide. Structure with substrate, 2.42 Å: 2XCU	2XCI	Data File Jmol Viewer	Schmidt et al. (2012). Schmidt H, Hansen G, Singh S, Hanuszkiewicz A, Lindner B, Fukase K, Woodard RW, Holst O, Hilgenfeld R, Mamat U, & Mesters JR (2012). Structural and mechanistic analysis of the membrane-embedded glycosyltransferase WaaA required for lipopolysaccharide synthesis. Proc Natl Acad Sci USA 109 :6253-6258. PubMed Id: 22474366. doi:10.1073/pnas.1119894109.
*Monofunctional glycosyltransferase in complex with Lipid II analog: Staphylococcus aureus* B Bacteria (expressed in E. coli), 2.30 Å** NOTE: The single TM segment is present in this structure. The active site is external to the membrane. Substrate-free protein, 2.52 Å: 3VMQ In complex with moenomycin, 3.69 Å: 3VMR In complex with NBD-Lipid II, 3.20 Å: 3VMS	3VMT	Data File Jmol Viewer	Huang et al. (2012). Huang CY, Shih HW, Lin LY, Tien YW, Cheng TJ, Cheng WC, Wong CH, & Ma C (2012). Crystal structure of Staphylococcus aureus transglycosylase in complex with a lipid II analog and elucidation of peptidoglycan synthesis mechanism. Proc Natl Acad Sci USA 109 :6496-6501. PubMed Id: 22493270. doi:10.1073/pnas.1203900109.
*PglH glycosyltransferase in complex with UDP-galNAc: Campylobacter jejuni* B Bacteria (expressed in E. coli), 2.3 Å** in complex w. UDP & synthetic LLO, 2.7 Å: 6EJJ in complex with UDP-CH₂-GalNAc, 3.3 Å: 6EJK	6EJI	Data File Jmol Viewer	Ramírez et al. (2018). Ramírez AS, Boilevin J, Mehdipour AR, Hummer G, Darbre T, Reymond JL, & Locher KP (2018). Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase. Nat Commun 9 1:445. PubMed Id: 29386647. doi:10.1038/s41467-018-02880-2.
GPI-Anchored Cell-Wall Proteins (GPI-CWPs) GPIs are glycosylphophatidylinositol anchors that are post-translational modifications in eukaryotes
*Dfg5 GH76 protein: Chaetomium thermophilum* E Eukaryota (expressed in E. coli), 1.05 Å** in complex with mannose, 1.30 Å: 6RY1 in complex with alpha-1,2-mannobiose, 1.30 Å: 6RY2 in complex with alpha-1,6-mannobiose, 1.30 Å: 6RY5 in complex with glucosamine, 1.30 Å: 6RY6 in complex with laminaribiose, 1.30 Å: 6RY7	6RY0	Data File Jmol Viewer	Vogt et al. (2020). Vogt MS, Schmitz GF, Varón Silva D, Mösch HU, & Essen LO (2020). Structural base for the transfer of GPI-anchored glycoproteins into fungal cell walls. Proc Natl Acad Sci USA 117 36:22061-22067. PubMed Id: 32839341. doi:10.1073/pnas.2010661117.
Phosphoglycosyl Transferases (PGT) These proteins catalyze the first membrane-committed step of glycoconjugates
*PglC phosphoglycosyl transferase, I57M/Q175M variant: Campylobacter concisus* B Bacteria (expressed in E. coli), 2.74 Å**	5W7L	Data File Jmol Viewer	Ray et al. (2018). Ray LC, Das D, Entova S, Lukose V, Lynch AJ, Imperiali B, & Allen KN (2018). Membrane association of monotopic phosphoglycosyl transferase underpins function. Nat Chem Biol 14 :538-541. PubMed Id: 29769739. doi:10.1038/s41589-018-0054-z.
Peptidases
*LepB Signal Peptidase (SPase) in complex with a β-lactam inhibitor: Escherichia coli* B Bacteria, 1.9 Å** Located in the periplasmic space, the SPase has two transmembrane segments (AAs 4-28 & 58-76), which are missing in this structure. The Ser-Lys catalytic site is part of a hydrophobic surface that interacts strongly with the membrane.	1B12	Data File Jmol Viewer	Paetzel et al. (1998). Paetzel M, Dalbey RE, & Strynadka NC (1998). Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor. Nature 396 :186-190. PubMed Id: 9823901.
*LepB Signal Peptidase (SPase), apoprotein: Escherichia coli* B Bacteria, 2.40 Å** Δ2-75 protein lacking the two transmembrane helices	1KN9	Data File Jmol Viewer	Paetzel et al. (2002). Paetzel M, Dalbey RE, & Strynadka NC (2002). Crystal structure of a bacterial signal peptidase apoenzyme J Biol Chem 277 :9512-9519. PubMed Id: 11741964.
*LepB Signal Peptidase (SPase) in complex with a lipopeptide inhibitor: Escherichia coli* B Bacteria, 2.47 Å** This structure of the Δ2-75 protein reveals the likely position of the signal peptide in the active site.	1T7D	Data File Jmol Viewer	Paetzel et al. (2004). Paetzel M, Goodall JJ, Kania M, Dalbey RE, & Page MG (2004). Crystallographic and biophysical analysis of a bacterial signal peptidase in complex with a lipopeptide-based inhibitor. J Biol Chem 279 :30781-30790. PubMed Id: 15136583.
*SpsB Signal Peptidase (SPase), apoprotein: Staphylococcus aureus* B Bacteria (expressed in E. coli), 2.05 Å** in complex with peptide 1, 2.10 Å: 4WVH in complex with peptide 2, 1.90 Å: 4WVI in complex with peptide 3, 1.95 Å: 4WVJ	4WVG	Data File Jmol Viewer	Ting et al. (2016). Ting YT, Harris PW, Batot G, Brimble MA, Baker EN, & Young PG (2016). Peptide binding to a bacterial signal peptidase visualized by peptide tethering and carrier-driven crystallization. IUCrJ 3 :10-19. PubMed Id: 26870377. doi:10.1107/S2052252515019971.
*Signal Peptide Peptidase (SppA), native protein: Escherichia coli* B Bacteria, 2.55 Å** SeMet protein, 2.76 Å: 3BEZ. Long thought to be a transmembrane protein, the structure reveals a peripheral homotetramer that likely is buried in the membrane interface. Each monomer has a putative N-terminal transmembrane helix for anchoring to the membrane. This anchor was removed for crystallization. Listed under TRANSMEMBRANE PROTEINS: ALPHA-HELICAL : Intramembrane Proteases, MONOTOPIC MEMBRANE PROTEINS : Peptidases.	3BF0	Data File Jmol Viewer	Kim et al. (2008). Kim AC, Oliver DC, & Paetzel M (2008). Crystal structure of a bacterial signal Peptide peptidase. J Mol Biol 376 :352-366. PubMed Id: 18164727.
*Signal Peptide Peptidase (SppA): Bacillus subtilis* B Bacteria (expressed in E. coli), 2.37 Å** Each monomer of the homooctamer has a putative N-terminal transmembrane helix for anchoring to the membrane. This anchor was removed for crystallization. Listed under TRANSMEMBRANE PROTEINS: ALPHA-HELICAL : Intramembrane Proteases, MONOTOPIC MEMBRANE PROTEINS : Peptidases.	3RST	Data File Jmol Viewer	Nam et al. (2012). Nam SE, Kim AC, & Paetzel M (2012). Crystal Structure of Bacillus subtilis Signal Peptide Peptidase A. J Mol Biol 419 :347-358. PubMed Id: 22472423. doi:10.1016/j.jmb.2012.03.020.
*Signal Peptide Peptidase (SppA) K199A mutant showing C-terminal peptide bound in eight active sites: Bacillus subtilis* B Bacteria (expressed in E. coli), 2.39 Å** Each monomer of the homooctamer has a putative N-terminal transmembrane helix for anchoring to the membrane. This anchor was removed for crystallization. Listed under TRANSMEMBRANE PROTEINS: ALPHA-HELICAL : Intramembrane Proteases, MONOTOPIC MEMBRANE PROTEINS : Peptidases.	4KWB	Data File Jmol Viewer	Nam & Paetzel (2013). Nam SE, & Paetzel M (2013). Structure of Signal Peptide Peptidase A with C-Termini Bound in the Active Sites: Insights into Specificity, Self-Processing, and Regulation. Biochemistry 52 :8811-8822. PubMed Id: 24228759.
*Meprin β sheddase (metalloproteinase), pro-form: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 1.85 Å** Mature form, 3.00 Å: 4GWN	4GWM	Data File Jmol Viewer	Arolas et al. (2012). Arolas JL, Broder C, Jefferson T, Guevara T, Sterchi EE, Bode W, Stöcker W, Becker-Pauly C, & Gomis-Rüth FX (2012). Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane. Proc Natl Acad Sci USA 109 :16131-16136. PubMed Id: 22988105. doi:10.1073/pnas.1211076109.
Cytochromes P450 P450s are members of the CYP51 family involved in sterol biosynthesis
*Lanosterol 14α-demethylase with bound lanosterol: Saccharomyces cerevisiae* E Eukaryota, 1.90 Å** with bound itraconazole, 2.19 Å: 5EQB. Supersedes 4K0F. This is the first structure of a full-length single-span 'bitopic' membrane protein. Proteins of this structural type are anchored at the membrane surface by one or two TM segments, which are generally not seen in the structures. See, for example, 1B12.	4LXJ	Data File Jmol Viewer	Monk et al. (2014). Monk BC, Tomasiak TM, Keniya MV, Huschmann FU, Tyndall JD, O'Connell JD 3rd, Cannon RD, McDonald JG, Rodriguez A, Finer-Moore JS, & Stroud RM (2014). Architecture of a single membrane spanning cytochrome P450 suggests constraints that orient the catalytic domain relative to a bilayer. Proc Natl Acad Sci USA 111 :3865-3870. PubMed Id: 24613931. doi:10.1073/pnas.1324245111.
Dihydroorotate Dehydrogenases (DHODH, class 2) Class 1 DHODHs are soluble proteins. Class 2 are membrane associated proteins.
*Dihydroorotate Dehydrogenase: Escherichia coli* B Bacteria, 1.70 Å**	1J79	Data File Jmol Viewer	Thoden et al. (2001). Thoden JB, Phillips GN Jr, Neal TM, Raushel FM, & Holden HM (2001). Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center. Biochemistry 40 :6989-6997. PubMed Id: 11401542.
*Dihydroorotate Dehydrogenase: Escherichia coli* B Bacteria, 1.90 Å**	1XGE	Data File Jmol Viewer	Lee et al. (2005). Lee M, Chan CW, Mitchell Guss J, Christopherson RI, & Maher MJ (2005). Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits. J Mol Biol 348 :523-533. PubMed Id: 15826651.
*Dihydroorotate Dehydrogenase in complex with atovaquone: Rattus rattus* E Eukaryota (expressed in E. coli), 2.30 Å** DHO in complex with brequinar, 2.40 Å: 1UUO	1UUM	Data File Jmol Viewer	Hansen et al. (2004). Hansen M, Le Nours J, Johansson E, Antal T, Ullrich A, Löffler M, & Larsen S (2004). Inhibitor binding in a class 2 dihydroorotate dehydrogenase causes variations in the membrane-associated N-terminal domain. Protein Sci 13 :1031-1042. PubMed Id: 15044733.
*Dihydroorotate Dehydrogenase, apo form: Homo sapiens* E Eukaryota (expressed in E. coli), 3.00 Å** DHODH in complex with brequinar analogue, 2.40 Å: 2PRH DHODH in complex with 'a novel inhibitor', 3.00 Å: 2PRL	2PRM	Data File Jmol Viewer	Walse et al. (2008). Walse B, Dufe VT, Svensson B, Fritzson I, Dahlberg L, Khairoullina A, Wellmar U, & Al-Karadaghi S (2008). The structures of human dihydroorotate dehydrogenase with and without inhibitor reveal conformational flexibility in the inhibitor and substrate binding sites. Biochemistry 47 :8929-8936. PubMed Id: 18672895.
*Dihydroorotate Dehydrogenase with triazolopyrimidine-based inhibitor DSM1: Plasmodium falciparum 3d7* E Eukaryota (expressed in E. coli), 2.00 Å** With bound triazolopyrimidine-based inhibitor DSM2, 2.40 Å: 3I68 With bound triazolopyrimidine-based inhibitor DSM74, 2.50 Å: 3I6R	3I65	Data File Jmol Viewer	Deng et al. (2009). Deng X, Gujjar R, El Mazouni F, Kaminsky W, Malmquist NA, Goldsmith EJ, Rathod PK, & Phillips MA (2009). Structural plasticity of malaria dihydroorotate dehydrogenase allows selective binding of diverse chemical scaffolds. J Biol Chem 284 :26999-27009. PubMed Id: 19640844.
Polymerases
*TagF teichoic acid polymerase: Staphylococcus epidermidis* B Bacteria (expressed in E. coli), 2.70 Å** H444N mutant, 2.81 Å: 3L7J H444N + CDPG, 15' soak, 3.10 Å: 3L7K H444N + CDPG, 30' soak, 2.95 Å: 3L7L H584A mutant, 2.85 Å: 3L7M	3L7I	Data File Jmol Viewer	Lovering et al. (2010). Lovering AL, Lin LY, Sewell EW, Spreter T, Brown ED, & Strynadka NC (2010). Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis. Nat Struct Mol Biol 17 :582-589. PubMed Id: 20400947.
ADP-Ribosylation Factors
*ADP-ribosylation factor (ARF1), myristoylated: Saccharomyces cerevisiae* E Eukaryota (expressed in E. coli), NMR Structure**	2K5U	Data File Jmol Viewer	Liu et al. (2009). Liu Y, Kahn RA, & Prestegard JH (2009). Structure and Membrane Interaction of Myristoylated ARF1. Structure 17 :79-87. PubMed Id: 19141284.
*ADP-ribosylation factor (ARF1GTP), myristoylated: Saccharomyces cerevisiae E Eukaryota (expressed in E. coli), NMR Structure**	2KSQ	Data File Jmol Viewer	Liu et al. (2010). Liu Y, Kahn RA, & Prestegard JH (2010). Dynamic structure of membrane-anchored ArfGTP. Nature Struct Molec Biol* 17 :876-881. PubMed Id: 20601958.
Isomerases
*RPE65 visual cycle retinoid isomerase: Bos taurus* E Eukaryota, 2.14 Å** This retinal pigment epithelium (RPE) protein simultaneously cleaves and isomerizes all-trans-retinyl esters to 11-cis-retinol and a fatty acid.	3FSN	Data File Jmol Viewer	Kiser et al. (2009). Kiser PD, Golczak M, Lodowski DT, Chance MR, Palczewski K (2009). Crystal structure of native RPE65, the retinoid isomerase of the visual cycle. Proc Natl Acad Sci USA 106 :17325-17330. PubMed Id: 19805034.
*RPE65 visual cycle retinoid isomerase in a lipid matrix (crystal form C): Bos taurus* E Eukaryota, 2.50 Å** Crystal form A, 3.00 Å: 4F2Z Crystal form B, iridium derivative, 2.60 Å: 4F3A Crystal form B, native, 3.15 Å: 4F30	4F3D	Data File Jmol Viewer	Kiser et al. (2012). Kiser PD, Farquhar ER, Shi W, Sui X, Chance MR, & Palczewski K (2012). Structure of RPE65 isomerase in a lipidic matrix reveals roles for phospholipids and iron in catalysis. Proc Natl Acad Sci USA 109 :E2747-2756. PubMed Id: 23012475.
Phosphoinositide Kinases
*Phosphatidylinositol 4-kinase IIα: Homo sapiens* E Eukaryota (expressed in E. coli), 2.77 Å**	4PLA	Data File Jmol Viewer	Baumlova et al. (2014). Baumlova A, Chalupska D, Róźycki B, Jovic M, Wisniewski E, Klima M, Dubankova A, Kloer DP, Nencka R, Balla T, & Boura E (2014). The crystal structure of the phosphatidylinositol 4-kinase II?. EMBO Rep 15 :1085-1092. PubMed Id: 25168678. doi:10.15252/embr.201438841.
*Akt1 serine/threonine protein kinase: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.05 Å**	7APJ	Data File Jmol Viewer	Truebestein et al. (2021). Truebestein L, Hornegger H, Anrather D, Hartl M, Fleming KD, Stariha JTB, Pardon E, Steyaert J, Burke JE, & Leonard TA (2021). Structure of autoinhibited Akt1 reveals mechanism of PIP₃-mediated activation. Proc Natl Acad Sci U S A 118 33:e2101496118. PubMed Id: 34385319. doi:10.1073/pnas.2101496118.
Membrane-Shaping Proteins (monotopic)
*IST1-CHMP1B ESCRT-III copolymer: Homo sapiens* E Eukaryota (expressed in E. coli), 4.00 Å** cryo-EM structure	3JC1	Data File Jmol Viewer	McCullough et al. (2015). McCullough J, Clippinger AK, Talledge N, Skowyra ML, Saunders MG, Naismith TV, Colf LA, Afonine P, Arthur C, Sundquist WI, Hanson PI, & Frost A (2015). Structure and membrane remodeling activity of ESCRT-III helical polymers. Science 350 6267:1548-1551. PubMed Id: 26634441. doi:10.1126/science.aad8305.
*ESCRT-III filament composed of CHMP1B, membrane bound: Homo sapiens* E Eukaryota (expressed in E. coli), 6.20 Å** cryo-EM structure ESCRT-III filament composed of CHMP1B+IST1 (right-handed), 3.20 Å: 6TZ4 ESCRT-III filament composed of CHMP1B+IST1 (left-handed), 3.10 Å: 6TZ5 filament composed of IST1 NTD, R16E,K27E mutant, 7.2 Å: 6TZA	6TZ9	Data File Jmol Viewer	Nguyen et al. (2020). Nguyen HC, Talledge N, McCullough J, Sharma A, Moss FR 3rd, Iwasa JH, Vershinin MD, Sundquist WI, & Frost A (2020). Membrane constriction and thinning by sequential ESCRT-III polymerization. Nat Struct Mol Biol 27 4:392-399. PubMed Id: 32251413. doi:10.1038/s41594-020-0404-x.
*CHMP2A-CHMP3 ESCRT-III copolymer, 430 Å diameter: Homo sapiens* E Eukaryota (expressed in E. coli), 3.30 Å** cryo-EM structure 410 Å diameter, 3.60 Å: 7ZCH	7ZCG	Data File Jmol Viewer	Azad et al. (2023). Azad K, Guilligay D, Boscheron C, Maity S, De Franceschi N, Sulbaran G, Effantin G, Wang H, Kleman JP, Bassereau P, Schoehn G, Roos WH, Desfosses A, & Weissenhorn W (2023). Structural basis of CHMP2A-CHMP3 ESCRT-III polymer assembly and membrane cleavage. Nat Struct Mol Biol 30 :81-90. PubMed Id: 36604498. doi:10.1038/s41594-022-00867-8.
*ESCRT-III Snf7 core domain, conformation A: Saccharomyces cerevisiae* E Eukaryota (expressed in E. coli), 2.40 Å** conformation B, 1.60 Å: 5FD9	5FD7	Data File Jmol Viewer	Tang et al. (2015). Tang S, Henne WM, Borbat PP, Buchkovich NJ, Freed JH, Mao Y, Fromme JC, & Emr SD (2015). Structural basis for activation, assembly and membrane binding of ESCRT-III Snf7 filaments. Elife 4 :e12548. PubMed Id: 26670543. doi:10.7554/eLife.12548.
*Shrub, fly ortholog of ESCRT-III SNF7/CHMP4B: Drosophila melanogaster* E Eukaryota (expressed in E. coli), 2.76 Å**	5J45	Data File Jmol Viewer	McMillan et al. (2016). McMillan BJ, Tibbe C, Jeon H, Drabek AA, Klein T, & Blacklow SC (2016). Electrostatic Interactions between Elongated Monomers Drive Filamentation of Drosophila Shrub, a Metazoan ESCRT-III Protein. Cell Rep 16 5:1211-1217. PubMed Id: 27452459. doi:10.1016/j.celrep.2016.06.093.
*Retromer Vps26-Vps29-Vps35 complex: Chaetomium thermophilum* E Eukaryota (expressed in E. coli), 11.4 Å** cryo-electron tomography with subtomogram averaging Vps29 structure by x-ray diffraction, 1.52 Å: 5W8M	6H7W	Data File Jmol Viewer	Kovtun et al. (2018). Kovtun O, Leneva N, Bykov YS, Ariotti N, Teasdale RD, Schaffer M, Engel BD, Owen DJ, Briggs JAG, & Collins BM (2018). Structure of the membrane-assembled retromer coat determined by cryo-electron tomography. Nature 561 7724:561-564. PubMed Id: 30224749. doi:10.1038/s41586-018-0526-z.
*Seipin lipid droplet-formation protein: Drosophila melanogaster* E Eukaryota (expressed in E. coli), 4 Å** cryo-EM structure	6MLU	Data File Jmol Viewer	Sui et al. (2018). Sui X, Arlt H, Brock KP, Lai ZW, DiMaio F, Marks DS, Liao M, Farese RV Jr, & Walther TC (2018). Cryo-electron microscopy structure of the lipid droplet-formation protein seipin. J Cell Biol 217 12:4080-4091. PubMed Id: 30327422. doi:10.1083/jcb.201809067.
*Seipin lipid droplet-formation protein: Saccharomyces cerevisiae* E Eukaryota, 3.45 Å** cryo-EM structure	7RSL	Data File Jmol Viewer	Arlt et al. (2022). Arlt H, Sui X, Folger B, Adams C, Chen X, Remme R, Hamprecht FA, DiMaio F, Liao M, Goodman JM, Farese RV Jr, & Walther TC (2022). Seipin forms a flexible cage at lipid droplet formation sites. Nat Struct Mol Biol 29 3:194-202. PubMed Id: 35210614. doi:10.1038/s41594-021-00718-y.
*Mgm1 mitochondrial remodeling GTPase: Chaetomium thermophilum* E Eukaryota (expressed in E. coli), 3.6 Å** by cryo-tomography: s-Mgm1 decorating the outer surface of tubulated lipid membranes, 14.7 Å: 6RZT s-Mgm1 decorating the outer surface of tubulated lipid membranes in the GTPγS bound state, 14.7 Å: 6RZU s-Mgm1 decorating the inner surface of tubulated lipid membranes, 20.6 Å: 6RZV s-Mgm1 decorating the inner surface of tubulated lipid membranes in the GTPγS bound state, 18.8 Å: 6RZW	6QL4	Data File Jmol Viewer	Faelber et al. (2019). Faelber K, Dietrich L, Noel JK, Wollweber F, Pfitzner AK, Mühleip A, Sánchez R, Kudryashev M, Chiaruttini N, Lilie H, Schlegel J, Rosenbaum E, Hessenberger M, Matthaeus C, Kunz S, von der Malsburg A, Noé F, Roux A, van der Laan M, Kühlbrandt W, & Daumke O (2019). Structure and assembly of the mitochondrial membrane remodelling GTPase Mgm1. Nature 571 7765:429-433. PubMed Id: 31292547. doi:10.1038/s41586-019-1372-3.
*Sorting nexin (SNX)-BAR Mvp1 tetramer: Saccharomyces cerevisiae* E Eukaryota (expressed in E. coli), 4.20 Å** cryo-EM structure	6Q0X	Data File Jmol Viewer	Sun et al. (2020). Sun D, Varlakhanova NV, Tornabene BA, Ramachandran R, Zhang P, & Ford MGJ (2020). The cryo-EM structure of the SNX-BAR Mvp1 tetramer. Nat Commun 11 1. PubMed Id: 32198400. doi:10.1038/s41467-020-15110-5.
*sorting nexin (SNX) protein SNX1, helical array: Mus musculus* E Eukaryota (expressed in E. coli), 9.00 Å** cryo-EM structure 10.0 Å: 7D6E	7D6D	Data File Jmol Viewer	Zhang et al. (2021). Zhang Y, Pang X, Li J, Xu J, Hsu VW, & Sun F (2021). Structural insights into membrane remodeling by SNX1. Proc Natl Acad Sci U S A 118 10. PubMed Id: 33658379. doi:10.1073/pnas.2022614118.
*ESCPE-1 membrane coat (ESCPE: endosomal SNX-BAR sorting complex for promoting exit): Homo sapiens* E Eukaryota (expressed in E. coli), 10.0 Å** cryo-EM structure x-ray: SNX1-SNX5 complex, 2.50 Å: 8A1G x-ray: SNX1-SNX5 complex, Pt derivative, 2.81 Å: 8ABQ	8AFZ	Data File Jmol Viewer	Lopez-Robles et al. (2023). Lopez-Robles C, Scaramuzza S, Astorga-Simon EN, Ishida M, Williamson CD, Baños-Mateos S, Gil-Carton D, Romero-Durana M, Vidaurrazaga A, Fernandez-Recio J, Rojas AL, Bonifacino JS, Castaño-Díez D, & Hierro A (2023). Architecture of the ESCPE-1 membrane coat. Nat Struct Mol Biol 30 7:958-969. PubMed Id: 37322239. doi:10.1038/s41594-023-01014-7.
*myelin P2 protein, N2D variant: Homo sapiens* E Eukaryota (expressed in E. coli), 1.65 Å** P2 protein is a small β-barrel protein involved in myelin sheath formation K3N mutant, 2.70 Å: 6XU9 K21Q mutant, 2.30 Å: 6XUA L27D mutantt, 2.31 Å: 6XUW R30Q mutantt, 3.00 Å: 6STS K31Q mutant, 1.80 Å: 6XVQ L35S mutant, 2.00 Å: 6XVR P38G mutant, unliganded, 1.80 Å: 6XVS K45S mutant, 2.20 Å: 4A1H K65Q mutant, 1.20 Å: 4A1Y R88Q mutant, 1.80 Å: 6XVY K112Q mutant, 1.80 Å: 4A8Z K120S mutant, 2.90 Å: 6XW9	6XU5	Data File Jmol Viewer	Ruskamo et al. (2020). Ruskamo S, Krokengen OC, Kowal J, Nieminen T, Lehtimäki M, Raasakka A, Dandey VP, Vattulainen I, Stahlberg H, & Kursula P (2020). Cryo-EM, X-ray diffraction, and atomistic simulations reveal determinants for the formation of a supramolecular myelin-like proteolipid lattice. J Biol Chem 295 26:8692-8705. PubMed Id: 32265298. doi:10.1074/jbc.RA120.013087.
*Endophilin B1 N-BAR helical scaffold protein: Homo sapiens* E Eukaryota (expressed in E. coli), 9.0 Å** cryo-EM helical scaffold, 10 Å: 6UPN	6UP6	Data File Jmol Viewer	Bhatt et al. (2021). Bhatt VS, Ashley R, & Sundborger-Lunna A (2021). Amphipathic Motifs Regulate N-BAR Protein Endophilin B1 Auto-inhibition and Drive Membrane Remodeling. Structure 29 1:61-69.e3. PubMed Id: 33086035. doi:10.1016/j.str.2020.09.012.
*coat protein complex II (COPII) on membranes, outer coat right-handed rod, class1: Saccharomyces cerevisiae* E Eukaryota (expressed in Spodoptera frugiperda), 40.0 Å** cryo-EM structure outer coat vertex, 12 Å: 6ZG6 inner coat, 4.60 Å: 6ZGA outer coat left-handed rod, 40 Å: 6ZL0	6ZG5	Data File Jmol Viewer	Hutchings et al. (2021). Hutchings J, Stancheva VG, Brown NR, Cheung ACM, Miller EA, & Zanetti G (2021). Structure of the complete, membrane-assembled COPII coat reveals a complex interaction network. Nat Commun 12 1:2034. PubMed Id: 33795673. doi:10.1038/s41467-021-22110-6.
*metazoan membrane-assembled retromer:SNX3, VPS35/VPS29 arch: Homo sapiens* E Eukaryota (expressed in E. coli), 8.90 Å** cryo-EM structure VPS26 dimer region, 9.50 Å 7BLO Grd19 complex (Chaetomium thermophilum, 9.50 Å 7BLP Grd19 complex, Vps26 dimer region, 9.20 Å 7BLQ Vps5 (SNX-BAR) complex (Chaetomium thermophilum), 9.30 Å 7BLR	7BLN	Data File Jmol Viewer	Leneva et al. (2021). Leneva N, Kovtun O, Morado DR, Briggs JAG, & Owen DJ (2021). Architecture and mechanism of metazoan retromer:SNX3 tubular coat assembly. Sci Adv 7 13:eabf8598. PubMed Id: 33762348. doi:10.1126/sciadv.abf8598.
*Atlastin-1 GTPase (residues 1-439) bound to GDP-Mg²⁺: Homo sapiens* E Eukaryota (expressed in E. coli), 2.20 Å** atlastin-3 (residues 1-334) bound to GDP-Mg²⁺, 2.10 Å 6XJO	6XJN	Data File Jmol Viewer	Kelly et al. (2021). Kelly CM, Byrnes LJ, Neela N, Sondermann H, & O'Donnell JP (2021). The hypervariable region of atlastin-1 is a site for intrinsic and extrinsic regulation. J Cell Biol 220 11:e202104128. PubMed Id: 34546351. doi:10.1083/jcb.202104128.
*caveolin-1 complex: Homo sapiens* E Eukaryota (expressed in E. coli), 3.40 Å** cryo-EM structure	7SC0	Data File Jmol Viewer	Porta et al. (2022). Porta JC, Han B, Gulsevin A, Chung JM, Peskova Y, Connolly S, Mchaourab HS, Meiler J, Karakas E, Kenworthy AK, & Ohi MD (2022). Molecular architecture of the human caveolin-1 complex. Sci Adv 8 19:eabn7232. PubMed Id: 35544577. doi:10.1126/sciadv.abn7232.
*Eps15-homology domain containing proteins (EHDs), EHD4 complex: Mus musculus* E Eukaryota (expressed in E. coli), 7.60 Å** cryo-EM structure by cryo-EM tomography	7SOX	Data File Jmol Viewer	Melo et al. (2022). Melo AA, Sprink T, Noel JK, Vázquez-Sarandeses E, van Hoorn C, Mohd S, Loerke J, Spahn CMT, & Daumke O (2022). Cryo-electron tomography reveals structural insights into the membrane remodeling mode of dynamin-like EHD filaments. Nat Commun 13 1:7641. PubMed Id: 36496453. doi:10.1038/s41467-022-35164-x.
Membrane Trafficking Proteins
*BBSome (complex of 7 Bardet–Biedl syndrome, BBS, proteins), apo form: Bos taurus* E Eukaryota, 3.44 Å** cryo-EM structure BBSome-ARL6 complex, 4.00 Å: 6VOA	6VNW	Data File Jmol Viewer	Yang et al. (2020). Yang S, Bahl K, Chou HT, Woodsmith J, Stelzl U, Walz T, & Nachury MV (2020). Near-atomic structures of the BBSome reveal the basis for BBSome activation and binding to GPCR cargoes. Elife 9 :e55954. PubMed Id: 32510327. doi:10.7554/eLife.55954.
Cell Adhesion Molecules
*Opioid Binding Protein/Cell Adhesion Molecule Like (OPCML): Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.65 Å**	5UV6	Data File Jmol Viewer	Birtley et al. (2019). Birtley JR, Alomary M, Zanini E, Antony J, Maben Z, Weaver GC, Von Arx C, Mura M, Marinho AT, Lu H, Morecroft EVN, Karali E, Chayen NE, Tate EW, Jurewicz M, Stern LJ, Recchi C, & Gabra H (2019). Inactivating mutations and X-ray crystal structure of the tumor suppressor OPCML reveal cancer-associated functions. Nat Commun 10 1. PubMed Id: 31316070. doi:10.1038/s41467-019-10966-8.
*P140-P110 Nap adhesion complex: Mycoplasma genitalium* B Bacteria, 4.10 Å** cryo-EM structure Adhesin P140 x-ray structure, 3.24 Å: 6S3U Heterodimer Nap Complex (P140-P110 globular) x-ray structure, 2.65 Å: 6RUT	6YRK	Data File Jmol Viewer	Aparicio et al. (2020). Aparicio D, Scheffer MP, Marcos-Silva M, Vizarraga D, Sprankel L, Ratera M, Weber MS, Seybert A, Torres-Puig S, Gonzalez-Gonzalez L, Reitz J, Querol E, Piñol J, Pich OQ, Fita I, & Frangakis AS (2020). Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium. Nat Commun 11 1:2877. PubMed Id: 32513917. doi:10.1038/s41467-020-16511-2.
Guanosine Triphosphatases
*Lysosomal Folliculin Complex (FLCN-FNIP2-RagA-RagC-Ragulator): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.6 Å** cryo-EM structure	6NZD	Data File Jmol Viewer	Lawrence et al. (2019). Lawrence RE, Fromm SA, Fu Y, Yokom AL, Kim DJ, Thelen AM, Young LN, Lim CY, Samelson AJ, Hurley JH, & Zoncu R (2019). Structural mechanism of a Rag GTPase activation checkpoint by the lysosomal folliculin complex. Science 366 6468:971-977. PubMed Id: 31672913. doi:10.1126/science.aax0364.
*FLCN-FNIP2-Rag-Ragulator complex: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.31 Å** cryo-EM structure	6ULG	Data File Jmol Viewer	Shen et al. (2019). Shen K, Rogala KB, Chou HT, Huang RK, Yu Z, & Sabatini DM (2019). Cryo-EM Structure of the Human FLCN-FNIP2-Rag-Ragulator Complex. Cell 179 6:1319-1329.e8. PubMed Id: 31704029. doi:10.1016/j.cell.2019.10.036.
Phospholipid Phosphatases
*MTMR8 catalytic phosphatase domain: Homo sapiens* E Eukaryota (expressed in E. coli), 2.8 Å**	4Y7I	Data File Jmol Viewer	Yoo et al. (2015). Yoo KY, Son JY, Lee JU, Shin W, Im DW, Kim SJ, Ryu SE, & Heo YS (2015). Structure of the catalytic phosphatase domain of MTMR8: implications for dimerization, membrane association and reversible oxidation. Acta Crystallogr. D Biol. Crystallogr. 71 :1528-1539. PubMed Id: 26143924. doi:10.1107/S139900471500927X.
*lipin/Pah phosphatidic acid phosphatase: Tetrahymena thermophila* B Bacteria (expressed in E. coli), 3 Å** Lipin Phosphatidic Acid Phosphatase with Magnesium, 3 Å: 6TZZ	6TZY	Data File Jmol Viewer	Khayyo et al. (2020). Khayyo VI, Hoffmann RM, Wang H, Bell JA, Burke JE, Reue K, & Airola MVV (2020). Crystal structure of a lipin/Pah phosphatidic acid phosphatase. Nat Commun 11 1:1309. PubMed Id: 32161260. doi:10.1038/s41467-020-15124-z.
Sorting Nexins
*sorting nexin 11 SNX11-PXe domain in dimer form: Homo sapiens* E Eukaryota (expressed in E. coli), 3.50 Å** SNX11-PXe domain in complex with PI(3,5)P₂, 2.14 Å: 6KOJ SNX11/SNX10-PXe Chimera, 2.00 Å: 6KOK	6KOI	Data File Jmol Viewer	Xu et al. (2020). Xu T, Gan Q, Wu B, Yin M, Xu J, Shu X, & Liu J (2020). Molecular Basis for PI(3,5)P₂ Recognition by SNX11, a Protein Involved in Lysosomal Degradation and Endosome Homeostasis Regulation. J Mol Biol 432 16:4750-4761. PubMed Id: 32561432. doi:10.1016/j.jmb.2020.06.010.
Pro-apoptotic BCL-2 Family
*BAK core domain BH3-groove in complex with E. coli* lipid: Homo sapiens E Eukaryota (expressed in E. coli), 2.49 Å** in complex with phosphatidylserine, 2.49 Å: 6UXN in complex with DDM, 1.80 Å: 6UXO in complex with phosphatidylglycerol, 2.49 Å: 6UXP in complex with POPC and C8E4, 1.70 Å: 6UXQ in complex with LysoPC, 1.80 Å: 6UXR	6UXM	Data File Jmol Viewer	Cowan et al. (2020). Cowan AD, Smith NA, Sandow JJ, Kapp EA, Rustam YH, Murphy JM, Brouwer JM, Bernardini JP, Roy MJ, Wardak AZ, Tan IK, Webb AI, Gulbis JM, Smith BJ, Reid GE, Dewson G, Colman PM, & Czabotar PE (2020). BAK core dimers bind lipids and can be bridged by them. Nat Struct Mol Biol 27 11:1024-1031. PubMed Id: 32929280. doi:10.1038/s41594-020-0494-5.
*Bax core dimer in bicelles: Homo sapiens* E Eukaryota (expressed in E coli), NMR structure**	6L8V	Data File Jmol Viewer	Lv et al. (2021). Lv F, Qi F, Zhang Z, Wen M, Kale J, Piai A, Du L, Wang S, Zhou L, Yang Y, Wu B, Liu Z, Del Rosario J, Pogmore J, Chou JJ, Andrews DW, Lin J, & OuYang B (2021). An amphipathic Bax core dimer forms part of the apoptotic pore wall in the mitochondrial␣membrane. EMBO J 40 14:e106438. PubMed Id: 34101209. doi:10.15252/embj.2020106438.
*Bak transmembrane helix in DPC micelles: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure** in lipid nanodiscs, 7OFO	7OFM	Data File Jmol Viewer	Sperl et al. (2021). Sperl LE, Rührnößl F, Schiller A, Haslbeck M, & Hagn F (2021). High-resolution analysis of the conformational transition of pro-apoptotic Bak at the lipid membrane. EMBO J 40 20:e107159. PubMed Id: 34523144. doi:10.15252/embj.2020107159.
Variant Surface Glycoproteins (VSG)
*N-terminal Domain of VSG2 (MITat 1.2): Trypanosoma brucei* B Bacteria, 2.90 Å**	1VSG	Data File Jmol Viewer	Freymann et al. (1990). Freymann D, Down J, Carrington M, Roditi I, Turner M, & Wiley D (1990). 2.9 Å resolution structure of the N-terminal domain of a variant surface glycoprotein from Trypanosoma brucei. J Mol Biol 216 1:141-160. PubMed Id: 2231728.
*N-terminal of VSG ILTat 1.24: Trypanosoma brucei* B Bacteria, 2.70 Å**	2VSG	Data File Jmol Viewer	Blum et al. (1993). Blum ML, Down JA, Gurnett AM, Carrington M, Turner MJ, & Wiley DC (1993). A structural motif in the variant surface glycoproteins of Trypanosoma brucei. Nature 362 6421:603-609. PubMed Id: 8464512.
*N-terminal domain of VSG M1.1: Trypanosoma brucei* B Bacteria, 1.65 Å** C-terminal domain of VSG M1.1 (NMR structure) 5M4T	5LY9	Data File Jmol Viewer	Bartossek et al. (2017). Bartossek T, Jones NG, Schäfer C, Cvitković M, Glogger M, Mott HR, Kuper J, Brennich M, Carrington M, Smith AS, Fenz S, Kisker C, & Engstler M (2017). Structural basis for the shielding function of the dynamic trypanosome variant surface glycoprotein coat. Nat Microbiol 2 11:1523-1532. PubMed Id: 28894098. doi:10.1038/s41564-017-0013-6.
*N-terminal Domain of VSG3: Trypanosoma brucei* B Bacteria, 1.41 Å**	6ELC	Data File Jmol Viewer	Pinger et al. (2018). Pinger J, Nešić D, Ali L, Aresta-Branco F, Lilic M, Chowdhury S, Kim HS, Verdi J, Raper J, Ferguson MAJ, Papavasiliou FN, & Stebbins CE (2018). African trypanosomes evade immune clearance by O-glycosylation of the VSG surface coat. Nat Microbiol 3 8:932-938. PubMed Id: 29988048. doi:10.1038/s41564-018-0187-6.
*Variant Surface Glycoproteins VSGsur & VSG13: Trypanosoma brucei* E Eukaryota, 1.21 Å** VSGsur bound to suramin, 1.86 Å 6Z7B VSGsur mutant H122A, 1.64 Å 6Z7C H122A soaked in 0.77 mM Suramin, 1.75 Å 6Z7D H122A soaked in 7.7 mM suramin, 1.66 Å 6Z7E VSG13 soaked in 0.5 M used to phase VSG13, 1.56 Å 6Z8G Variant Surface Glycoprotein VSG13, 1.38 Å 6Z8H VSGsur, I3C ("Magic Triangle") derivative, 1.92 Å 6Z79	6Z7A	Data File Jmol Viewer	Zeelen et al. (2021). Zeelen J, van Straaten M, Verdi J, Hempelmann A, Hashemi H, Perez K, Jeffrey PD, Hälg S, Wiedemar N, Mäser P, Papavasiliou FN, & Stebbins CE (2021). Structure of trypanosome coat protein VSGsur and function in suramin resistance. Nat Microbiol 6 3:392-400. PubMed Id: 33462435. doi:10.1038/s41564-020-00844-1.
TRANSMEMBRANE PROTEINS: BETA-BARREL
Adventitious Membrane Proteins: Beta-sheet Pore-forming Toxins/Attack Complexes
*α-hemolysin: Staphylococcus aureus* B Bacteria, 1.9 Å**	7AHL	Data File Jmol Viewer 7AHL alpha-hemolysin	Song et al. (1996). Song L, Hobaugh MR, Shustak C, Cheley S, Bayley H, & Gouaux JE (1996). Structure of staphylococcal a -hemolysin, a heptameric transmembrane pore. Science 274 :1859-1866. PubMed Id: 8943190.
*α-hemolysin, M113F mutant: Staphylococcus aureus* B Bacteria, 2.10 Å** M113F mutant complexed with β-cyclodextrin, 2.20 Å: 3M3R M113N mutant, 1.90 Å: 3M4D M113N mutant complexed with β-cyclodextrin, 2.30 Å: 3M4E	3M2L	Data File Jmol Viewer 3M2L 3M4E 3M3R 3M4D	Banerjee et al. (2010). Banerjee A, Mikhailova E, Cheley S, Gu LQ, Montoya M, Nagaoka Y, Gouaux E, & Bayley H (2010). Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores. Proc Natl Acad Sci USA 107 :8165-8170. PubMed Id: 20400691. doi:10.1073/pnas.0914229107 .
*α-hemolysin: Staphylococcus aureus* B Bacteria (expressed in E. coli), 2.30 Å** Crystals were prepared using 2-methyl-2,4-pentanediol without detergent.	3ANZ	Data File Jmol Viewer 3ANZ	Tanaka et al. (2011). Tanaka Y, Hirano N, Kaneko J, Kamio Y, Yao M, & Tanaka I (2011). 2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structure. Protein Sci 20 :448-456. PubMed Id: 21280135. doi:10.1002/pro.579.
*α-hemolysin heptamer, C₁₄-bound: Staphylococcus aureus* B Bacteria (expressed in E. coli), 2.35 Å** heptamer, H35A mutant, C₁₄-bound, 2.49 Å:: 6U4P monomer, H35A mutant, C₁₄-bound, 2.79 Å: 6U3T	6U49	Data File Jmol Viewer 6U49 6U3T 6U4P	Liu et al. (2020). Liu J, Kozhaya L, Torres VJ, Unutmaz D, & Lu M (2020). Structure-based discovery of a small-molecule inhibitor of methicillin-resistant Staphylococcus aureus virulence. J Biol Chem 295 18:5944-5959. PubMed Id: 32179646. doi:10.1074/jbc.RA120.012697.
*α-hemolysin: Vibrio campbelli* B Bacteria (expressed in E. coli), 2.00 Å** X-ray structure assembled heptamer, cryo-EM structure, 2.06 Å: 8JC7	8JBQ	Data File Jmol Viewer 8JBQ 8JC7	Chiu et al. (2023). Chiu YC, Yeh MC, Wang CH, Chen YA, Chang H, Lin HY, Ho MC, & Lin SM (2023). Structural basis for calcium-stimulating pore formation of Vibrio α-hemolysin. Nat Commun 14 1:5946. PubMed Id: 37741869. doi:10.1038/s41467-023-41579-x.
*γ-hemolysin composed of LukF and Hlg2: Staphylococcus aureus* B Bacteria (expressed in E. coli), 2.50 Å**	3B07	Data File Jmol Viewer 3B07	Yamashita et al. (2011). Yamashita K, Kawai Y, Tanaka Y, Hirano N, Kaneko J, Tomita N, Ohta M, Kamio Y, Yao M, & Tanaka I (2011). Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components. Proc Natl Acad Sci USA 108 :17314-17319. PubMed Id: 21969538. doi:10.1073/pnas.1110402108.
*γ-hemolysin prepore: Staphylococcus aureus* B Bacteria (expressed in E. coli), 2.99 Å**	4P1Y	Data File Jmol Viewer 4P1Y	Yamashita et al. (2014). Yamashita D, Sugawara T, Takeshita M, Kaneko J, Kamio Y, Tanaka I, Tanaka Y, & Yao M (2014). Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins. Nat Commun 5 :4897. PubMed Id: 25263813. doi:10.1038/ncomms5897.
*LukF component of γ-hemolysin: Staphylococcus aureus* B Bacteria (expressed in E. coli), 1.9 Å** The structure is of the water soluble form of the protein. At 2.5 Å: 2LKF. With bound phosphocholine, 1.9 Å: 3LKF	1LKF	Data File Jmol Viewer 1LKF 2LKF 3LKF	Olson et al. (1999). Olson R, Nariya H, Yokota K, Kamio Y, & Gouaux E (1999). Crystal structure of Staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nature Struc. Biol 6 :134-140. PubMed Id: 10048924.
*LUK prepore formed from LukF & LukS: Staphylococcus aureus* B Bacteria (expressed in E. coli), 2.40 Å**	4P1X	Data File Jmol Viewer 4P1X	Yamashita et al. (2014). Yamashita D, Sugawara T, Takeshita M, Kaneko J, Kamio Y, Tanaka I, Tanaka Y, & Yao M (2014). Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins. Nat Commun 5 :4897. PubMed Id: 25263813. doi:10.1038/ncomms5897.
*LukGH octamer: Staphylococcus aureus* B Bacteria (expressed in E. coli), 2.80 Å**	4TW1	Data File Jmol Viewer 4TW1	Badarau et al. (2015). Badarau A, Rouha H, Malafa S, Logan DT, Håkansson M, Stulik L, Dolezilkova I, Teubenbacher A, Gross K, Maierhofer B, Weber S, Jägerhofer M, Hoffman D, & Nagy E (2015). Structure-function analysis of heterodimer formation, oligomerization, and receptor binding of the Staphylococcus aureus bi-component toxin LukGH. J Biol Chem 290 1:142-156. PubMed Id: 25371205. doi:10.1074/jbc.M114.598110.
*Leukocidin (LukFG) in complex with mouse CD11b I-domain (CD11b-I): Staphylococcus aureus* B Bacteria (expressed in E. coli), 2.29 Å** in complex with human CD11b I-domain (CD11b-I), 2.75 Å: 6RHW	6RHV	Data File Jmol Viewer 6RHV 6RHW	Trstenjak et al. (2020). Trstenjak N, Milić D, Graewert MA, Rouha H, Svergun D, Djinović-Carugo K, Nagy E, & Badarau A (2020). Molecular mechanism of leukocidin GH-integrin CD11b/CD18 recognition and species specificity. Proc Natl Acad Sci USA 117 1:317-327. PubMed Id: 31852826. doi:10.1073/pnas.1913690116.
*LukD, no ligand: Staphylococcus aureus* B Bacteria (expressed in E. coli), 1.75 Å** LukD, C₁₄PC-bound, 1.5 Å: 6U2S LukF-PV, C₁₄PC-bound, 1.78 Å: 6U3F	6U33	Data File Jmol Viewer 6U33 6U2S 6U3F	Liu et al. (2020). Liu J, Kozhaya L, Torres VJ, Unutmaz D, & Lu M (2020). Structure-based discovery of a small-molecule inhibitor of methicillin-resistant Staphylococcus aureus virulence. J Biol Chem 295 18:5944-5959. PubMed Id: 32179646. doi:10.1074/jbc.RA120.012697.
*leukotoxin LukE: Staphylococcus aureus* B Bacteria (expressed in E. coli), 1.46 Å** LukE, 1.90 Å 7P8S in complex with p-cresyl sulfate, 1.60 Å 7P8U in complex with a doubly sulfated CCR2 N-terminal peptide, 1.40 Å 7P8X in complex with a sulfated ACKR1 N-terminal peptide, 1.55 Å 7P93	7P8T	Data File Jmol Viewer 7P8T 7P93 7P8U 7P8S 7P8X	Lambey et al. (2022). Lambey P, Otun O, Cong X, Hoh F, Brunel L, Verdié P, Grison CM, Peysson F, Jeannot S, Durroux T, Bechara C, Granier S, & Leyrat C (2022). Structural insights into recognition of chemokine receptors by Staphylococcus aureus leukotoxins. Elife 11 :e72555. PubMed Id: 35311641. doi:10.7554/eLife.72555.
*Panton-Valentine leukocidin (PVL) with bound C₁₄PC: Staphylococcus aureus* B Bacteria (expressed in E. coli), 2.04 Å**	6U3Y	Data File Jmol Viewer 6U3Y	Liu et al. (2020). Liu J, Kozhaya L, Torres VJ, Unutmaz D, & Lu M (2020). Structure-based discovery of a small-molecule inhibitor of methicillin-resistant Staphylococcus aureus virulence. J Biol Chem 295 18:5944-5959. PubMed Id: 32179646. doi:10.1074/jbc.RA120.012697.
*NetB Necrotic B-like enteritis toxin: Clostridium perfringens* B Bacteria (expressed in E. coli), 3.90 Å**	4H56	Data File Jmol Viewer 4H56	Savva et al. (2013). Savva CG, Fernandes da Costa SP, Bokori-Brown M, Naylor CE, Cole AR, Moss DS, Titball RW, & Basak AK (2013). Molecular architecture and functional analysis of NetB, a pore-forming toxin from Clostridium perfringens. J Biol Chem 288 5:3512-3522. PubMed Id: 23239883. doi:10.1074/jbc.M112.430223.
*Perfringolysin O (PFO) protomer: Clostridium perfringens* B Bacteria (expressed in E. coli), 2.20 Å** The protein is a thiol-activated cytolysin that uses membrane cholesterol as a receptor. 40 or more protomers assemble into a large pore anchored in the bilayer by the β-sheets of domain 4. Space group is C222₁. P2₁2₁2 space group, 3.0 Å: 1M3J. P3₁ space group, 2.90 Å: 1M3I.	1PFO	Data File Jmol Viewer 1PFO 1M3I 1M3J	Rossjohn et al. (1997). Rossjohn J, Feil SC, McKinstry WJ, Tweten RK, & Parker MW (1997). Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 89 :685-692. PubMed Id: 9182756.
*Anthrax Protective Antigen (PA) and Lethal Factor (LF) Prechannel Complex: Bacillus anthraciss* B Bacteria (expressed in E. coli), 3.10 Å** The structure is the PA₈LF₄ prechannel.	3KWV	Data File Jmol Viewer 3KWV	Feld et al. (2010). Feld GK, Thoren KL, Kintzer AF, Sterling HJ, Tang II, Greenberg SG, Williams ER, & Krantz BA (2010). Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers. Nat Struct Mol Biol 17 :1383-1390. PubMed Id: 21037566.
*Anthrax protective antigen pore: Bacillus anthracis* B Bacteria (expressed in E. coli), 2.9 Å** cryo-EM structure	3J9C	Data File Jmol Viewer 3J9C	Jiang et al. (2015). Jiang J, Pentelute BL, Collier RJ, & Zhou ZH (2015). Atomic structure of anthrax protective antigen pore elucidates toxin translocation. Nature 521 :545-549. PubMed Id: 25778700. doi:10.1038/nature14247.
*Anthrax octamer prechannel bound to full-length edema factor (EF): Bacillus anthracis* B Bacteria (expressed in E. coli), 3.30 Å** cryo-EM structure bound to full-length lethal factor (LF), 3.80 Å: 6WJJ	6VRA	Data File Jmol Viewer 6VRA 6WJJ	Zhou et al. (2020). Zhou K, Liu S, Hardenbrook NJ, Cui Y, Krantz BA, & Zhou ZH (2020). Atomic Structures of Anthrax Prechannel Bound with Full-Length Lethal and Edema Factors. Structure 28 8:879-887.e3. PubMed Id: 32521227. doi:10.1016/j.str.2020.05.009.
*Anthrax protective antigen pore translating N-terminal of LF: Bacillus anthracis* B Bacteria (expressed in E. coli), 3.30 Å** cryo-EM structure	7KXR	Data File Jmol Viewer 7KXR	Machen et al. (2021). Machen AJ, Fisher MT, & Freudenthal BD (2021). Anthrax toxin translocation complex reveals insight into the lethal factor unfolding and refolding mechanism. Sci Rep 11 1:13038. PubMed Id: 34158520. doi:10.1038/s41598-021-91596-3.
*Lymphocyte perforin monomer: Mus musculus* E Eukaryota (expressed in S. frugiperda), 2.75 Å** The multimeric pore structure has been visualized by cryo-EM.	3NSJ	Data File Jmol Viewer 3NSJ	Law et al. (2010). Law RH, Lukoyanova N, Voskoboinik I, Caradoc-Davies TT, Baran K, Dunstone MA, D'Angelo ME, Orlova EV, Coulibaly F, Verschoor S, Browne KA, Ciccone A, Kuiper MJ, Bird PI, Trapani JA, Saibil HR, & Whisstock JC (2010). The structural basis for membrane binding and pore formation by lymphocyte perforin. Nature 468 :447-451. PubMed Id: 21037563.
*Lymphocyte perforin pore: Mus musculus* E Eukaryota (expressed in Spodoptera frugiperda), 4.00 Å** cryo-EM structure	7PAG	Data File Jmol Viewer 7PAG	Ivanova et al. (2022). Ivanova ME, Lukoyanova N, Malhotra S, Topf M, Trapani JA, Voskoboinik I, & Saibil HR (2022). The pore conformation of lymphocyte perforin. Sci Adv 8 6:eabk3147. PubMed Id: 35148176. doi:10.1126/sciadv.abk3147.
*Macrophage-expressed gene 1 (MPEG1/Perforin-2), wild-type soluble pre-pore: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.49 Å** cryo-EM structure L425K, alpha conformation pre-pore, 2.37 Å: 6U2J L425K, alpha conformation pre-pore, monomer, 2.93 Å: 6U2K L425K soluble pre-pore complex, 2.83 Å: 6U2L L425K pre-pore complex bound to liposome, 3.63 Å: 6U2W	6U23	Data File Jmol Viewer 6U23 6U2J 6U2K 6U2L 6U2W	Pang et al. (2019). Pang SS, Bayly-Jones C, Radjainia M, Spicer BA, Law RHP, Hodel AW, Parsons ES, Ekkel SM, Conroy PJ, Ramm G, Venugopal H, Bird PI, Hoogenboom BW, Voskoboinik I, Gambin Y, Sierecki E, Dunstone MA, & Whisstock JC (2019). The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1. Nat Commun 10 1. PubMed Id: 31537793. doi:10.1038/s41467-019-12279-2.
*Macrophage-expressed gene 1 (MPEG1/Perforin-2), pore in ring form: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure pore in twisted form, 4.00 Å: 8A1S	8A1D	Data File Jmol Viewer 8A1D 8A1S	Yu et al. (2022). Yu X, Ni T, Munson G, Zhang P, & Gilbert RJC (2022). Cryo-EM structures of perforin-2 in isolation and assembled on a membrane suggest a mechanism for pore formation. EMBO J 41 23:e111857. PubMed Id: 36245269. doi:10.15252/embj.2022111857.
*Cytolysin pore-forming toxin: Vibrio cholerae* B Bacteria (expressed in E. coli), 2.88 Å** Reveals the full structure of the assembled heptameric pore. The pore has a novel ring of tryptophan residues lining the narrowest constriction.	3O44	Data File Jmol Viewer 3O44	De & Olson (2011). De S & Olson R. (2011). Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins Proc Natl Acad Sci USA 108 :7385-7390. PubMed Id: 21502531. doi:10.1073/pnas.1017442108.
*Cytolysin pore-forming toxin protomer: Vibrio cholerae* B Bacteria (expressed in E. coli), 2.30 Å**	1XEZ	Data File Jmol Viewer 1XEZ	Olson & Gouaux (2005). Olson R & Gouaux E (2005). Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore J Mol Biol 350 :997-1016. PubMed Id: 15978620 . doi:10.1016/j.jmb.2005.05.045.
*Streptolysin O pore-forming toxin: Streptococcus pyogenes* B Bacteria (expressed in E. coli), 2.10 Å**	4HSC	Data File Jmol Viewer 4HSC	Feil et al. (2014). Feil SC, Ascher DB, Kuiper MJ, Tweten RK, & Parker MW (2014). Structural Studies of Streptococcus pyogenes Streptolysin O Provide Insights into the Early Steps of Membrane Penetration. J Mol Biol 426 :785-792. PubMed Id: 24316049. doi:10.1016/j.jmb.2013.11.020.
*Aerolysin pore-forming toxin Y221G mutant: Aeromonas hydrophila* B Bacteria (expressed in Aeromonas salmonicida), 2.88 Å** Y221G mutant, 2.20 Å: 3C0N Y221G mutant in complex with mannose-6-phosphate, 2.50 Å: 3C0O The paper shows models of the assembled heptameric pore.	3C0M	Data File Jmol Viewer 3C0M 3C0O 3C0N	Degiacomi et al. (2013). Degiacomi MT, Iacovache I, Pernot L, Chami M, Kudryashev M, Stahlberg H, van der Goot FG, & Dal Peraro M (2013). Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism. Nat Chem Biol 9 10:623-629. PubMed Id: 23912165. doi:10.1038/nchembio.1312.
*Monalysin pore-forming toxin, cleaved form: Pseudomonas entomophila* B Bacteria (expressed in E. coli), 1.70 Å** mutant deleted of the membrane-spanning domain, 2.65 Å: 4MKQ EM structure deposited in EMBD as EMD-2698.	4MKO	Data File Jmol Viewer 4MKO 4MKQ	Leone et al. (2015). Leone P, Bebeacua C, Opota O, Kellenberger C, Klaholz B, Orlov I, Cambillau C, Lemaitre B, & Roussel A (2015). X-ray and Cryo-electron Microscopy Structures of Monalysin Pore-forming Toxin Reveal Multimerization of the Pro-form. J Biol Chem 290 :13191-13201. PubMed Id: 25847242. doi:10.1074/jbc.M115.646109.
*poly-C9 component of the complement membrane attack Complex: Homo sapiens* E Eukaryota, 8 Å** model from cryo-EM	5FMW	Data File Jmol Viewer 5FMW	Dudkina et al. (2016). Dudkina NV, Spicer BA, Reboul CF, Conroy PJ, Lukoyanova N, Elmlund H, Law RH, Ekkel SM, Kondos SC, Goode RJ, Ramm G, Whisstock JC, Saibil HR, & Dunstone MA (2016). Structure of the poly-C9 component of the complement membrane attack complex. Nat Commun 7 . PubMed Id: 26841934. doi:10.1038/ncomms10588. See also: Serna et al. (2016). Serna M, Giles JL, Morgan BP, & Bubeck D (2016). Structural basis of complement membrane attack complex formation. Nat Commun 7 :10587. PubMed Id: 26841837. doi:10.1038/ncomms10587.
*poly-C9 component of the complement membrane attack Complex: Homo sapiens* E Eukaryota (expressed in Expi293 cells), 3.9 Å** cryo-EM structure	6DLW	Data File Jmol Viewer 6DLW	Spicer et al. (2018). Spicer BA, Law RHP, Caradoc-Davies TT, Ekkel SM, Bayly-Jones C, Pang SS, Conroy PJ, Ramm G, Radjainia M, Venugopal H, Whisstock JC, & Dunstone MA (2018). The first transmembrane region of complement component-9 acts as a brake on its self-assembly. Nat Commun 9 1:3266. PubMed Id: 30111885. doi:10.1038/s41467-018-05717-0.
*Membrane attack complex (MAC) in open conformation: Homo sapiens* E Eukaryota, 5.6 Å** cryo-EM structure closed conformation, 5.6 Å: 6H04	6H03	Data File Jmol Viewer 6H03 6H04	Menny et al. (2018). Menny A, Serna M, Boyd CM, Gardner S, Joseph AP, Morgan BP, Topf M, Brooks NJ, & Bubeck D (2018). CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers. Nat Commun 9 1. PubMed Id: 30552328. doi:10.1038/s41467-018-07653-5.
*3C9-sMAC Complement membrane attack complex packaged for clearance: Homo sapiens* E Eukaryota, 3.54 Å** cryo-EM structure 2C9-sMAC, 3.27 Å 7NYD	7NYC	Data File Jmol Viewer 7NYC 7NYD	Menny et al. (2021). Menny A, Lukassen MV, Couves EC, Franc V, Heck AJR, & Bubeck D (2021). Structural basis of soluble membrane attack complex packaging for clearance. Nat Commun 12 1:6086. PubMed Id: 34667172. doi:10.1038/s41467-021-26366-w.
*monomeric C9 component of the complement membrane attack Complex: Mus musculus* E Eukaryota (expressed in Expi293 cells), 2.2 Å**	6CXO	Data File Jmol Viewer 6CXO	Spicer et al. (2018). Spicer BA, Law RHP, Caradoc-Davies TT, Ekkel SM, Bayly-Jones C, Pang SS, Conroy PJ, Ramm G, Radjainia M, Venugopal H, Whisstock JC, & Dunstone MA (2018). The first transmembrane region of complement component-9 acts as a brake on its self-assembly. Nat Commun 9 1:3266. PubMed Id: 30111885. doi:10.1038/s41467-018-05717-0.
*Lysenin Pore complex: Eisenia fetida* B Bacteria (expressed in E. coli), 3.1 Å** cryo-EM structure	5GAQ	Data File Jmol Viewer 5GAQ	Bokori-Brown et al. (2016). Bokori-Brown M, Martin TG, Naylor CE, Basak AK, Titball RW, & Savva CG (2016). Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein. Nat Commun 7 :11293. PubMed Id: 27048994. doi:10.1038/ncomms11293.
*ILY^ml Cholesterol-dependent cytolysin, CD59-responsive: Streptococcus intermedius* B Bacteria (expressed in E. coli), 2.89 Å** ILY^ml = monomer-locked via a disulfide. Bound to CD59^D22A, 2.7 Å: 5IMT	5IMW	Data File Jmol Viewer 5IMW 5IMT	Lawrence et al. (2016). Lawrence SL, Gorman MA, Feil SC, Mulhern TD, Kuiper MJ, Ratner AJ, Tweten RK, Morton CJ, & Parker MW (2016). Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins. Structure 24 :1488-1498. PubMed Id: 27499440. doi:10.1016/j.str.2016.06.017.
*VLY^ml Cholesterol-dependent cytolysin, CD-59 responsive, bound to CD59^D22A: Gardnerella vaginalis* B Bacteria (expressed in E. coli), 2.4 Å** VLY^ml = monomer locked via a disulfide	5IMY	Data File Jmol Viewer 5IMY	Lawrence et al. (2016). Lawrence SL, Gorman MA, Feil SC, Mulhern TD, Kuiper MJ, Ratner AJ, Tweten RK, Morton CJ, & Parker MW (2016). Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins. Structure 24 :1488-1498. PubMed Id: 27499440. doi:10.1016/j.str.2016.06.017.
*Pneumolysin (PLY) complex: Streptococcus pneumoniae* B Bacteria (expressed in E. coli), 4.5 Å** cryo-EM structure x-ray structure of PLY_D168A monomer, 2.5 Å: 5AOE x-ray structure of PLY_Δ146/147 monomer, 2.45 Å: 5AOF	5LY6	Data File Jmol Viewer 5LY6 5AOF 5AOE	van Pee et al. (2017). van Pee K, Neuhaus A, D'Imprima E, Mills DJ, Kühlbrandt W, & Yildiz Ö (2017). CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin. Elife 6 :e23644. PubMed Id: 28323617. doi:10.7554/eLife.23644.
*Epsilon toxin (Etx): Clostridium perfringens* B Bacteria (expressed in E. coli), 3.2 Å** cryo-EM structure	6RB9	Data File Jmol Viewer 6RB9	Savva et al. (2019). Savva CG, Clark AR, Naylor CE, Popoff MR, Moss DS, Basak AK, Titball RW, & Bokori-Brown M (2019). The pore structure of Clostridium perfringens epsilon toxin. Nat Commun 10 1. PubMed Id: 31201325. doi:10.1038/s41467-019-10645-8.
*Binary iota toxin complex Ib pore: Clostridium perfringens* B Bacteria (expressed in E. coli), 2.9 Å** cryo-EM structure enzymatic component (Ia) and binding component (Ib) pore with short stem, 2.8 Å: 6KLO enzymatic component (Ia) and binding component (Ib) pore with long stem, 2.9 Å: 6KLW	6KLX	Data File Jmol Viewer 6KLX 6KLW 6KLO	Yamada et al. (2020). Yamada T, Yoshida T, Kawamoto A, Mitsuoka K, Iwasaki K, & Tsuge H (2020). Cryo-EM structures reveal translocational unfolding in the clostridial binary iota toxin complex. Nat Struct Mol Biol 27 3:288-296. PubMed Id: 32123390. doi:10.1038/s41594-020-0388-6.
*binary toxin translocase CDTb in asymmetric tetradecamer conformation: Clostridioides difficile* B Bacteria (expressed in E. coli), 2.8 Å** cryo-EM structure CDTb tetradecamer in symmetric conformation, 3.1 Å: 6UWT translocase CDTb, 3.7 Å: 6UWI receptor binding domain 2 (by x-ray), 2.3 Å: 6UWO	6UWR	Data File Jmol Viewer 6UWR 6UWI 6UWT 6UWO	Xu et al. (2020). Xu X, Godoy-Ruiz R, Adipietro KA, Peralta C, Ben-Hail D, Varney KM, Cook ME, Roth BM, Wilder PT, Cleveland T, Grishaev A, Neu HM, Michel SLJ, Yu W, Beckett D, Rustandi RR, Lancaster C, Loughney JW, Kristopeit A, Christanti S, Olson JW, MacKerell AD, Georges AD, Pozharski E, & Weber DJ (2020). Structure of the cell-binding component of the Clostridium difficile binary toxin reveals a di-heptamer macromolecular assembly. Proc Natl Acad Sci USA 117 2:1049-1058. PubMed Id: 31896582. doi:10.1073/pnas.1919490117.
*binary toxin translocase CDTb with CDTa long-stem pore: Clostridioides difficile* B Bacteria (expressed in E. coli), 2.64 Å** cryo-EM structure pore with short stem, 2.56 Å: 7VNJ CDTa-bound CDTb-pore (short), 3.18 Å: 7YVQ unfolded CDTa-bound CDTb-pore (short), 2.80 Å: 7YVS	7VNN	Data File Jmol Viewer 7VNN 7YVQ 7YVS 7VNJ	Kawamoto et al. (2022). Kawamoto A, Yamada T, Yoshida T, Sato Y, Kato T, & Tsuge H (2022). Cryo-EM structures of the translocational binary toxin complex CDTa-bound CDTb-pore from Clostridioides difficile. Nat Commun 13 1:6119. PubMed Id: 36253419. doi:10.1038/s41467-022-33888-4.
De novo Designed β-barrel Membrane Proteins β-barrel Proteins Designed from First Principles
*de novo designed β-barrel TMB2.3: de novo designed* U Unclassified (expressed in E. coli), NMR structure** de novo designed TMB2.17, crystal structure, 2.07 Å: 6X9Z	6X1K	Data File Jmol Viewer 6X1K 6X9Z	Vorobieva et al. (2021). Vorobieva AA, White P, Liang B, Horne JE, Bera AK, Chow CM, Gerben S, Marx S, Kang A, Stiving AQ, Harvey SR, Marx DC, Khan GN, Fleming KG, Wysocki VH, Brockwell DJ, Tamm LK, Radford SE, & Baker D (2021). De novo design of transmembrane β barrels. Science 371 6531. PubMed Id: 33602829. doi:10.1126/science.abc8182.
Beta-Barrel Membrane Proteins: Porins and Relatives
*Porin: Rhodobacter capsulatus* B Bacteria, 1.8 Å**	2POR	Data File Jmol Viewer 2POR porin	Weiss & Schulz (1992). Weiss MS & Schulz GE (1992). Structure of porin refined at 1.8 Å resolution. J. Mol. Biol. 227 :493-509. PubMed Id: 1328651.
*Porin: Rhodopeudomonas blastica* B Bacteria, 1.96 Å**	1PRN	Data File Jmol Viewer 1PRN outer membrane porin	Kreusch & Schulz (1994). Kreusch A & Schulz GE (1994). Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus. J Mol Biol 243 :891-905. PubMed Id: 7525973. doi:10.1006/jmbi.1994.1690. See also: Kreusch et al. (1994). Kreusch A, Neubüser A, Schiltz E, Weckesser J, & Schulz GE (1994). Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution. Protein Sci 3 :58-63. PubMed Id: 8142898. doi:10.1002/pro.5560030108.
*Porin, E1M/A116K Mutant: Rhodopseudomonas blastica* B Bacteria (expressed in E. coli), 2.19 Å** E1M/E99W/A116W mutant, 1.93 Å: 2PRN E1M/A104W mutant, 1.90 Å: 3PRN E1M/Y96W/S119W mutant, 2.00 Å: 5PRN E1M/K50A/R52A mutant, 2.04 Å: 6PRN E1M/D97A/E99A mutant, 2.25 Å: 7PRN E1M/K50A/R52A/D97A/E99A mutant, 2.30 Å: 8PRN	1BH3	Data File Jmol Viewer 1BH3 6PRN 8PRN 3PRN 5PRN 2PRN 7PRN	Schmid et al. (1998). Schmid B, Maveyraud L, Krömer M, & Schulz GE (1998). Porin mutants with new channel properties. Protein Sci 7 :1603-1611. PubMed Id: 9684893. doi:10.1002/pro.5560070714.
*Porin: Rhodopseudomonas blastica* B Bacteria (expressed in E. coli), 3.00 Å** Positively charged peptide GGGGPKLAKMEKARGGGG inserted in periplasmic turn.	1H6S	Data File Jmol Viewer 1H6S	Bannwarth & Schulz (2002). Bannwarth M & Schulz GE (2002). Asymmetric conductivity of engineered porins. Protein Eng 15 :799-804. PubMed Id: 12468713. doi:10.1093/protein/15.10.799.
*OmpK36 osmoporin: Klebsiella pneumoniae* B Bacteria, 3.2 Å**	1OSM	Data File Jmol Viewer 1OSM OmpK36 osmoporin	Dutzler et al. (1999). Dutzler R, Rummel G, Alberti S, Hernandez-Alles S, Phale P, Rosenbusch J, Benedi V, & Schirmer T (1999). Crystal structure and functional characterization of OmpK36, the osmoporin of Klebsiella pneumoniae. Structure Fold. Des 7 :425-434. PubMed Id: 10196126.
*OmpK36 osmoporin, wild-type: Klebsiella pneumoniae* B Bacteria (expressed in E. coli), 1.98 Å** clinical isolate ST258, 3.23 Å: 6RCP GD insertion chimera, 2.03 Å: 6RCK	6RD3	Data File Jmol Viewer 6RD3 6RCK 6RCP	Wong et al. (2019). Wong JLC, Romano M, Kerry LE, Kwong HS, Low WW, Brett SJ, Clements A, Beis K, & Frankel G (2019). OmpK36-mediated Carbapenem resistance attenuates ST258 Klebsiella pneumoniae in vivo. Nat Commun 10 1. PubMed Id: 31477712. doi:10.1038/s41467-019-11756-y.
*OmpK36 osmoporin, native-SAD structure determined at wavelength 4.13 Å: Klebsiella pneumoniae* B Bacteria (expressed in E. coli), 2.70 Å** X-ray Structure	8PYZ	Data File Jmol Viewer 8PYZ	El Omari et al. (2023). El Omari K, Duman R, Mykhaylyk V, Orr CM, Latimer-Smith M, Winter G, Grama V, Qu F, Bountra K, Kwong HS, Romano M, Reis RI, Vogeley L, Vecchia L, Owen CD, Wittmann S, Renner M, Senda M, Matsugaki N, Kawano Y, Bowden TA, Moraes I, Grimes JM, Mancini EJ, Walsh MA, Guzzo CR, Owens RJ, Jones EY, Brown DG, Stuart DI, Beis K, & Wagner A (2023). Experimental phasing opportunities for macromolecular crystallography at very long wavelengths. Commun Chem 6 1:219. PubMed Id: 37828292. doi:10.1038/s42004-023-01014-0.
*Omp32 anion-selective porin: Comamonas acidovorans* B Bacteria, 2.1 Å**	1E54	Data File Jmol Viewer 1E54 Omp32	Zeth et al. (2000). Zeth K, Diederichs K, Welte W, & Engelhardt H (2000). Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 A resolution. Structure 8 :981-992. PubMed Id: 10986465.
*Omp32 anion-selective porin: Delftia acidovorans* B Bacteria, 1.5 Å** With bound malate, 1.45 Å: 2FGQ	2FGR	Data File Jmol Viewer 2FGR 2FGQ	Zachariae et al. (2006). Zachariae U, Kluhspies T, De S, Engelhardt H, & Zeth K (2006). High resolution crystal structures and molecular dynamics studies reveal substrate binding in the porin omp32. J Biol Chem 281 :7413-7420. PubMed Id: 16434398.
*OmpF Porin: Escherichia coli* B Bacteria, 2.4 Å** Note: Also see BtuB with bound colicin E3 R-domain, below.	2OMF	Data File Jmol Viewer 2OMF	Cowan et al. (1992). Cowan SW, Schirmer T, Rummel G, Steiert M, Ghosh R, Pauptit RA, Jansonius JN, & Rosenbusch JP (1992). Crystal structures explain functional properties of two Escherichia coli porins. Nature 358 :727-733. PubMed Id: 1380671.
*OmpF Porin from colicin-resistant E. coli: Escherichia coli* B Bacteria, 3.00 Å**	1MPF	Data File Jmol Viewer 1MPF	Jeanteur et al. (1994). Jeanteur D, Schirmer T, Fourel D, Simonet V, Rummel G, Widmer C, Rosenbusch JP, Pattus F, & Pagès JM (1994). Structural and functional alterations of a colicin-resistant mutant of OmpF porin from Escherichia coli. Proc Natl Acad Sci USA 91 :10675-10679. PubMed Id: 7524100.
*OmpF Porin: Escherichia coli* B Bacteria, 3.20 Å** Tetragonal crystal form.	1OPF	Data File Jmol Viewer 1OPF OmpF porin	Cowan et al. (1995). Cowan SW, Garavito RM, Jansonius JN, Jenkins JA, Karlsson R, König N, Pai EF, Pauptit RA, Rizkallah PJ, Rosenbusch JP, Rummel G, & Schirmer T (1995). The structure of OmpF porin in a tetragonal crystal form. Structure 3 :1041-1050. PubMed Id: 8589999. doi:10.1016/S0969-2126(01)00240-4.
*OmpF Porin, D113G mutant: Escherichia coli* B Bacteria, 3.50 Å** Deletion Mutant (Δ 109-114), 3.10 Å: 1GFN R132P Mutant, 3.30 Å: 1GFO R42C Mutant, 2.70 Å: 1GFP R82C Mutant, 2.80 Å: 1GFQ	1GFM	Data File Jmol Viewer 1GFM 1GFP 1GFQ 1GFN 1GFO	Lou et al. (1996). Lou KL, Saint N, Prilipov A, Rummel G, Benson SA, Rosenbusch JP, & Schirmer T (1996). Structural and functional characterization of OmpF porin mutants selected for larger pore size. I. Crystallographic analysis. J Biol Chem 271 :20669-20675. PubMed Id: 8702816. doi:10.1074/jbc.271.34.20669 .
*OmpF Porin, D74A mutant: Escherichia coli* B Bacteria (expressed in Escherichia coli B), 3.00 Å**	1BT9	Data File Jmol Viewer 1BT9	Phale et al. (1998). Phale PS, Philippsen A, Kiefhaber T, Koebnik R, Phale VP, Schirmer T, & Rosenbusch JP (1998). Stability of trimeric OmpF porin: the contributions of the latching loop L2. Biochemistry 37 :15663-15670. PubMed Id: 9843370. doi:10.1021/bi981215c.
*OmpF Porin, Y106F Mutant: Escherichia coli* B Bacteria, 2.20 Å** NQAAA (D113N/E117Q/R42A/R82A/R132A) Mutant, 2.40 Å: 1HXT KK (V18K/G131K) Mutant, 3.00 Å: 1HXU	1HXX	Data File Jmol Viewer 1HXX 1HXT 1HXU	Phale et al. (2001). Phale PS, Philippsen A, Widmer C, Phale VP, Rosenbusch JP, & Schirmer T (2001). Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation. Biochemistry 40 :6319-6325. PubMed Id: 11371193. doi:10.1021/bi010046k.
*OmpF Porin: Escherichia coli* B Bacteria, 1.6 Å** With inserted 83 residue N-terminal peptide of colicin E3, 3.0 Å: 2ZLD	2ZFG	Data File Jmol Viewer 2ZFG 2ZLD	Yamashita et al. (2008). Yamashita E, Zhalnina MV, Zakharov SD, Sharma O, & Cramer WA (2008). Crystal structures of the OmpF porin: function in a colicin translocon. EMBO J 27 :2171-2180. PubMed Id: 18636093.
*OmpF porin with a synthetic dibenzo-18-crown-6: Escherichia coli* B Bacteria, 3.40 Å**	3FYX	Data File Jmol Viewer 3FYX	Reitz et al. (2009). Reitz S, Cebi M, Reiss P, Studnik G, Linne U, Koert U, & Essen LO (2009). On the function and structure of synthetically modified porins. Angew Chem Int Ed Engl 48 :4853-4857. PubMed Id: 19322865. doi:10.1002/anie.200900457.
*OmpF Porin in complex with colicin peptide OBS1: Escherichia coli* B Bacteria, 3.01 Å** Shows colicin bound within porin lumen spanning the membrane bilayer	3O0E	Data File Jmol Viewer 3O0E	Housden et al. (2010). Housden NG, Wojdyla JA, Korczynska J, Grishkovskaya I, Kirkpatrick N, Brzozowski AM, & Kleanthous C. (2010). Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF. Proc Natl Acad Sci USA 107 :21412-21417. PubMed Id: 21098297.
*OmpF Porin: Escherichia coli* B Bacteria, 2.61 Å** Cation-selective pathway revealed by anomalous x-ray diffraction. Structure at 3.00 Å: 3HWB	3HW9	Data File Jmol Viewer 3HW9 3HWB	Dhakshnamoorthy et al. (2010). Dhakshnamoorthy B, Raychaudhury S, Blachowicz L, & Roux B (2010). Cation-selective pathway of OmpF porin revealed by anomalous X-ray diffraction. J Mol Biol 396 :293-300. PubMed Id: 19932117. doi:10.1016/j.jmb.2009.11.042.
*OmpF Porin in presence of foscholine-12: Escherichia coli* B Bacteria, 3.79 Å** Structure at 4.39 Å: 3K1B	3K19	Data File Jmol Viewer 3K19 3K1B	Kefala et al. (2010). Kefala G, Ahn C, Krupa M, Esquivies L, Maslennikov I, Kwiatkowski W, & Choe S (2010). Structures of the OmpF porin crystallized in the presence of foscholine-12. Protein Sci 19 :1117-1125. PubMed Id: 20196071. doi:10.1002/pro.369.
*OmpF porin in lipidic cubic phase: Escherichia coli* B Bacteria, 2.80 Å**	3POU	Data File Jmol Viewer 3POU	Efremov & Sazanov (2012). Efremov RG, & Sazanov LA (2012). Structure of Escherichia coli OmpF porin from lipidic mesophase. J Struct Biol 178 3:311-318. PubMed Id: 22484237. doi:10.1016/j.jsb.2012.03.005.
*OmpF Porin: Escherichia coli* B Bacteria, 3.5 Å** I2 space group	4D5U	Data File Jmol Viewer 4D5U	Chaptal et al. (2016). Chaptal V, Kilburg A, Flot D, Wiseman B, Aghajari N, Jault JM, & Falson P (2016). Two different centered monoclinic crystals of the E. coli outer-membrane protein OmpF originate from the same building block. Biochim Biophy Acta 1858 :326-332. PubMed Id: 26620074. doi:10.1016/j.bbamem.2015.11.021.
*OmpF Porin: Escherichia coli* B Bacteria, 2.54 Å** cryo-EM structure	6WTZ	Data File Jmol Viewer 6WTZ	Su et al. (2021). Su CC, Lyu M, Morgan CE, Bolla JR, Robinson CV, & Yu EW (2021). A 'Build and Retrieve' methodology to simultaneously solve cryo-EM structures of membrane proteins. Nat Methods 18 1:69-75. PubMed Id: 33408407. doi:10.1038/s41592-020-01021-2.
*OmpF and BtuB Porin in complex with colicin E9 (colE9): Escherichia coli* E Eukaryota, 4.70 Å** cryo-EM structure ColicinE9 partial translocation complex, 3.70 Å 7NST	7NSU	Data File Jmol Viewer 7NSU 7NST	Francis et al. (2021). Francis MR, Webby MN, Housden NG, Kaminska R, Elliston E, Chinthammit B, Lukoyanova N, & Kleanthous C (2021). Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF. EMBO J 40 21:e108610. PubMed Id: 34515361. doi:10.15252/embj.2021108610.
*Omp35 (OmpF): Enterobacter aerogenes* B Bacteria (expressed in E. coli), 2.85 Å**	5O78	Data File Jmol Viewer 5O78	Acosta-Gutiérrez et al. (2018). Acosta-Gutiérrez S, Ferrara L, Pathania M, Masi M, Wang J, Bodrenko I, Zahn M, Winterhalter M, Stavenger RA, Pagès JM, Naismith JH, van den Berg B, Page MGP, & Ceccarelli M (2018). Getting Drugs into Gram-Negative Bacteria: Rational Rules for Permeation through General Porins. ACS Infect Dis 4 10:1487-1498. PubMed Id: 29962203. doi:10.1021/acsinfecdis.8b00108.
*OmpF Porin: Salmonella typhi* B Bacteria (expressed in E. coli), 2.79 Å**	3NSG	Data File Jmol Viewer 3NSG	Balasubramaniam et al. (2012). Balasubramaniam D, Arockiasamy A, Kumar PD, Sharma A, & Krishnaswamy S (2012). Asymmetric pore occupancy in crystal structure of OmpF porin from Salmonella typhi. J Struc Biol 178 :233-244. PubMed Id: 22525817. doi:10.1016/j.jsb.2012.04.005.
*OmpE35 (OmpF): Enterobacter cloacae* B Bacteria (expressed in E. coli), 2.3 Å**	6ENE	Data File Jmol Viewer 6ENE	Acosta-Gutiérrez et al. (2018). Acosta-Gutiérrez S, Ferrara L, Pathania M, Masi M, Wang J, Bodrenko I, Zahn M, Winterhalter M, Stavenger RA, Pagès JM, Naismith JH, van den Berg B, Page MGP, & Ceccarelli M (2018). Getting Drugs into Gram-Negative Bacteria: Rational Rules for Permeation through General Porins. ACS Infect Dis 4 10:1487-1498. PubMed Id: 29962203. doi:10.1021/acsinfecdis.8b00108.
*OmpK35 (OmpF): Klebsiella pneumoniae* B Bacteria (expressed in E. coli), 1.5 Å**	5O77	Data File Jmol Viewer 5O77	Acosta-Gutiérrez et al. (2018). Acosta-Gutiérrez S, Ferrara L, Pathania M, Masi M, Wang J, Bodrenko I, Zahn M, Winterhalter M, Stavenger RA, Pagès JM, Naismith JH, van den Berg B, Page MGP, & Ceccarelli M (2018). Getting Drugs into Gram-Negative Bacteria: Rational Rules for Permeation through General Porins. ACS Infect Dis 4 10:1487-1498. PubMed Id: 29962203. doi:10.1021/acsinfecdis.8b00108.
*OmpC Osmoporin: Escherichia coli* B Bacteria, 2.0 Å**	2J1N	Data File Jmol Viewer 2J1N	Baslé et al. (2006). Baslé A, Rummel G, Storici P, Rosenbusch J, & Schirmer T (2006). Crystal Structure of Osmoporin OmpC from E. coli at 2.0 Å. J Mol Biol 362 :933-942. PubMed Id: 16949612.
*OmpC Osmoporin clinical variant OmpC06: Escherichia coli* B Bacteria, 2.50 Å** Clinical variant OmpC20, 2.50 Å: 2XE2 Clinical variant OmpC26, 2.28 Å: 2XE5 Clinical variant OmpC28, 2.85 Å: 2XE3 Clinical variant OmpC33, 3.47 Å: 2XG6	2XE1	Data File Jmol Viewer 2XE1 2XE2 2XE3 2XE5 2XG6	Lou et al. (2011). Lou H, Chen M, Black SS, Bushell SR, Ceccarelli M, Mach T, Beis K, Low AS, Bamford VA, Booth IR, Bayley H, & Naismith JH (2011). Altered antibiotic transport in OmpC mutants isolated from a series of clinical strains of multi-drug resistant E. coli. PLoS One 6 :e25825. PubMed Id: 22053181. doi:10.1371/journal.pone.0025825.
*OmpC Osmoporin: Escherichia coli* B Bacteria, 2.56 Å** cryo-EM structure	7JZ3	Data File Jmol Viewer 7JZ3	Su et al. (2021). Su CC, Lyu M, Morgan CE, Bolla JR, Robinson CV, & Yu EW (2021). A 'Build and Retrieve' methodology to simultaneously solve cryo-EM structures of membrane proteins. Nat Methods 18 1:69-75. PubMed Id: 33408407. doi:10.1038/s41592-020-01021-2.
*OmpK36 (OmpC): Klebsiella pneumoniae* B Bacteria (expressed in E. coli), 1.65 Å**	5O79	Data File Jmol Viewer 5O79	Acosta-Gutiérrez et al. (2018). Acosta-Gutiérrez S, Ferrara L, Pathania M, Masi M, Wang J, Bodrenko I, Zahn M, Winterhalter M, Stavenger RA, Pagès JM, Naismith JH, van den Berg B, Page MGP, & Ceccarelli M (2018). Getting Drugs into Gram-Negative Bacteria: Rational Rules for Permeation through General Porins. ACS Infect Dis 4 10:1487-1498. PubMed Id: 29962203. doi:10.1021/acsinfecdis.8b00108.
*Omp36 (OmpC): Klebsiella aerogenes* B Bacteria (expressed in E. coli), 2.47 Å**	5O9C	Data File Jmol Viewer 5O9C	Acosta-Gutiérrez et al. (2018). Acosta-Gutiérrez S, Ferrara L, Pathania M, Masi M, Wang J, Bodrenko I, Zahn M, Winterhalter M, Stavenger RA, Pagès JM, Naismith JH, van den Berg B, Page MGP, & Ceccarelli M (2018). Getting Drugs into Gram-Negative Bacteria: Rational Rules for Permeation through General Porins. ACS Infect Dis 4 10:1487-1498. PubMed Id: 29962203. doi:10.1021/acsinfecdis.8b00108.
*OmpC homolog (OmpE36) with bound lipopolysaccharide (LPS): Enterobacter cloacae* B Bacteria (expressed in E. coli), 1.45 Å**	5FVN	Data File Jmol Viewer 5FVN	Arunmanee et al. (2016). Arunmanee W, Pathania M, Solovyova AS, Le Brun AP, Ridley H, Baslé A, van den Berg B, & Lakey JH (2016). Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis. Proc Natl Acad Sci USA 113 34:E5034-E5043. PubMed Id: 27493217. doi:10.1073/pnas.1602382113.
*OmpG monomeric* porin: Escherichia coli B Bacteria, 2.3 Å**	2F1C	Data File Jmol Viewer 2F1C	Subbarao and van den Berg (2006). Subbarao GV & van den Berg B (2006). Crystal structure of the monomeric porin OmpG. J Mol Biol 360 :750-759. PubMed Id: 16797588.
*OmpG monomeric* porin in open state: Escherichia coli B Bacteria, 2.3 Å** OmpG in closed state, 2.73 Å: 2IWW	2IWV	Data File Jmol Viewer 2IWV 2IWW	Yildiz et al. (2006). Yildiz O, Vinothkumar KR, Goswami P, & Kuhlbrandt W (2006). Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation. EMBO J. 25 :3702-3713. PubMed Id: 16888630.
*OmpG monomeric* porin: Escherichia coli B Bacteria, 2.18 Å** His231A/His261A mutant stable in open state	2X9K	Data File Jmol Viewer 2X9K	Korkmaz-Ozkan et al. (2010). Korkmaz-Özkan F, Köster S, Kühlbrandt W, Mäntele W, & Yildiz O (2010). Correlation between the OmpG secondary structure and its pH-dependent alterations monitored by FTIR. J Mol Biol 401 :56-67. PubMed Id: 20561532. doi:10.1016/j.jmb.2010.06.015.
*OmpG monomeric* porin: Escherichia coli B Bacteria, NMR Structure (DPC micelles)**	2JQY	Data File Jmol Viewer 2JQY	Liang & Tamm (2007). Liang B & Tamm LK (2007). Structure of outer membrane protein G by solution NMR Spectroscopy. Proc Natl Acad Sci USA 104 :16140-16145. PubMed Id: 17911261.
*OmpG monomeric* porin: Escherichia coli B Bacteria, solid-state NMR structure** protein embedded in E. coli lipid extracts	5MWV	Data File Jmol Viewer 5MWV	Retel et al. (2017). Retel JS, Nieuwkoop AJ, Hiller M, Higman VA, Barbet-Massin E, Stanek J, Andreas LB, Franks WT, van Rossum BJ, Vinothkumar KR, Handel L, de Palma GG, Bardiaux B, Pintacuda G, Emsley L, Kühlbrandt W, & Oschkinat H (2017). Structure of outer membrane protein G in lipid bilayers. Nat Commun 8 1:2073. PubMed Id: 29233991. doi:10.1038/s41467-017-02228-2.
*OmpG ΔL6-ΔD215 mutant, "quiet" porin: Escherichia coli* B Bacteria, NMR Structure**	6OQH	Data File Jmol Viewer 6OQH	Sanganna Gari et al. (2019). Sanganna Gari RR, Seelheim P, Liang B, & Tamm LK (2019). Quiet Outer Membrane Protein G (OmpG) Nanopore for Biosensing. ACS Sens 4 5:1230-1235. PubMed Id: 30990011. doi:10.1021/acssensors.8b01645.
*OmpT porin (outer membrane expressed): Vibrio cholerae* B Bacteria, 3.2 Å** in vitro folded (monomeric), 1.66 Å: 6EHD in vitro folded (trimeric), 2.72 Å: 6EHF OmpTΔL8, 2.31 Å: 6EHE	5OYK	Data File Jmol Viewer 5OYK 6EHD 6EHE 6EHF	Pathania et al. (2018). Pathania M, Acosta-Gutierrez S, Bhamidimarri SP, Baslé A, Winterhalter M, Ceccarelli M, & van den Berg B (2018). Unusual Constriction Zones in the Major Porins OmpU and OmpT from Vibrio cholerae. Structure 26 5:708-721.e4. PubMed Id: 29657131. doi:10.1016/j.str.2018.03.010.
*OmpU: Vibrio cholerae* B Bacteria (expressed in E. coli), 2.22 Å**	5ONU	Data File Jmol Viewer 5ONU	Li et al. (2018). Li H, Zhang W, & Dong C (2018). Crystal structure of the outer membrane protein OmpU from Vibrio cholerae at 2.2 Å resolution. Acta Crystallogr D Struct Biol 74 :21-29. PubMed Id: 29372896. doi:10.1107/S2059798317017697.
*OmpU porin: Vibrio cholerae* B Bacteria (expressed in E. coli), 1.55 Å** OmpU ΔN, 2.02 Å: 6EHC	6EHB	Data File Jmol Viewer 6EHB 6EHC	Pathania et al. (2018). Pathania M, Acosta-Gutierrez S, Bhamidimarri SP, Baslé A, Winterhalter M, Ceccarelli M, & van den Berg B (2018). Unusual Constriction Zones in the Major Porins OmpU and OmpT from Vibrio cholerae. Structure 26 5:708-721.e4. PubMed Id: 29657131. doi:10.1016/j.str.2018.03.010.
*PhoE: Escherichia coli* B Bacteria, 3.0 Å**	1PHO	Data File Jmol Viewer 1PHO PhoE phosphoporin	Cowan et al. (1992). Cowan SW, Schirmer T, Rummel G, Steiert M, Ghosh R, Pauptit RA, Jansonius JN, & Rosenbusch JP (1992). Crystal structures explain functional properties of two Escherichia coli porins. Nature 358 :727-733. PubMed Id: 1380671.
*LamB Maltoporin: Salmonella typhimurium* B Bacteria, 2.4 Å**	2MPR	Data File Jmol Viewer 2MPR maltoporin	Meyer et al. (1997). Meyer JEW, Hofnung M, & Schulz GE (1997). Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J. Mol. Biol 266 :761-775. PubMed Id: 9102468.
*LamB Maltoporin: Escherichia coli* B Bacteria, 3.1 Å**	1MAL	Data File Jmol Viewer 1MAL maltoporin	Schirmer et al. (1995). Schirmer T, Keller TA, Wang YF, & Rosenbusch JP (1995). Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science 267 :512-4. PubMed Id: 7824948.
*LamB Maltoporin in complex with maltose: Escherichia coli* B Bacteria, 2.6 Å** In complex with maltotriose, 3.20 Å: 1MPN In complex with maltohexaose, 2.80 Å: 1MPO	1MPM	Data File Jmol Viewer 1MPM 1MPO 1MPN	Dutzler et al. (1996). Dutzler R, Wang YF, Rizkallah P, Rosenbusch JP, Schirmer T (1996). Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure 4 :127-134. PubMed Id: 8805519.
*LamB Maltoporin in complex with sucrose: Escherichia coli* B Bacteria, 2.4 Å** In complex with trehalose, 3.0 Å: 1MPQ	1AF6	Data File Jmol Viewer 1AF6 1MPQ	Wang et al. (1997). Wang YF, Dutzler R, Rizkallah PJ, Rosenbusch JP, & Schirmer T (1997). Channel specificity: structural basis for sugar discrimination and differential flux rates in maltoporin. J Mol Biol 272 :56-63. PubMed Id: 9299337.
*ScrY sucrose-specific porin: Salmonella typhimurium* B Bacteria, 2.4 Å** Complexed Form, 1A0T. Uncomplexed form, 1A0S.	1A0T	Data File Jmol Viewer 1A0T 1A0S porin scrY, sucrose-specific	Forst et al. (1998). Forst D, Welte W, Wacker T, & Diederichs K (1998). Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nature Structural Biol 5 :37-46. PubMed Id: 9437428.
*MspA mycobacterial porin: Mycobacterium smegmatis* B Bacteria, 2.5 Å** Homooctamer	1UUN	Data File Jmol Viewer 1UUN MspA	Faller et al. (2004). Faller M, Niederweis M, & Schulz GE (2004). The structure of a mycobacterial outer-membrane channel. Science 303 :1189-1192. PubMed Id: 14976314.
*OprB carbohydrate-specific transporter at high pH: Pseudomonas putida* B Bacteria (expressed in E. coli), 2.70 Å** low-pH structure, 3.10 Å: 4GF4	4GEY	Data File Jmol Viewer 4GEY 4GF4	van den Berg (2012). van den Berg B (2012). Structural basis for outer membrane sugar uptake in pseudomonads. J Biol Chem 287 :41044-41052. PubMed Id: 23066028. doi:10.1074/jbc.M112.408518.
*OprO diphosphate-specific transporter: Pseudomonas aeruginosa* B Bacteria, 1.52 Å** F62Y/D114Y mutant, 1.54 Å: 4RJX	4RJW	Data File Jmol Viewer 4RJW 4RJX	Modi et al. (2015). Modi N, Ganguly S, Bárcena-Uribarri I, Benz R, van den Berg B, & Kleinekathöfer U (2015). Structure, Dynamics, and Substrate Specificity of the OprO Porin from Pseudomonas aeruginosa. Biophys J 109 :1429-1438. PubMed Id: 26445443. doi:10.1016/j.bpj.2015.07.035.
*OprP phosphate-specific transporter: Pseudomonas aeruginosa* B Bacteria, 1.9 Å** Contains a novel nine-residue arginine ladder	2O4V	Data File Jmol Viewer 2O4V OprP	Moraes et al. (2007). Moraes TF, Bains M, Hancock REW & Strynadka NCJ (2007). An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane. Nature Struc Mol Biol 14 :85-87. PubMed Id: 17187075.
*PorB outer membrane protein, native structure: Neisseria meningitidis* B Bacteria (expressed in E. coli), 2.30 Å** The second most common OMP of Neisseria, PorB is required for pathogenesis. Former 3A2R, 3A2T, and 3A2U superseded by 3VZT, 3VZW, and 3VZU, respectively. In complex with sucrose, 2.20 Å: 3A2S In complex with galactose, 3.20 Å: 3VZW In complex with AMP-PNP, 2.90 Å: 3ZVU	3VZT	Data File Jmol Viewer 3VZT 3A2S 3VZW 3VZU	Tanabe et al. (2010). Tanabe M, Nimigean CM, & Iverson TM (2010). Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Proc Natl Acad Sci USA 107 :6811-6816. PubMed Id: 20351243.
*PorB outer membrane protein: Neisseria meningitidis* B Bacteria (expressed in E. coli), 3.32 Å** Loop 7 mutant, 2.40 Å: 3WI5	3WI4	Data File Jmol Viewer 3WI4 3WI5	Kattner et al. (2014). Kattner C, Toussi DN, Zaucha J, Wetzler LM, Rüppel N, Zachariae U, Massari P, & Tanabe M (2014). Crystallographic analysis of Neisseria meningitidis PorB extracellular loops potentially implicated in TLR2 recognition. J Struct Biol 185 3:440-447. PubMed Id: 24361688. doi:10.1016/j.jsb.2013.12.006.
*PorB outer membrane protein, G103K mutant: Neisseria meningitidis* B Bacteria (expressed in E. coli), 2.76 Å**	7DE8	Data File Jmol Viewer 7DE8	Bartsch et al. (2021). Bartsch A, Ives CM, Kattner C, Pein F, Diehn M, Tanabe M, Munk A, Zachariae U, Steinem C, & Llabrás S (2021). An antibiotic-resistance conferring mutation in a neisserial porin: Structure, ion flux, and ampicillin binding. Biochim Biophys Acta Biomembr 1863 6:183601. PubMed Id: 33675718. doi:10.1016/j.bbamem.2021.183601.
*PorB outer membrane protein: Neisseria gonorrhoeae* B Bacteria, 3.20 Å**	4AUI	Data File Jmol Viewer 4AUI	Zeth et al. (2013). Zeth K, Kozjak-Pavlovic V, Faulstich M, Fraunholz M, Hurwitz R, Kepp O, & Rudel T (2013). Structure and function of the PorB porin from disseminating Neisseria gonorrhoeae. Biochem J 449 3:631-642. PubMed Id: 23095086. doi:10.1042/BJ20121025.
*KdgM monomeric* porin in complex with disordered oligogalacturonate, wild-type: Dickeya dadantii B Bacteria (expressed in E. coli), 2.10 Å** K161S mutant in complex with disordered oligogalacturonate, 2.10 Å: 4PR7	4FQE	Data File Jmol Viewer 4FQE 4PR7	Hutter et al. (2014). Hutter CA, Lehner R, Wirth Ch, Condemine G, Peneff C, & Schirmer T (2014). Structure of the oligogalacturonate-specific KdgM porin. Acta Crystallogr. D Biol. Crystallogr. 70 :1770-1778. PubMed Id: 24914987. doi:10.1107/S1399004714007147.
*CymA monomeric outer membrane protein (NHis-SeMet): Klebsiella oxytoca* B Bacteria (expressed in E. coli), 2.51 Å** NHis-native, 1.83 Å: 4V3H wild-type, 2.30 Å: 4D51 &alfa;-cyclodextrin soak, 1.70 Å: 4D5B β-cyclodextrin soak, 1.90 Å: 4D5D	4V3G	Data File Jmol Viewer 4V3G 4V3H 4D5B 4D5D 4D51	van den Berg et al. (2015). van den Berg B, Prathyusha Bhamidimarri S, Dahyabhai Prajapati J, Kleinekathöfer U, & Winterhalter M (2015). Outer-membrane translocation of bulky small molecules by passive diffusion. Proc Natl Acad Sci USA 112 :E2991-E2999. PubMed Id: 26015567. doi:10.1073/pnas.1424835112.
*COG4313 outer membrane channel: Pseudomonas putida* B Bacteria (expressed in E. coli), 2.30 Å**	4RL8	Data File Jmol Viewer 4RL8	van den Berg et al. (2015). van den Berg B, Bhamidimarri SP, & Winterhalter M (2015). Crystal structure of a COG4313 outer membrane channel. Sci Rep 5 :11927. PubMed Id: 26149193. doi:10.1038/srep11927.
*OprG outer membrane amino acid transporter: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), NMR structure** P92A mutant, NMR structure: 2N6P	2N6L	Data File Jmol Viewer 2N6L 2N6P	Kucharska et al. (2015). Kucharska I, Seelheim P, Edrington T, Liang B, & Tamm LK (2015). OprG Harnesses the Dynamics of its Extracellular Loops to Transport Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa. Structure 23 :2234-2245. PubMed Id: 26655471. doi:10.1016/j.str.2015.10.009.
*MOMP major outer membrane protein: Campylobacter jejuni* (expressed in E. coli), 2.1 Å** expressed in C. jejuni, 2.88 Å: 5LDT	5LDV	Data File Jmol Viewer 5LDV 5LDT	Ferrara et al. (2016). Ferrara LG, Wallat GD, Moynié L, Dhanasekar NN, Aliouane S, Acosta-Gutiérrez S, Pagès JM, Bolla JM, Winterhalter M, Ceccarelli M, & Naismith JH (2016). MOMP from Campylobacter jejuni Is a Trimer of 18-Stranded β-Barrel Monomers with a Ca²⁺ Ion Bound at the Constriction Zone. J Mol Biol 428 :4528-4543. PubMed Id: 27693650. doi:10.1016/j.jmb.2016.09.021.
*Omp-Pst1 type-A porin: Providencia stuartii* B Bacteria (expressed in E. coli), 3.2 Å** Structures reveal that these porins can self-associate to form dimers of trimers Omp-Pst1 type-B, 2.7 Å: 5NXR Omp-Pst1 type-B in complex with maltose, 3 Å: 5NXU Omp-Pst2 reveals dimer of trimers, 2.2 Å: 4D65 283-LGNY-286, steric zipper that supports dimerization of Pst2, 0.997 Å: 5N9H 206-GVVTSE-211 steric zipper that supports dimerization of Pst1, 1.91 Å: 5N9I Pst1 L5 deletion, 3.12 Å: 5NXN	4D64	Data File Jmol Viewer 4D64 5N9I 5NXU 4D65 5NXN 5N9H 5NXR	El-Khatib et al. (2018). El-Khatib M, Nasrallah C, Lopes J, Tran QT, Tetreau G, Basbous H, Fenel D, Gallet B, Lethier M, Bolla JM, Pagès JM, Vivaudou M, Weik M, Winterhalter M, & Colletier JP (2018). Porin self-association enables cell-to-cell contact inProvidencia stuartiifloating communities. Proc Natl Acad Sci USA 115 10:E2220-E2228. PubMed Id: 29476011. doi:10.1073/pnas.1714582115.
*Chitoporin (ChiP), in vitro-folded crystal form I: Vibrio harveyi* B Bacteria (expressed in E. coli), 1.95 Å** in vitro-folded crystal form II, 3.08 Å: 5MDP outer membrane (OM) expressed ChiP, 2.5 Å: 5MDQ with chito-hexose, in vitro-folded 1.9 Å: 5MDR with chito-tetraose OM-expressed, 2.6 Å:5MDS	5MDO	Data File Jmol Viewer 5MDO 5MDP 5MDQ 5MDS 5MDR	Aunkham et al. (2018). Aunkham A, Zahn M, Kesireddy A, Pothula KR, Schulte A, Baslá A, Kleinekathöfer U, Suginta W, & van den Berg B (2018). Structural basis for chitin acquisition by marine Vibrio species. Nat Commun 9 1. PubMed Id: 29335469. doi:10.1038/s41467-017-02523-y.
*FapF amyloid secretion protein FapF_β: Pseudomonas sp. UK4* B Bacteria (expressed in E. coli), 2.5 Å** engineered protein, residues 83-406 (N-terminal domain and following disordered linker removed) F103A mutant, 2.84 Å: 5O67 R157A mutant, 3.08 Å: 5O68	5O65	Data File Jmol Viewer 5O65 5O68 5O67	Rouse et al. (2017). Rouse SL, Hawthorne WJ, Berry JL, Chorev DS, Ionescu SA, Lambert S, Stylianou F, Ewert W, Mackie U, Morgan RML, Otzen D, Herbst FA, Nielsen PH, Dueholm M, Bayley H, Robinson CV, Hare S, & Matthews S (2017). A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis. Nat Commun 8 1. PubMed Id: 28811582. doi:10.1038/s41467-017-00361-6.
*DcaP outer membrane channel: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 2.2 Å**	6EUS	Data File Jmol Viewer 6EUS	Bhamidimarri et al. (2019). Bhamidimarri SP, Zahn M, Prajapati JD, Schleberger C, Söderholm S, Hoover J, West J, Kleinekathöfer U, Bumann D, Winterhalter M, & van den Berg B (2019). A Multidisciplinary Approach toward Identification of Antibiotic Scaffolds for Acinetobacter baumannii. Structure 27 2:268-280.e6. PubMed Id: 30554842. doi:10.1016/j.str.2018.10.021.
*MtrAB electron transporter complex: Shewanella baltica* B Bacteria (expressed in Shewanella oneidensis), 2.70 Å** MtrC, 2.29 Å: 6QYC	6R2Q	Data File Jmol Viewer 6R2Q 6QYC	Edwards et al. (2020). Edwards MJ, White GF, Butt JN, Richardson DJ, & Clarke TA (2020). The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire. Cell 181 3:665-673.e10. PubMed Id: 32289252. doi:10.1016/j.cell.2020.03.032.
Outer Membrane Carboxylate Channels (Occ) These outer membrane proteins require substrates to have a carboxyl group for efficient transport. OccD channels are selective for basic amino acids. OccK channels prefer cyclic substrates. See Eren et al. (2012).
*OccD1 (OprD) basic amino acid uptake channel: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.9 Å**	2ODJ	Data File Jmol Viewer 2ODJ	Biswas et al. (2007). Biswas S, Mohammad MM, Patel DR, Movileanu L, & van den Berg B (2007). Structural insight into OprD substrate specificity. Nature Struct Mol Biol 14 :1108-1109. PubMed Id: 17952093.
*OccD1 (OprD) basic amino acid uptake channel: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.15 Å**	3SY7	Data File Jmol Viewer 3SY7	Eren et al. (2012). Eren E, Vijayaraghavan J, Liu J, Cheneke BR, Touw DS, Lepore BW, Indic M, Movileanu L, & van den Berg B (2012). Substrate Specificity within a Family of Outer Membrane Carboxylate Channels. PLoS Biol 10 :e1001242. PubMed Id: 22272184. doi:10.1371/journal.pbio.1001242.
*OccD2 (OpdC) basic amino acid uptake channel: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.80 Å**	3SY9	Data File Jmol Viewer 3SY9	Eren et al. (2012). Eren E, Vijayaraghavan J, Liu J, Cheneke BR, Touw DS, Lepore BW, Indic M, Movileanu L, & van den Berg B (2012). Substrate Specificity within a Family of Outer Membrane Carboxylate Channels. PLoS Biol 10 :e1001242. PubMed Id: 22272184. doi:10.1371/journal.pbio.1001242.
*OccD3 (OpdP) basic amino acid uptake channel: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.70 Å**	3SYB	Data File Jmol Viewer 3SYB	Eren et al. (2012). Eren E, Vijayaraghavan J, Liu J, Cheneke BR, Touw DS, Lepore BW, Indic M, Movileanu L, & van den Berg B (2012). Substrate Specificity within a Family of Outer Membrane Carboxylate Channels. PLoS Biol 10 :e1001242. PubMed Id: 22272184. doi:10.1371/journal.pbio.1001242.
*OccK1 (OpdK) benzoate channel: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.8 Å** Binds vanillate. Forms labile trimer.	2QTK	Data File Jmol Viewer 2QTK	Biswas et al. (2008). Biswas S, Mohammad MM, Movileanu L, & van den Berg B (2008). Crystal structure of the outer membrane protein OpdK from Pseudomonas aeruginosa. Structure 16 :1027-1035. PubMed Id: 18611376.
*OccK1 (OpdK) benzoate channel: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 1.65 Å**	3SYS	Data File Jmol Viewer 3SYS	Eren et al. (2012). Eren E, Vijayaraghavan J, Liu J, Cheneke BR, Touw DS, Lepore BW, Indic M, Movileanu L, & van den Berg B (2012). Substrate Specificity within a Family of Outer Membrane Carboxylate Channels. PLoS Biol 10 :e1001242. PubMed Id: 22272184. doi:10.1371/journal.pbio.1001242.
*OccK2 (OpdF) glucuronate channel: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.30 Å**	3SZD	Data File Jmol Viewer 3SZD	Eren et al. (2012). Eren E, Vijayaraghavan J, Liu J, Cheneke BR, Touw DS, Lepore BW, Indic M, Movileanu L, & van den Berg B (2012). Substrate Specificity within a Family of Outer Membrane Carboxylate Channels. PLoS Biol 10 :e1001242. PubMed Id: 22272184. doi:10.1371/journal.pbio.1001242.
*OccK3 (OpdO) aromatic hydrocarbon channel: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 1.45 Å**	3SZV	Data File Jmol Viewer 3SZV	Eren et al. (2012). Eren E, Vijayaraghavan J, Liu J, Cheneke BR, Touw DS, Lepore BW, Indic M, Movileanu L, & van den Berg B (2012). Substrate Specificity within a Family of Outer Membrane Carboxylate Channels. PLoS Biol 10 :e1001242. PubMed Id: 22272184. doi:10.1371/journal.pbio.1001242.
*OccK4 (OpdL) aromatic hydrocarbon channel: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.10 Å**	3T0S	Data File Jmol Viewer 3T0S	Eren et al. (2012). Eren E, Vijayaraghavan J, Liu J, Cheneke BR, Touw DS, Lepore BW, Indic M, Movileanu L, & van den Berg B (2012). Substrate Specificity within a Family of Outer Membrane Carboxylate Channels. PLoS Biol 10 :e1001242. PubMed Id: 22272184. doi:10.1371/journal.pbio.1001242.
*OccK5 (OpdH) aromatic hydrocarbon channel: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.60 Å**	3T20	Data File Jmol Viewer 3T20	Eren et al. (2012). Eren E, Vijayaraghavan J, Liu J, Cheneke BR, Touw DS, Lepore BW, Indic M, Movileanu L, & van den Berg B (2012). Substrate Specificity within a Family of Outer Membrane Carboxylate Channels. PLoS Biol 10 :e1001242. PubMed Id: 22272184. doi:10.1371/journal.pbio.1001242.
*OccK6 (OpdQ) aromatic hydrocarbon channel: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.35 Å**	3T24	Data File Jmol Viewer 3T24	Eren et al. (2012). Eren E, Vijayaraghavan J, Liu J, Cheneke BR, Touw DS, Lepore BW, Indic M, Movileanu L, & van den Berg B (2012). Substrate Specificity within a Family of Outer Membrane Carboxylate Channels. PLoS Biol 10 :e1001242. PubMed Id: 22272184. doi:10.1371/journal.pbio.1001242.
*BenF-like Porin (putative) benzoate channel: Pseudomonas fluorescens* B Bacteria, 2.60 Å** Probably belongs to OccK subfamily	3JTY	Data File Jmol Viewer 3JTY	Sampathkumar et al. (2010). Sampathkumar P, Lu F, Zhao X, Li Z, Gilmore J, Bain K, Rutter ME, Gheyi T, Schwinn KD, Bonanno JB, Pieper U, Fajardo JE, Fiser A, Almo SC, Swaminathan S, Chance MR, Baker D, Atwell S, Thompson DA, Emtage JS, Wasserman SR, Sali A, Sauder JM, &Burley SK (2010). Structure of a putative BenF-like porin from Pseudomonas fluorescens Pf-5 at 2.6 Å resolution. Proteins 78 :3056-3062. PubMed Id: 20737437.
*OccAB1 outer membrane channel: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 2.05 Å**	5DL5	Data File Jmol Viewer 5DL5	Zahn et al. (2016). Zahn M, Bhamidimarri SP, Baslé A, Winterhalter M, & van den Berg B (2016). Structural Insights into Outer Membrane Permeability of Acinetobacter baumannii. Structure 24 :221-231. PubMed Id: 26805524. doi:10.1016/j.str.2015.12.009.
*OccAB2 outer membrane channel: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 2.9 Å**	5DL6	Data File Jmol Viewer 5DL6	Zahn et al. (2016). Zahn M, Bhamidimarri SP, Baslé A, Winterhalter M, & van den Berg B (2016). Structural Insights into Outer Membrane Permeability of Acinetobacter baumannii. Structure 24 :221-231. PubMed Id: 26805524. doi:10.1016/j.str.2015.12.009.
*OccAB3 outer membrane channel: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 1.75 Å**	5DL7	Data File Jmol Viewer 5DL7	Zahn et al. (2016). Zahn M, Bhamidimarri SP, Baslé A, Winterhalter M, & van den Berg B (2016). Structural Insights into Outer Membrane Permeability of Acinetobacter baumannii. Structure 24 :221-231. PubMed Id: 26805524. doi:10.1016/j.str.2015.12.009.
*OccAB4 outer membrane channel: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 2.2 Å**	5DL8	Data File Jmol Viewer 5DL8	Zahn et al. (2016). Zahn M, Bhamidimarri SP, Baslé A, Winterhalter M, & van den Berg B (2016). Structural Insights into Outer Membrane Permeability of Acinetobacter baumannii. Structure 24 :221-231. PubMed Id: 26805524. doi:10.1016/j.str.2015.12.009.
Beta-Barrel Membrane Proteins: Monomeric/Dimeric
*TolC outer membrane protein: Escherichia coli* B Bacteria, 2.1 Å** NOTE: Functional protein is a homotrimer. Each monomer contributes 4 strands to a single barrel.	1EK9	Data File Jmol Viewer 1EK9 outer membrane protein TolC	Koronakis et al. (2000). Koronakis V, Sharff A, Koronakis E, Luisi B, & Hughes C (2000). Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405 :914-919. PubMed Id: 10879525.
*TolC outer membrane protein, ligand blocked: Escherichia coli* B Bacteria, 2.75 Å**	1TQQ	Data File Jmol Viewer 1TQQ	Higgins et al. (2004). Higgins MK, Eswaran J, Edwards P, Schertler GF, Hughes C, & Koronakis V (2004). Structure of the ligand-blocked periplasmic entrance of the bacterial multidrug efflux protein TolC. J Mol Biol 342 :697-702. PubMed Id: 15342230.
*TolC outer membrane protein (Y362F, R367E), partially open state: Escherichia coli* B Bacteria, 3.2 Å** 2VDE is P2₁2₁2₁ form. C2 form, 3.30 Å: 2VDD	2VDE	Data File Jmol Viewer 2VDE 2VDD	Bavro et al. (2008). Bavro VN, Pietras Z, Furnham N, Pérez-Cano L, Fernández-Recio J, Pei XY, Misra R, & Luisi B (2008). Assembly and channel opening in a bacterial drug efflux machine. Mol Cell 30 :114-121. PubMed Id: 18406332.
*TolC outer membrane protein in a nanodisc with colicin E1 fragment: Escherichia coli* B Bacteria, 3.09 Å** cryo-EM structure TolC alone, 2.84 Å 6WXI	6WXH	Data File Jmol Viewer 6WXH 6WXI	Budiardjo et al. (2022). Budiardjo SJ, Stevens JJ, Calkins AL, Ikujuni AP, Wimalasena VK, Firlar E, Case DA, Biteen JS, Kaelber JT, & Slusky JSG (2022). Colicin E1 opens its hinge to plug TolC. Elife 11 :e73297. PubMed Id: 35199644. doi:10.7554/eLife.73297.
*TolC outer membrane protein in complex with KlebC: Klebsiella quasipneumoniae* B Bacteria (expressed in E. coli), 3.20 Å** cryo-EM structure Trimeric efflux pump alone, 3.30 Å 7NG9 x-ray structure: KlebC, 1.90 Å 7NNA	7NG8	Data File Jmol Viewer 7NG8 7NNA 7NG9	Housden et al. (2021). Housden NG, Webby MN, Lowe ED, El-Baba TJ, Kaminska R, Redfield C, Robinson CV, & Kleanthous C (2021). Toxin import through the antibiotic efflux channel TolC. Nat Commun 12 1:4625. PubMed Id: 34330923. doi:10.1038/s41467-021-24930-y.
*CmeC bacterial multi-drug efflux transporter outer membrane channel: Campylobacter jejuni* B Bacteria, 2.37 Å**	4MT4	Data File Jmol Viewer 4MT4	Su et al. (2014). Su CC, Radhakrishnan A, Kumar N, Long F, Bolla JR, Lei HT, Delmar JA, Do SV, Chou TH, Rajashankar KR, Zhang Q, & Yu EW (2014). Crystal structure of the Campylobacter jejuni CmeC outer membrane channel. Protein Sci 23 7:954-961. PubMed Id: 24753291. doi:10.1002/pro.2478.
*VceC outer membrane protein: Vibrio cholerae* B Bacteria, 1.8 Å** NOTE: Functional protein is a homotrimer. Each monomer contributes 4 strands to a single barrel.	1YC9	Data File Jmol Viewer 1YC9	Federici et al. (2005). Federici L, Du D, Walas F, Matsumura H, Fernandez-Recio J, McKeegan KS, Borges-Walmsley MI, Luisi BF, & Walmsley AR (2005). The Crystal Structure of the Outer Membrane Protein VceC from the Bacterial Pathogen Vibrio cholerae at 1.8 A Resolution. J Biol Chem 280 :15307-15314. PubMed Id: 15684414.
*OprM drug discharge outer membrane protein: Pseudomonas aeruginosa* B Bacteria, 2.56 Å** Functional protein is a homotrimer. Each monomer contributes 4 strands to a single barrel. H32 space group. OprM is the discharge channel for the tripartite efflux complex MexAB-OprM. The structures of MexB (the inner membrane efflux pump) and MexA (periplasmic fusion protein) are known. See 2V50 and 1T5E, respectively. See 6IOK for structure of entire complex.	1WP1	Data File Jmol Viewer 1WP1	Akama et al. (2004). Akama H, Kanemaki M, Yoshimura M, Tsukihara T, Kashiwagi T, Yoneyama H, Narita S, Nakagawa A, & Nakae T (2004). Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end. J Biol Chem 279 :52816-52819. PubMed Id: 15507433.
*OprM drug discharge outer membrane protein: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.40 Å** Structure of OprM in a non-symmetrical space group, P2₁2₁2₁	3D5K	Data File Jmol Viewer 3D5K	Phan et al. (2010). Phan G, Benabdelhak H, Lascombe MB, Benas P, Rety S, Picard M, Ducruix A, Etchebest C, & Broutin I (2010). Structural and dynamical insights into the opening mechanism of P. aeruginosa OprM channel. Structure 18 :507-517. PubMed Id: 20399187.
*OprN drug discharge outer membrane protein, I4 space group: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 1.69 Å** P321 space group, 2.70 Å: 5AZP	5AZO	Data File Jmol Viewer 5AZO 5AZP	Yonehara et al. (2016). Yonehara R, Yamashita E, & Nakagawa A (2016). Crystal structures of OprN and OprJ, outer membrane factors of multidrug tripartite efflux pumps of Pseudomonas aeruginosa. Proteins 84 6:759-769. PubMed Id: 26914226. doi:10.1002/prot.25022.
*OprJ drug discharge outer membrane protein: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 3.10 Å**	5AZS	Data File Jmol Viewer 5AZS	Yonehara et al. (2016). Yonehara R, Yamashita E, & Nakagawa A (2016). Crystal structures of OprN and OprJ, outer membrane factors of multidrug tripartite efflux pumps of Pseudomonas aeruginosa. Proteins 84 6:759-769. PubMed Id: 26914226. doi:10.1002/prot.25022.
*ST50 discharge outer membrane protein: Salmonella enterica* B Bacteria (expressed in E. coli), 2.98 Å** Functional protein is a homotrimer. Each monomer contributes 4 strands to a single barrel.	5BUN	Data File Jmol Viewer 5BUN	Guan et al. (2015). Guan HH, Yoshimura M, Chuankhayan P, Lin CC, Chen NC, Yang MC, Ismail A, Fun HK, & Chen CJ (2015). Crystal structure of an antigenic outer-membrane protein from Salmonella Typhi suggests a potential antigenic loop and an efflux mechanism. Sci Rep 5 :16441. PubMed Id: 26563565. doi:10.1038/srep16441.
*CusC heavy metal discharge outer membrane protein: Escherichia coli* B Bacteria, 2.30 Å** NOTE: Functional protein is a homotrimer. Each monomer contributes 4 strands to a single barrel. H32 space group.	3PIK	Data File Jmol Viewer 3PIK	Kulathila et al. (2011). Kulathila R, Kulathila R, Indic M, & van den Berg B (2011). Crystal structure of Escherichia coli CusC, the outer membrane component of a heavy metal efflux pump. PLoS One 6 :e15610. PubMed Id: 21249122. doi:10.1371/journal.pone.0015610.
*CusC heavy metal discharge outer membrane protein: Escherichia coli* B Bacteria, 2.09 Å** ΔC1 mutant, 2.53 Å: 4K7K C1S mutant, 2.69 Å: 4K34	4K7R	Data File Jmol Viewer 4K7R 4K7K 4K34	Lei et al. (2014). Lei HT, Bolla JR, Bishop NR, Su CC, & Yu EW (2014). Crystal Structures of CusC Review Conformational Changes Accompanying Folding and Transmembrane Channel Formation. J Mol Biol 426 :403-411. PubMed Id: 24099674. doi:10.1016/j.jmb.2013.09.042.
*apo BtuB cobalamin transporter: Escherichia coli* B Bacteria, 2.0 Å** Related structures: 1NQF (SeMet-BtuB), 1NQG (Ca²⁺-BtuB), 1NQH (Ca²⁺-B₁₂-BtuB).	1NQE	Data File Jmol Viewer 1NQE 1NQG 1NQH 1NQF vitamin B12 receptor	Chimento et al. (2003). Chimento DP, Mohanty AK, Kadner RJ, & Wiener MC (2003). Substrate-induced transmembrane signaling in the cobalamin transporter BtuB. Nat Struct Biol. 10 :394-401. PubMed Id: 12652322.
*BtuB with bound colicin E3 R-domain: Escherichia coli* B Bacteria, 2.75 Å** NOTE: The 135-residue coiled-coil R-domain is believed to deliver the colicin to OmpF (above).	1UJW	Data File Jmol Viewer 1UJW	Kurisu et al. (2003). Kurisu G, Zakharov SD, Zhalnina MV, Bano S, Eroukova VY, Rokitskaya TI, Antonenko YN, Wiener MC, & Cramer WA (2003). The structure of BtuB with bound colicin E3 R-domain implies a translocon. Nat. Struct. Biol. 10 :948-954. PubMed Id: 14528295.
*apo BtuB by in meso* crystallization: Escherichia coli B Bacteria, 1.95 Å** NOTE: Crystals were prepared from cubic phase lipids. This is the first β-barrel protein prepared by this method.	2GUF	Data File Jmol Viewer 2GUF	Cherezov et al. (2006). Cherezov V, Yamashita E, Liu W, Zhalnina M, Cramer WA & Caffrey M (2006). In meso structure of the cobalamin transporter, BtuB, at 1.95 Å resolution. J Mol Biol 364 :716-734. PubMed Id: 17028020.
*BtuB in complex with TonB: Escherichia coli* B Bacteria, 2.1 Å**	2GSK	Data File Jmol Viewer 2GSK	Shultis et al. (2006). Shultis DD, Purdy MD, Banchs CN, & Wiener MC (2006). Outer membrane active transport: structure of the BtuB:TonB complex. Science 312 :1396-1399. PubMed Id: 16741124.
*BtuB with bound colicin E2 R-domain: Escherichia coli* B Bacteria, 3.50 Å**	2YSU	Data File Jmol Viewer 2YSU	Sharma et al. (2007). Sharma O, Yamashita E, Zhalnina MV, Zakharov SD, Datsenko KA, Wanner BL, & Cramer WA (2007). Structure of the complex of the colicin E2 R-domain and its BtuB receptor. The outer membrane colicin translocon. J Biol Chem 282 :23163-23170. PubMed Id: 17548346.
*apo BtuB V10R1 spin-labeled: Escherichia coli* B Bacteria, 2.44 Å** Spin-labeled BtuB V10R1 with bound calcium and cyanocobalamin, 2.44 Å: 3M8D	3M8B	Data File Jmol Viewer 3M8B 3M8D	Freed et al. (2010). Freed DM, Horanyi PS, Wiener MC, & Cafiso DS (2010). Conformational exchange in a membrane transport protein is altered in protein crystals. Biophys J 99 :1604-1610. PubMed Id: 20816073. doi:10.1016/j.bpj.2010.06.026.
*Colicin I receptor Cir in complex with Colicin Ia binding domain: Escherichia coli* B Bacteria, 2.5 Å** Cir Colicin I receptor alone, 2.65 Å: 2HDF	2HDI	Data File Jmol Viewer 2HDI 2HDF	Buchanan et al. (2007). Buchanan S, Lukacik P, Grizot S, Ghirlando R, Ali MMU, Barnard TJ, Jakes S, Kienker PK, & Esser L. (2007). Structure of colicin I receptor bound to the R-domain of colicin Ia: Implications for protein import. EMBO J 26 :2594-2604. PubMed Id: 17464289.
*OmpA: Escherichia coli* B Bacteria, 2.50 Å**	1BXW	Data File Jmol Viewer 1BXW OmpA	Pautsch & Schulz (1998). Pautsch A & Schulz GE (1998). Structure of the outer membrane protein A transmembrane domain. Nature Struct Biol 5 :1013-1017. PubMed Id: 9808047.
*OmpA: Escherichia coli* B Bacteria, 1.60 Å**	1QJP	Data File Jmol Viewer 1QJP OmpA	Pautsch & Schulz (2000). Pautsch A & Schulz GE (2000). High-resolution structure of the OmpA membrane domain. J Mol Biol 298 :273-282. PubMed Id: 10764596.
*OmpA: Escherichia coli* B Bacteria, NMR Structure** in DPC micelles	1G90	Data File Jmol Viewer 1G90 OmpA	Arora et al. (2001). Arora A, Abildgaard F, Bushweller JH, & Tamm LK (2001). Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nature Structural Biol. 8 :334-338. PubMed Id: 11276254.
*OmpA: Escherichia coli* B Bacteria, NMR structure** DPC micelles. High-resolution structure determined using residual dipolar couplings.	2GE4	Data File Jmol Viewer 2GE4	Cierpicki et al. (2006). Cierpicki T, Liang B, Tamm LK, & Bushweller JH (2006). Increasing the accuracy of solution NMR structures of membrane proteins by application of residual dipolar couplings. High-resolution structure of outer membrane protein A. J Am Chem Soc 128 :6947-6951. PubMed Id: 16719475.
*OmpA with four shortened loops: Escherichia coli* B Bacteria, NMR Structure** DHPC micelles. Called β-barrel platform (BBP).	2JMM	Data File Jmol Viewer 2JMM	Johansson et al. (2007). Johansson MU, Alioth S, Hu K, Walser R, Koebnik R, & Pervushin K (2007). A minimal transmembrane β-barrel platform protein studied by nuclear magnetic resonance. Biochemistry 46 :1128-1140. PubMed Id: 17260943.
*OmpA: Klebsiella pneumoniae* B Bacteria (expressed in E. coli), NMR Structure** DHPC micelles	2K0L	Data File Jmol Viewer 2K0L	Renault et al. (2009). Renault M, Saurel O, Czaplicki J, Demange P, Gervais V, Löhr F, Réat V, Piotto M, & Milon A (2009). Solution state NMR structure and dynamics of KpOmpA, a 210 residue transmembrane domain possessing a high potential for immunological applications J Mol Biol 385 :117-130. PubMed Id: 18952100. doi:10.1016/j.jmb.2008.10.021.
*OmpT outer membrane protease: Escherichia coli* B Bacteria, 2.6 Å**	1I78	Data File Jmol Viewer 1I78 OmpT	Vandeputte-Rutten et al. (2001). Vandeputte-Rutten L, Kramer RA, Kroon J, Dekker N, Egmond, MR, & Gros P (2001). Crystal structure of the outer membrane protease OmpT from Eschericia coli suggests a novel catalytic site. EMBO J 20 :5033-5039. PubMed Id: 11566868.
*Pla Plasminogen activator (native 1): Yersinia pestis* B Bacteria (expressed in E. coli), 1.90 Å** Wild-type (Native 2), 2.30 Å: 2X56 D86A mutant, 2.55 Å: 2X4M	2X55	Data File Jmol Viewer 2X55 2X56 2X4M	Eren et al. (2010). Eren E, Murphy M, Goguen J, & van den Berg B. (2010). An active site water network in the plasminogen activator Pla from Yersinia pestis. Structure 18 :809-818. PubMed Id: 20637417.
*OmpW outer membrane protein: Escherichia coli* B Bacteria, 2.7 Å** 2F1V is orthorhomibic form. Trigonal form, 3.0 Å: 2F1T	2F1V	Data File Jmol Viewer 2F1V 2F1T OmpW	Hong et al. (2006). Hong H, Patel DR, Tamm LK, & van den Berg B (2006). The Outer Membrane Protein OmpW Forms an Eight-stranded beta-Barrel with a Hydrophobic Channel. J Biol Chem 281 :7568-7577. PubMed Id: 16414958.
*OmpW outer membrane protein: Escherichia coli* B Bacteria, NMR structure** 30-Fos detergent	2MHL	Data File Jmol Viewer 2MHL	Horst et al. (2014). Horst R, Stanczak P, & Wüthrich K (2014). NMR polypeptide backbone conformation of the E. coli outer membrane protein W. Structure 22 :1204-1209. PubMed Id: 25017731. doi:10.1016/j.str.2014.05.016.
*AlkL passive importer of hydrophobic molecules in DMPC lipid bilayer: Pseudomonas oleovorans* B Bacteria (expressed in E. coli), NMR structure** Solution NMR structure, 6QAM	6QWR	Data File Jmol Viewer 6QWR 6QAM	Schubeis et al. (2020). Schubeis T, Le Marchand T, Daday C, Kopec W, Tekwani Movellan K, Stanek J, Schwarzer TS, Castiglione K, de Groot BL, Pintacuda G, & Andreas LB (2020). A β-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL. Proc Natl Acad Sci USA 117 35:21014-21021. PubMed Id: 32817429. doi:10.1073/pnas.2002598117.
*CarO outer membrane protein, isoform 1: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 2.70 Å** isoform 2, 2.70 Å: 4RLB isoform 3, 2.15 Å: 4FUV	4RL9	Data File Jmol Viewer 4RL9 4RLB 4FUV	Zahn et al. (2015). Zahn M, D'Agostino T, Eren E, Baslé A, Ceccarelli M, & van den Berg B (2015). Small-Molecule Transport by CarO, an Abundant Eight-Stranded β-Barrel Outer Membrane Protein from Acinetobacter baumannii. J Mol Biol 427 :2329-2339. PubMed Id: 25846137. doi:10.1016/j.jmb.2015.03.016.
*OprF outer membrane protein, N-terminal β-barrel domain: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 1.6 Å**	4RLC	Data File Jmol Viewer 4RLC	Zahn et al. (2015). Zahn M, D'Agostino T, Eren E, Baslé A, Ceccarelli M, & van den Berg B (2015). Small-Molecule Transport by CarO, an Abundant Eight-Stranded β-Barrel Outer Membrane Protein from Acinetobacter baumannii. J Mol Biol 427 :2329-2339. PubMed Id: 25846137. doi:10.1016/j.jmb.2015.03.016.
*OprG outer membrane protein: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.4 Å** Potential channel for hydrophobic molecule transport	2X27	Data File Jmol Viewer 2X27	Touw et al. (2010). Touw DS, Patel DR, & van den Berg B (2010). The crystal structure of OprG from Pseudomonas aeruginosa, a potential channel for transport of hydrophobic molecules across the outer membrane. PLoS One 5 :e15016. PubMed Id: 21124774. doi:10.1371/journal.pone.0015016.
*OprH, outer membrane protein H: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), NMR Structure** Structure determined in DHPC micelles. Eight strands. Chemical-shift measurements identify likely lipopolysaccharide interaction sites.	2LHF	Data File Jmol Viewer 2LHF	Edrington et al. (2011). Edrington TC, Kintz E, Goldberg JB, & Tamm LK (2011). Structural Basis for the Interaction of Lipopolysaccharide with Outer Membrane Protein H (OprH) from Pseudomonas aeruginosa J Biol Chem 286 :39211-39223. PubMed Id: 21865172. doi:10.1074/jbc.M111.280933.
*OmpX: Escherichia coli* B Bacteria, 1.9 Å** Structure at 2.1 Å, 1QJ9	1QJ8	Data File Jmol Viewer 1QJ8 1QJ9 OmpX	Vogt & Schulz (1999). Vogt J & Schulz GE (1999). The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence. Structure Fold.Des. 7 :1301-1309. PubMed Id: 10545325.
*OmpX: Escherichia coli* B Bacteria, NMR (DHPC micelles)**	1ORM	Data File Jmol Viewer 1ORM	Fernández et al. (2001). Fernández C, Adeishvili K, & Wüthrich K (2001). Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles. Proc Natl Acad Sci USA 98 :2358-2363. PubMed Id: 11226244.
*OmpX: Escherichia coli* B Bacteria, NMR (DPC micelles, with H-bond constraints)** For structure without H-bond constraints, see 1Q9G	1Q9F	Data File Jmol Viewer 1Q9F 1Q9G	Fernández et al. (2004). Fernández C, Hilty C, Wider G, Guntert P, & Wüthrich K (2004). NMR structure of the integral membrane protein OmpX. J Mol Biol. 336 :1211-1221. PubMed Id: 15037080.
*OmpX in optimized nanodiscs: Escherichia coli* B Bacteria, NMR Structure** In DPC micelles, NMR Structure: 2M07	2M06	Data File Jmol Viewer 2M06 2M07	Hagn et al. (2013). Hagn F, Etzkorn M, Raschle T, & Wagner G (2013). Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins. J Am Chem Soc 135 :1919-1925. PubMed Id: 23294159. doi:10.1021/ja310901f.
*Ail adhesion protein: Yersinia pestis* B Bacteria (expressed in E. coli), 1.80 Å** In complex with sucrose octasulfate (SOS), 1.85 Å: 3QRC	3QRA	Data File Jmol Viewer 3QRA 3QRC	Yamashita et al. (2011). Yamashita S, Lukacik P, Barnard TJ, Noinaj N, Felek S, Tsang TM, Krukonis ES, Hinnebusch BJ, & Buchanan SK (2011). Structural Insights into Ail-Mediated Adhesion in Yersinia pestis. Structure 19 :1672-1682. PubMed Id: 22078566. doi:10.1016/j.str.2011.08.010.
*Ail adhesion protein, decylphosphocholine micelles: Yersinia pestis* B Bacteria (expressed in E. coli), NMR structure** in decylphosphocholine micelles calculated with implicit membrane solvation, NMR structure: 2N2L	2N2M	Data File Jmol Viewer 2N2M 2N2L	Marassi et al. (2015). Marassi FM, Ding Y, Schwieters CD, Tian Y, & Yao Y (2015). Backbone structure of Yersinia pestis Ail determined in micelles by NMR-restrained simulated annealing with implicit membrane solvation. J Biomol NMR 63 :59-65. PubMed Id: 26143069. doi:10.1007/s10858-015-9963-2.
*Ail adhesion protein: Yersinia pestis* B Bacteria (expressed in E. coli), NMR structure** Structure of protein in phospholipid nano-disc. Examines the effect of KDO2-lipid A.	5VJ8	Data File Jmol Viewer 5VJ8	Dutta et al. (2017). Dutta SK, Yao Y, & Marassi FM (2017). Structural Insights into the Yersinia pestis Outer Membrane Protein Ail in Lipid Bilayers. J Phys Chem B 121 :7561-7570. PubMed Id: 28726410. doi:10.1021/acs.jpcb.7b03941.
*TtoA Outer Membrane Protein (OMP): Thermus thermophilus HB27* B Bacteria, 2.8 Å** First structure of an OMP from a thermophile	3DZM	Data File Jmol Viewer 3DZM	Brosig et al. (2009). Brosig A, Nesper J, Boos W, Welte W, & Diederichs K (2009). Crystal structure of a major outer membrane protein from Thermus thermophilus HB27. J Mol Biol 385 :1445-1455. PubMed Id: 19101566.
*OmpLA (PldA) outer membrane phospholipase A monomer: Escherichia coli* B Bacteria, 2.17 Å** Dimer, 2.10 Å: 1QD6	1QD5	Data File Jmol Viewer 1QD5 1QD6 outer membrane phospholipase A	Snijder et al. (1999). Snijder HJ, Ubarretxena-Belandia I, Blaauw M, Kalk KH, Verheij HM, Egmond MR, Dekker N, & Dijkstra BW (1999). Structural evidence for dimerization-regulated activation of an integral membrane phospholipase. Nature 401 :717-721. PubMed Id: 10537112.
*OmpLA (PldA) outer membrane phospholipase A monomer with Ca⁺⁺: Escherichia coli* B Bacteria, 2.60 Å** Dimer, 2.80 Å: 1FW3	1FW2	Data File Jmol Viewer 1FW2 1FW3	Snijder et al. (2001). Snijder HJ, Kingma RL, Kalk KH, Dekker N, Egmond MR, & Dijkstra BW (2001). Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli. J Mol Biol 309 :477-489. PubMed Id: 11371166.
*OmpLA (PldA) active-site mutant (N156A), pH 6.1: Escherichia coli* B Bacteria, 2.50 Å** pH 4.6, 2.80 Å: 1ILD pH 8.3, 2.98 Å: 1IM0	1ILZ	Data File Jmol Viewer 1ILZ 1ILD 1IM0	Snijder et al. (2001). Snijder HJ, Van Eerde JH, Kingma RL, Kalk KH, Dekker N, Egmond MR, & Dijkstra BW (2001). Structural investigations of the active-site mutant Asn156Ala of outer membrane phospholipase A: function of the Asn-His interaction in the catalytic triad. Protein Sci 10 :1962-1969. PubMed Id: 11567087.
*OpcA adhesin protein: Neisseria meningitidis* B Bacteria, 2.0 Å**	1K24	Data File Jmol Viewer 1K24 OpcA	Prince et al. (2002). Prince SM, Achtman M, & Derrick JP (2002). Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis. Proc. Natl. Acad. Sci. USA 99 :3417-3421. PubMed Id: 11891340.
*OpcA adhesin protein: Neisseria meningitidis* B Bacteria (expressed in E. coli), 1.95 Å** In meso crystallization	2VDF	Data File Jmol Viewer 2VDF	Cherezov et al. (2008). Cherezov V, Liu W, Derrick JP, Luan B, Aksimentiev A, Katritch V, & Caffrey M (2008). In meso crystal structure and docking simulations suggest an alternative proteoglycan binding site in the OpcA outer membrane adhesin. Proteins 71 :24-34. PubMed Id: 18076035. doi:10.1002/prot.21841.
*NspA surface protein: Neisseria meningitidis* B Bacteria, 2.55 Å**	1P4T	Data File Jmol Viewer 1P4T NspA surface protein A	Vandeputte-Rutten et al. (2003). Vandeputte-Rutten L, Bos MP, Tommassen J, & Gros P (2003). Crystal structure of Neisserial surface protein A (NspA), a conserved outer membrane protein with vaccine potential. J. Biol. Chem. 278 :24825-24830. PubMed Id: 12716881.
*NanC Porin, model for KdgM porin family: Escherichia coli* B Bacteria, 1.80 Å** H3 space group. See also 2WJQ, p6₃22 space group, 2.0 Å resolution.	2WJR	Data File Jmol Viewer 2WJR 2WJQ	Wirth et al. (2009). Wirth C, Condemine G, Boiteux C, Bernèche S, Schirmer T, & Peneff CM (2009). NanC Crystal Structure, a Model for Outer-Membrane Channels of the Acidic Sugar-Specific KdgM Porin Family. J Mol Biol 394 :718-731. PubMed Id: 19796645.
*PagL LPS 3-O-deacylase: Pseudomonas aeruginosa* B Bacteria, 2.00 Å**	2ERV	Data File Jmol Viewer 2ERV	Rutten et al. (2006). Rutten L, Geurtsen J, Lambert W, Smolenaers JJ, Bonvin AM, de Haan A, van der Ley P, Egmond MR, Gros P, & Tommassen J (2006). Crystal structure and catalytic mechanism of the LPS 3-O-deacylase PagL from Pseudomonas aeruginosa. Proc Natl Acad Sci USA 103 :7071-7076. PubMed Id: 16632613. doi:10.1073/pnas.0509392103.
*LpxR lipid A deacylase: Salmonella typhimurium* B Bacteria (expressed in E. coli), 1.90 Å**	3FID	Data File Jmol Viewer 3FID	Rutten et al. (2009). Rutten L, Mannie JP, Stead CM, Raetz CR, Reynolds CM, Bonvin AM, Tommassen JP, Egmond MR, Trent MS, & Gros P (2009). Active-site architecture and catalytic mechanism of the lipid A deacylase LpxR of Salmonella typhimurium. Proc Natl Acad Sci USA 106 :1960-1964. PubMed Id: 19174515. doi:10.1073/pnas.0813064106 .
*PagP outer membrane palimitoyl transferease: Escherichia coli* B Bacteria, NMR** 1MM4 is Structure in DPC micelles. Structure in OG micelles: 1MM5	1MM4	Data File Jmol Viewer 1MM4 1MM5 PagP	Hwang et al. (2002). Hwang PM, Choy WY, Lo EI, Chen L, Forman-Kay JD, Raetz CR, Privé GG, Bishop RE, Kay LE (2002). Solution structure and dynamics of the outer membrane enzyme PagP by NMR. Proc Natl Acad Sci USA 99 :13560-13565. PubMed Id: 12357033.
*PagP outer membrane palimitoyl transferease: Escherichia coli* B Bacteria, 1.90 Å**	1THQ	Data File Jmol Viewer 1THQ	Ahn et al. (2004). Ahn VE, Lo EI, Engel CK, Chen L, Hwang PM, Kay LE, Bishop RE, & Prive GG (2004). A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin. EMBO J. 23 :2931-2941. PubMed Id: 15272304.
*PagP outer membrane palimitoyl transferease crystallized from SDS/Co-solvent: Escherichia coli* B Bacteria, 1.40 Å** Reveals phospholipid access route (crenel between strands F and G)	3GP6	Data File Jmol Viewer 3GP6	Cuesta-Seijo et al. (2010). Cuesta-Seijo JA, Neale C, Khan MA, Moktar J, Tran CD, Bishop RE, Pomès R, & Privé GG (2010). PagP crystallized from SDS/cosolvent reveals the route for phospholipid access to the hydrocarbon ruler. Structure 18 :1210-1219. PubMed Id: 20826347.
*FadL long-chain fatty acid transporter: Escherichia coli* B Bacteria, 2.6 Å** 1T16 is from Monoclinic crystals. From hexagonal crystals, 2.8 Å: 1T1L	1T16	Data File Jmol Viewer 1T16 1T1L FadL	van den Berg et al. (2004). van den Berg B, Black PN, Clemons WM Jr, & Rapoport TA (2004). Crystal structure of the long-chain fatty acid transporter FadL. Science 304 :1506-1509. PubMed Id: 15178802.
*FadL long-chain fatty acid transporter A77E/S100R mutant: Escherichia coli* B Bacteria, 2.5 Å** Mutants show that channel wall opening for passage of fatty acids into inner layer of outer membrane is likely. ΔS3 kink, 2.60 Å: 2R88 P34A mutant, 3.3 Å: 2R4L N33A mutant, 3.2 Å: 2R4N ΔNPA mutant, 3.6 Å: 2R4O G212E mutant, 2.9 Å: 2R4P	3DWN	Data File Jmol Viewer 3DWN 2R4N 2R4O 2R88 2R4P 2R4L	Hearn et al. (2009). Hearn EM, Patel DR, Lepore BW, Indic M, van den Berg B (2009). Transmembrane passage of hydrophobic compounds through a protein channel wall. Nature 458 :367-370. PubMed Id: 19182779.
*FadL long-chain fatty acid transporter D348R mutant: Escherichia coli* B Bacteria, 2.60 Å** This and associated structures in conjunction with in vivo transport assays and Trp fluorescence demonstrate ligand gating of the β-barrel protein. delta N3 mutant, 3.40 Å: 2R89 D348A mutant, 2.70 Å: 3PF1 F3E mutant, 1.70 Å: 3PGU F3G mutant, 1.90 Å: 3PGS	3PGR	Data File Jmol Viewer 3PGR 3PF1 3PGS 2R89 3PGU	Lepore et al. (2011). Lepore BW, Indic M, Pham H, Hearn EM, Patel DR, & van den Berg B (2011). Ligand-gated diffusion across the bacterial outer membrane Proc Natl Acad Sci USA 108 :10121-10126. PubMed Id: 21593406. doi:10.1073/pnas.1018532108.
*FadL homologue long-chain fatty acid transporter: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.2 Å** Shows break in channel wall for passage of fatty acids into inner layer of outer membrane in a species other than E. coli. Residues 22-463.	3DWO	Data File Jmol Viewer 3DWO	Hearn et al. (2009). Hearn EM, Patel DR, Lepore BW, Indic M, van den Berg B (2009). Transmembrane passage of hydrophobic compounds through a protein channel wall. Nature 458 :367-370. PubMed Id: 19182779.
*YebT lipid transporter, domains 1-4: Escherichia coli* B Bacteria, 3.1 Å** cryo-EM structure domains 5-7, 3 Å: 6KZ4	6KZ3	Data File Jmol Viewer 6KZ3 6KZ4	Liu et al. (2020). Liu C, Ma J, Wang J, Wang H, & Zhang L (2020). Cryo-EM Structure of a Bacterial Lipid Transporter YebT. J Mol Biol 432 4:1008-1019. PubMed Id: 31870848. doi:10.1016/j.jmb.2019.12.008.
*FauA alcaligin outer membrane transporter: Bordetella pertussis* B Bacteria (expressed in E. coli), 2.3 Å**	3EFM	Data File Jmol Viewer 3EFM	Brillet et al. (2009). Brillet K, Meksem A, Lauber E, Reimmann & C, Cobessi D (2009). Use of an in-house approach to study the three-dimensional structures of various outer membrane proteins: structure of the alcaligin outer membrane transporter FauA from Bordetella pertussis. Acta Crystallogr D Biol Crystallogr 65 :326-331. PubMed Id: 19307713.
*TodX hydrocarbon transporter: Pseudomonas putida* B Bacteria, 2.6 Å** 3BS0 is P1 space group, 2 molecules in asymmetric unit. I222 space group, 3.2 Å: 3BRZ	3BS0	Data File Jmol Viewer 3BS0 3BRZ	Hearn et al. (2008). Hearn EM, Patel DR, & van den Berg BO (2008). Outer-membrane transport of aromatic hydrocarbons as a first step in biodegradation. Proc Natl Acad Sci USA 105 :8601-8606. PubMed Id: 18559855.
*TbuX hydrocarbon transporter: Ralstonia pickettii* B Bacteria, 3.2 Å**	3BRY	Data File Jmol Viewer 3BRY	Hearn et al. (2008). Hearn EM, Patel DR, & van den Berg BO (2008). Outer-membrane transport of aromatic hydrocarbons as a first step in biodegradation. Proc Natl Acad Sci USA 105 :8601-8606. PubMed Id: 18559855.
*Tsx nucleoside transporter (apoprotein): Escherichia coli* B Bacteria, 3.0 Å** Protein + thymidine, 3.10 Å: 1TLW Protein + uridine, 3.10 Å: 1TLZ	1TLY	Data File Jmol Viewer 1TLY 1TLW 1TLZ	Ye and van den Berg (2004). Ye J & van den Berg B (2004). Crystal structure of the bacterial nucleoside transporter Tsx. EMBO J. 23 :3187-3195. PubMed Id: 15272310.
*FhuA, Ferrichrome-iron receptor without ligand: Escherichia coli* B Bacteria, 2.7 Å** With ligand: 1BY5	1BY3	Data File Jmol Viewer 1BY3 1BY5	Locher et al. (1998). Locher KP, Rees B, Koebnik R, Mitschler A, Moulinier L, Rosenbusch JP, & Moras D (1998). Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell 11 :771-8. PubMed Id: 9865695.
*FhuA: Escherichia coli* B Bacteria, 2.50 Å** Includes the structure of a bound lipopolysaccharide (LPS) molecule In complex with ferrichrome-iron, 2.70 Å: 1FCP	2FCP	Data File Jmol Viewer 2FCP 1FCP Ferric hydroxamate uptake receptor	Ferguson et al. (1998). Ferguson AD, Hofmann E, Coulton JW, Diederichs K, & Welte W (1998). Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Protein Sci 9 :956-963. PubMed Id: 9856937.
*FhuA-AW140-LPS: Escherichia coli* B Bacteria, 2.5 Å** Structure of lipopolysaccharide (LPS) in complex with FhuA. FhuA-DL41-LPS-ferricrocin, 2.7 Å: 1QFF	1QFG	Data File Jmol Viewer 1QFG 1QFF	Ferguson et al. (2000). Ferguson AD, Welte W, Hofmann E, Lindner B, Holst O, Coulton JW, & Diederichs K (2000). A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins. Structure 8 :585-592. PubMed Id: 10873859.
*FhuA in complex with albomycin: Escherichia coli* B Bacteria, 3.10 Å** In complex with phenylferricrocin, 2.95 Å: 1QJQ	1QKC	Data File Jmol Viewer 1QKC 1QJQ	Ferguson et al. (2000). Ferguson AD, Braun V, Fiedler HP, Coulton JW, Diederichs K, & Welte W (2000). Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA. Science 282 :2215-2220. PubMed Id: 10850805.
*FhuA in complex with lipopolysaccharide and rifamycin CGP4832: Escherichia coli* B Bacteria, 2.90 Å**	1FI1	Data File Jmol Viewer 1FI1	Ferguson et al. (2001). Ferguson AD, Ködding J, Walker G, Bös C, Coulton JW, Diederichs K, Braun V, & Welte W (2001). Active transport of an antibiotic rifamycin derivative by the outer-membrane protein FhuA. Structure 9 :707-716. PubMed Id: 11587645.
*FhuA in complex withTonB: Escherichia coli* B Bacteria, 3.3 Å**	2GRX	Data File Jmol Viewer 2GRX	Pawelek et al. (2006). Pawelek PD, Croteau N, Ng-Thow-Hing C, Khursigara CM, Moiseeva N, Allaire M, & Coulton JW (2006). Structure of TonB in complex with FhuA, E. coli outer membrane receptor. Science 312 :1399-1402. PubMed Id: 16741125.
*FhuA in complex with lasso peptide microcin J25 (MccJ25): Escherichia coli* B Bacteria, 2.30 Å**	4CU4	Data File Jmol Viewer 4CU4	Mathavan et al. (2014). Mathavan I, Zirah S, Mehmood S, Choudhury HG, Goulard C, Li Y, Robinson CV, Rebuffat S, & Beis K (2014). Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides. Nat Chem Biol 10 5:340-342. PubMed Id: 24705590. doi:10.1038/nchembio.1499.
*FhuA in complex with superinfection exclusion (SE) lipoprotein Llp: Escherichia coli* B Bacteria, 3.37 Å** In complex with T5 phage receptor-binding protein (RBP) pb5, cryo-EM structure, 3.1 Å: 8A8C	8A60	Data File Jmol Viewer 8A60 8A8C	van den Berg et al. (2022). van den Berg B, Silale A, Baslé A, Brandner AF, Mader SL, & Khalid S (2022). Structural basis for host recognition and superinfection exclusion by bacteriophage T5. Proc Natl Acad Sci U S A 119 42:e2211672119. PubMed Id: 36215462. doi:10.1073/pnas.2211672119.
*FyuA siderophore transporter: Yersinia pestis* B Bacteria (expressed in E. coli), 3.20 Å** pesticin bacteriocin toxin, 2.09 Å: 4EPF phage lysin containing the binding domain of pesticin and the killing domain of T4-lysozyme, 2.60 Å: 4EXM pesticin-T4 lysozyme hybrid stabilized by engineered disulfide bonds, 1.74 Å: 4EPI	4EPA	Data File Jmol Viewer 4EPA 4EXM 4EPF 4EPI	Lukacik et al. (2012). Lukacik P, Barnard TJ, Keller PW, Chaturvedi KS, Seddiki N, Fairman JW, Noinaj N, Kirby TL, Henderson JP, Steven AC, Hinnebusch BJ, & Buchanan SK (2012). Structural engineering of a phage lysin that targets gram-negative pathogens. Proc Natl Acad Sci USA 109 25:9857-9862. PubMed Id: 22679291. doi:10.1073/pnas.1203472109.
*FepA, Ferric enterobactin receptor: Escherichia coli* B Bacteria, 2.4 Å**	1FEP	Data File Jmol Viewer 1FEP FepA	Buchanan et al. (1999). Buchanan S, Smith BS, Venkatramani L, Xia D, Esser L, Palnitkar M, Chakraborty R, van der Helm D, & Deisenhofer J. (1999). Crystal Structure of the outer membrane active transporter FepA from Escherichia coli. Nature Structural Biol 6 :56-63. PubMed Id: 9886293.
*Fiu Ferric-Catecholate import receptor, open C222(1) crystal form: B Bacteria (expressed in Escherichia coli), 2.1 Å* Closed form (C21), 2.5 Å: 6BPM Closed form (P1), 2.9 Å: 6BPO	6BPN	Data File Jmol Viewer 6BPN 6BPM 6BPO	Grinter & Lithgow (2019). Grinter R, & Lithgow T (2019). The structure of the bacterial iron-catecholate transporter Fiu suggests that it imports substrates via a two-step mechanism. J Biol Chem 294 51:19523-19534. PubMed Id: 31712312. doi:10.1074/jbc.RA119.011018.
*FecA, siderophore transporter: Escherichia coli* B Bacteria, 2.0 Å** Structure at 2.5 Å: 1KMP	1KMO	Data File Jmol Viewer 1KMO 1KMP FecA	Ferguson et al. (2002). Ferguson AD, Chakraborty R, Smith BS, Esser L, van der Helm D, & Deisenhofer, J (2002). Structural basis of gating by the outer Membrane transporter FecA. Science 295 :1715-1719. PubMed Id: 11872840.
*FecA, siderophore transporter (no ligand): Escherichia coli* B Bacteria, 2.5 Å** FecA with iron-free dicitrate, 2.15 Å: : 1PO0 FecA with diferric dicitrate, 3.4 Å: : 1PO3	1PNZ	Data File Jmol Viewer 1PNZ 1PO0 1PO3	Yue et al. (2003). Yue WW, Grizot S, & Buchanan SK (2003). Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA. J Mol Biol 332 :353-368. PubMed Id: 12948487.
*FecA, siderophore transporter periplasmic signalling domain: Escherichia coli* B Bacteria, NMR Structure** Shows the signalling domain not seen x-ray structures	2D1U	Data File Jmol Viewer 2D1U	Garcia-Herrero & Vogel (2005). Garcia-Herrero A & Vogel HJ (2005). Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB-dependent outer membrane transporter FecA from Escherichia coli. Mol Microbiol 58 :1226-1237. PubMed Id: 16313612.
*PiuA siderophore receptor: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 1.90 Å**	5FOK	Data File Jmol Viewer 5FOK	Moyniéet al. (2017). Moynié L, Luscher A, Rolo D, Pletzer D, Tortajada A, Weingart H, Braun Y, Page MG, Naismith JH, & Köhler T (2017). Structure and Function of the PiuA and PirA Siderophore-Drug Receptors from Pseudomonas aeruginosa and Acinetobacter baumannii. Antimicrob Agents Chemother 61 4. PubMed Id: 28137795. doi:10.1128/AAC.02531-16.
*PiuD siderophore receptor: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.30 Å**	5NEC	Data File Jmol Viewer 5NEC	Luscher et al. (2018). Luscher A, Moynié L, Auguste PS, Bumann D, Mazza L, Pletzer D, Naismith JH, & Köhler T (2018). TonB-Dependent Receptor Repertoire of Pseudomonas aeruginosa for Uptake of Siderophore-Drug Conjugates. Antimicrob Agents Chemother 62 6. PubMed Id: 29555629. doi:10.1128/AAC.00097-18.
*PiuA siderophore receptor: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 1.94 Å**	5FP1	Data File Jmol Viewer 5FP1	Moyniéet al. (2017). Moynié L, Luscher A, Rolo D, Pletzer D, Tortajada A, Weingart H, Braun Y, Page MG, Naismith JH, & Köhler T (2017). Structure and Function of the PiuA and PirA Siderophore-Drug Receptors from Pseudomonas aeruginosa and Acinetobacter baumannii. Antimicrob Agents Chemother 61 4. PubMed Id: 28137795. doi:10.1128/AAC.02531-16.
*PirA siderophore receptor: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.97 Å**	5FP2	Data File Jmol Viewer 5FP2	Moyniéet al. (2017). Moynié L, Luscher A, Rolo D, Pletzer D, Tortajada A, Weingart H, Braun Y, Page MG, Naismith JH, & Köhler T (2017). Structure and Function of the PiuA and PirA Siderophore-Drug Receptors from Pseudomonas aeruginosa and Acinetobacter baumannii. Antimicrob Agents Chemother 61 4. PubMed Id: 28137795. doi:10.1128/AAC.02531-16.
*PirA siderophore receptor: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 2.83 Å**	5FR8	Data File Jmol Viewer 5FR8	Moyniéet al. (2017). Moynié L, Luscher A, Rolo D, Pletzer D, Tortajada A, Weingart H, Braun Y, Page MG, Naismith JH, & Köhler T (2017). Structure and Function of the PiuA and PirA Siderophore-Drug Receptors from Pseudomonas aeruginosa and Acinetobacter baumannii. Antimicrob Agents Chemother 61 4. PubMed Id: 28137795. doi:10.1128/AAC.02531-16.
*HasR heme-uptake receptor in complex with HasA hemophore and heme: Serratia marcescens* B Bacteria (expressed in E. coli), 2.7 Å** HasA~HasR, 3.0 Å: 3CSN HasA~HasR[I671G]~heme, 2.8 Å: 3DDR	3CSL	Data File Jmol Viewer 3CSL 3CSN 3DDR	Krieg et al. (2009). Krieg S, Huché F, Diederichs K, Izadi-Pruneyre N, Lecroisey A, Wandersman C, Delepelaire P, & Welte W. (2009). Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex. Proc Natl Acad Sci USA 106 :1045-1050. PubMed Id: 19144921.
*ShuA heme-uptake receptor in complex with HasA hemophore and heme: Shigella dysenteriae* B Bacteria (expressed in E. coli), 2.6 Å**	3FHH	Data File Jmol Viewer 3FHH	Cobessi et al. (2010). Cobessi D, Meksem A, & Brillet K (2010). Structure of the heme/hemoglobin outer membrane receptor ShuA from Shigella dysenteriae: heme binding by an induced fit mechanism. Proteins 78 :286-294. PubMed Id: 19731368. doi:10.1002/prot.22539.
*FptA pyochelin siderophore transporter: Pseudomonas aeruginosa* B Bacteria, 2.0 Å**	1XKW	Data File Jmol Viewer 1XKW FptA	Cobessi et al. (2005). Cobessi D, Celia H, Pattus F (2005). Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa. J Mol Biol 352 :893-904. PubMed Id: 16139844.
*FptA pyochelin siderophore transporter: Pseudomonas fluorescens* B Bacteria, 3.26 Å**	3QLB	Data File Jmol Viewer 3QLB	Brillet et al. (2011). Brillet K, Reimmann C, Mislin GL, Noël S, Rognan D, Schalk IJ, & Cobessi D (2011). Pyochelin enantiomers and their outer-membrane siderophore transporters in fluorescent pseudomonads: structural bases for unique enantiospecific recognition. J Am Chem Soc 133 41:16503-16509. PubMed Id: 21902256. doi:10.1021/ja205504z.
*FpvA, Pyoverdine receptor: Pseudomonas aeruginosa* B Bacteria, 3.6 Å**	1XKH	Data File Jmol Viewer 1XKH	Cobessi et al. (2005). Cobessi D, Celia H, Folschweiller N, Schaik IJ, Abdallah MA, & Pattus F (2005). The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6 Å resolution. J Mol Biol 347 :121-134. PubMed Id: 15733922.
*FpvA, Pyoverdine receptor (apo form): Pseudomonas aeruginosa* B Bacteria, 2.77 Å**	2O5P	Data File Jmol Viewer 2O5P	Brillet et al. (2007). Brillet K, Journet L, Célia H, Paulus L, Stahl A, Pattus F, & Cobessi D (2007). A β strand lock exchange for signal transduction in TonB-dependent transducers on the basis of a common structural motif. Structure 15 :1383-1391. PubMed Id: 17997964.
*FpvA, Full-length structure bound to iron-pyoverdine: Pseudomonas aeruginosa* B Bacteria, 2.73 Å**	2IAH	Data File Jmol Viewer 2IAH	Wirth et al. (2007). Wirth C, Meyer-Klaucke W, Pattus F, & Cobessi D (2007). From the periplasmic signaling domain to the extracellular face of an outer membrane signal transducer of Pseudomonas aeruginosa: crystal structure of the ferric pyoverdine outer membrane receptor. J Mol Biol 368 :398-406. PubMed Id: 17349657.
*AlgE alginate export protein: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.30 Å** 18-stranded β-barrel with a highly electropositive pore constriction that acts as a selectivity filter for negatively charged alginate.	3RBH	Data File Jmol Viewer 3RBH	Whitney et al. (2011). Whitney JC, Hay ID, Li C, Eckford PD, Robinson H, Amaya MF, Wood LF, Ohman DE, Bear CE, Rehm BH, & Lynne Howell P (2011). Structural basis for alginate secretion across the bacterial outer membrane. Proc Natl Acad Sci USA 108 :13083-13088. PubMed Id: 21778407. doi:10.1073/pnas.1104984108.
*AlgE alginate export protein: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 1.90 Å** In meso crystallization. Crystal form 2, 2.80 Å: 4AZL Crystal form 3, 2.40 Å: 4B61	4AFK	Data File Jmol Viewer 4AFK 4AZL 4B61	Tan et al. (2014). Tan J, Rouse SL, Li D, Pye VE, Vogeley L, Brinth AR, El Arnaout T, Whitney JC, Howell PL, Sansom MS, & Caffrey M (2014). A conformational landscape for alginate secretion across the outer membrane of Pseudomonas aeruginosa. Acta Crystallogr D Biol Crystallogr 70 :2054-2068. PubMed Id: 25084326. doi:10.1107/S1399004714001850.
*AlgE alginate export protein at 100 K: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.90 Å** data collected at 293 K, 2.80 Å: 4XNK Structures determined by serial x-ray crystallography	4XNL	Data File Jmol Viewer 4XNL 4XNK	Huang et al. (2015). Huang CY, Olieric V, Ma P, Panepucci E, Diederichs K, Wang M, & Caffrey M (2015). In meso in situ serial X-ray crystallography of soluble and membrane proteins. Acta Crystallogr D Biol Crystallogr 71 :1238-1256. PubMed Id: 26057665. doi:10.1107/S1399004715005210.
*AlgE alginate export protein, native-SAD structure determined at wavelength 2.755 Å: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 1.77 Å** X-ray Structure	8PZ4	Data File Jmol Viewer 8PZ4	El Omari et al. (2023). El Omari K, Duman R, Mykhaylyk V, Orr CM, Latimer-Smith M, Winter G, Grama V, Qu F, Bountra K, Kwong HS, Romano M, Reis RI, Vogeley L, Vecchia L, Owen CD, Wittmann S, Renner M, Senda M, Matsugaki N, Kawano Y, Bowden TA, Moraes I, Grimes JM, Mancini EJ, Walsh MA, Guzzo CR, Owens RJ, Jones EY, Brown DG, Stuart DI, Beis K, & Wagner A (2023). Experimental phasing opportunities for macromolecular crystallography at very long wavelengths. Commun Chem 6 1:219. PubMed Id: 37828292. doi:10.1038/s42004-023-01014-0.
*AlgE alginate export protein in 7.10 monoacylglycerol (MAG): Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 1.45 Å** X-ray structure	8RQP	Data File Jmol Viewer 8RQP	Krawinski et al. (2024). Krawinski P, Smithers L, van Dalsen L, Boland C, Ostrovitsa N, Pérez J, & Caffrey M (2024). 7.10 MAG. A Novel Host Monoacylglyceride for In Meso (Lipid Cubic Phase) Crystallization of Membrane Proteins. Cryst Growth Des 24 7:2985-3001. PubMed Id: 38585376. doi:10.1021/acs.cgd.4c00087.
*AlgK–AlgX alginate export protein complex: Pseudomonas putida* B Bacteria (expressed in E. coli), 2.46 Å**	7ULA	Data File Jmol Viewer 7ULA	Gheorghita et al. (2022). Gheorghita AA, Li YE, Kitova EN, Bui DT, Pfoh R, Low KE, Whitfield GB, Walvoort MTC, Zhang Q, Codée JDC, Klassen JS, & Howell PL (2022). Structure of the AlgKX modification and secretion complex required for alginate production and biofilm attachment in Pseudomonas aeruginosa. Nat Commun 13 1:7631. PubMed Id: 36494359. doi:10.1038/s41467-022-35131-6.
*P pilus usher translocation domain, PapC_130-640: Escherichia coli* B Bacteria, 3.2 Å**	2VQI	Data File Jmol Viewer 2VQI	Remaut et al. (2008). Remaut H, Tang C, Henderson NS, Pinkner JS, Wang T, Hultgren SJ, Thanassi DG, Waksman G, & Li H (2008). Fiber formation across the bacterial outer membrane by the chaperone/usher pathway. Cell 133 :640-652. PubMed Id: 18485872.
*P pilus usher translocation domain, PapC_146-637: Escherichia coli* B Bacteria, 3.15 Å**	3FIP	Data File Jmol Viewer 3FIP	Huang et al. (2009). Huang Y, Smith BS, Chen LX, Baxter RH, & Deisenhofer J (2009). Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC. Proc Natl Acad Sci USA 106 18:7403-7407. PubMed Id: 19380723. doi:10.1073/pnas.0902789106.
*P pilus FimD usher bound to FimC:FimH substrate: Escherichia coli* B Bacteria, 2.80 Å** FimD translocation domain, 3.01 Å: 3OHN	3RFZ	Data File Jmol Viewer 3RFZ 3OHN	Phan et al. (2011). Phan G, Remaut H, Wang T, Allen WJ, Pirker KF, Lebedev A, Henderson NS, Geibel S, Volkan E, Yan J, Kunze MB, Pinkner JS, Ford B, Kay CW, Li H, Hultgren SJ, Thanassi DG, & Waksman G (2011). Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate. Nature 474 :49-53. PubMed Id: 21637253. doi:10.1038/nature10109.
*P pilus FimD usher in complex with FimC:FimF:FimG:FimH: Escherichia coli* B Bacteria, 3.80 Å** This is the complete structure of the tip complex assembly in which the FimC:FimF:FimG:FimH complex passes through FimD.	4J3O	Data File Jmol Viewer 4J3O	Geibel et al. (2013). Geibel S, Procko E, Hultgren SJ, Baker D, & Waksman G (2013). Structural and energetic basis of folded-protein transport by the FimD usher. Nature 496 :243-246. PubMed Id: 23579681. doi:10.1038/nature12007.
*P pilus assembly intermediate (FimD-FimC-FimF-FimG-FimH), conformer 1: Escherichia coli* B Bacteria, 4 Å** cryo-EM structure conformer 2, 5.1 Å: 6E15	6E14	Data File Jmol Viewer 6E14 6E15	Du et al. (2018). Du M, Yuan Z, Yu H, Henderson N, Sarowar S, Zhao G, Werneburg GT, Thanassi DG, & Li H (2018). Handover mechanism of the growing pilus by the bacterial outer-membrane usher FimD. Nature 562 7727:444-447. PubMed Id: 30283140. doi:10.1038/s41586-018-0587-z.
*P pilus tip assembly intermediate PapC-PapD-PapK-PapF-PapG: Escherichia coli* B Bacteria, 7.60 Å** cryo-EM structure PapC-PapD-PapK-PapG in the first conformation, 3.80 Å 7LHG PapC-PapD-PapK-PapG in the second conformation, 7.20 Å 7LHH	7LHI	Data File Jmol Viewer 7LHI 7LHH 7LHG	Du et al. (2021). Du M, Yuan Z, Werneburg GT, Henderson NS, Chauhan H, Kovach A, Zhao G, Johl J, Li H, & Thanassi DG (2021). Processive dynamics of the usher assembly platform during uropathogenic Escherichia coli P pilus biogenesis. Nat Commun 12 1:5207. PubMed Id: 34471127. doi:10.1038/s41467-021-25522-6.
*Transferrin binding protein A (TbpA) in complex with human transferrin: Neisseria meningitidis serogroup b* B Bacteria (expressed in E. coli), 2.60 Å** TbpA in complex with human transferrin C-lobe, 3.10 Å: 3V89 Diferric human transferrin, 2.10 Å: 3V83 Apo-human transferrin C-lobe with bound sulfate ions, 1.70 Å: 3SKP Transferrin binding protein B (TbpB), 2.40 Å: 3V8U	3V8X	Data File Jmol Viewer 3V8X 3V89 3V8U 3V83 3SKP	Noinaj et al. (2012). Noinaj N, Easley NC, Oke M, Mizuno N, Gumbart J, Boura E, Steere AN, Zak O, Aisen P, Tajkhorshid E, Evans RW, Gorringe AR, Mason AB, Steven AC, & Buchanan SK (2012). Structural basis for iron piracy by pathogenic Neisseria. Nature 483 :53-58. PubMed Id: 22327295. doi:10.1038/nature10823.
*Wzi outer-membrane lectin: Escherichia coli* B Bacteria, 2.64 Å** Assists in the formation of the bacterial capsule via direct interaction with capsular polysaccharides.	2YNK	Data File Jmol Viewer 2YNK	Bushell et al. (2013). Bushell SR, Mainprize IL, Wear MA, Lou H, Whitfield C, & Naismith JH (2013). Wzi Is an Outer Membrane Lectin that Underpins Group 1 Capsule Assembly in Escherichia coli. Structure 21 :844-853. PubMed Id: 23623732. doi:10.1016/j.str.2013.03.010.
*Opa₆₀ for receptor-mediated engulfment, EXPLOR refined: Neisseria gonorrhoeae* B Bacteria, NMR strucuture** MD/EXPLOR refined structure, NMR structure: 2MAF	2MLH	Data File Jmol Viewer 2MLH 2MAF	Fox et al. (2014). Fox DA, Larsson P, Lo RH, Kroncke BM, Kasson PM, & Columbus L (2014). Structure of the neisserial outer membrane protein opa60: loop flexibility essential to receptor recognition and bacterial engulfment. J Am Chem Soc 136 :9938-9946. PubMed Id: 24813921. doi:10.1021/ja503093y.
*CsgG bacterial amyloid secretion channel: Escherichia coli* B Bacteria, 3.59 Å** Pre-pore conformation, 2.80 Å: 4UV2	4UV3	Data File Jmol Viewer 4UV3 4UV2	Goyal et al. (2014). Goyal P, Krasteva PV, Van Gerven N, Gubellini F, Van den Broeck I, Troupiotis-Tsaïlaki A, Jonckheere W, Péhau-Arnaudet G, Pinkner JS, Chapman MR, Hultgren SJ, Howorka S, Fronzes R, & Remaut H (2014). Structural and mechanistic insights into the bacterial amyloid secretion channel CsgG. Nature 516 7530:250-253. PubMed Id: 25219853. doi:10.1038/nature13768.
*CsgG bacterial amyloid secretion channel: Escherichia coli* B Bacteria, 3.10 Å**	4Q79	Data File Jmol Viewer 4Q79	Cao et al. (2014). Cao B, Zhao Y, Kou Y, Ni D, Zhang XC, & Huang Y (2014). Structure of the nonameric bacterial amyloid secretion channel. Proc Natl Acad Sci USA 111 50:E5439-E5444. PubMed Id: 25453093. doi:10.1073/pnas.1411942111.
*CsgG-CsgF complex involved in curli biogenesis: Escherichia coli* B Bacteria, 2.94 Å** cryo-EM structure Low resolution architecture of curli complex, 3.24 Å: 6LQJ curli complex architecture, 3.60 Å: 7BRM	6LQH	Data File Jmol Viewer 6LQH 7BRM 6LQJ	Zhang et al. (2020). Zhang M, Shi H, Zhang X, Zhang X, & Huang Y (2020). Cryo-EM structure of the nonameric CsgG-CsgF complex and its implications for controlling curli biogenesis in Enterobacteriaceae. PLoS Biol 18 6. PubMed Id: 32559189. doi:10.1371/journal.pbio.3000748.
*CsgG-CsgF complex involved in curli biogenesis: Escherichia coli* B Bacteria, 3.38 Å** cryo-EM structure complex with substrate CsgAN6 peptide, 3.34 Å: 6L7C	6L7A	Data File Jmol Viewer 6L7A 6L7C	Yan et al. (2020). Yan Z, Yin M, Chen J, & Li X (2020). Assembly and substrate recognition of curli biogenesis system. Nat Commun 11 1:241. PubMed Id: 31932609. doi:10.1038/s41467-019-14145-7.
*CsgG-CsgF complex involved in curli biogenesis: Escherichia coli* B Bacteria, 3.40 Å** cryo-EM structure	6SI7	Data File Jmol Viewer 6SI7	Van der Verren et al. (2020). Van der Verren SE, Van Gerven N, Jonckheere W, Hambley R, Singh P, Kilgour J, Jordan M, Wallace EJ, Jayasinghe L, & Remaut H (2020). A dual-constriction biological nanopore resolves homonucleotide sequences with high fidelity. Nat Biotechnol 38 12:1415-1420. PubMed Id: 32632300. doi:10.1038/s41587-020-0570-8.
*FusA plant-ferredoxin receptor: Pectobacterium atrosepticum* B Bacteria (expressed in E. coli), 3.2 Å**	4ZGV	Data File Jmol Viewer 4ZGV	Grinter et al. (2016). Grinter R, Josts I, Mosbahi K, Roszak AW, Cogdell RJ, Bonvin AM, Milner JJ, Kelly SM, Byron O, Smith BO, & Walker D (2016). Structure of the bacterial plant-ferredoxin receptor FusA. Nat Commun 7 :13308. PubMed Id: 27796364. doi:10.1038/ncomms13308.
*Omp33 outer membrane protein: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 2.2 Å**	6GIE	Data File Jmol Viewer 6GIE	Abellón-Ruiz et al. (2018). Abellón-Ruiz J, Zahn M, Baslé A, & van den Berg B (2018). Crystal structure of the Acinetobacter baumannii outer membrane protein Omp33. Acta Crystallogr D Struct Biol 74 :852-860. PubMed Id: 30198896. doi:10.1107/S205979831800904X.
*FrpB TonB-dependent iron transporter: Neisseria meningitidis* B Bacteria (expressed in E. coli), 2.40 Å** F5-1 variant, 2.60 Å: 4AIQ F5-1 variant, apo form, 2.32 Å: 4B7O	4AIP	Data File Jmol Viewer 4AIP 4AIQ 4B7O	Saleem et al. (2013). Saleem M, Prince SM, Rigby SE, Imran M, Patel H, Chan H, Sanders H, Maiden MC, Feavers IM, & Derrick JP (2013). Use of a molecular decoy to segregate transport from antigenicity in the FrpB iron transporter from Neisseria meningitidis. PLoS ONE 8 2. PubMed Id: 23457610. doi:10.1371/journal.pone.0056746.
*FhuE TonB-dependent transporter: Escherichia coli* B Bacteria, 2 Å**	6E4V	Data File Jmol Viewer 6E4V	Grinter & Lithgow (2019). Grinter R, & Lithgow T (2019). Determination of the molecular basis for coprogen import by Gram-negative bacteria. IUCrJ 6 :401-411. PubMed Id: 31098021. doi:10.1107/S2052252519002926.
*YncD TonB-dependent transporter: Escherichia coli* B Bacteria, 2.96 Å**	6V81	Data File Jmol Viewer 6V81	Grinter & Lithgow (2020). Grinter R, & Lithgow T (2020). The crystal structure of the TonB-dependent transporter YncD reveals a positively charged substrate-binding site. Acta Crystallogr D Struct Biol 76 :484-495. PubMed Id: 32355044. doi:10.1107/S2059798320004398.
*PfeA ferric enterobactin receptor, apo form: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.12 Å** in complex with enterobactin, 2.7 Å: 6Q5E in complex with azotochelin, 2.78 Å: 5NR2 in complex with protochelin, 2.8 Å: 5NC4 R480A, Q482A mutant, 2.67 Å: 5MZS G324V mutant, 2.9 Å: 5OUT R480A mutant in complex with enterobactin, 3.11 Å: 6R1F Q482A mutant in complex with enterobactin, 2.96 Å: 6I2J	5M9B	Data File Jmol Viewer 5M9B 6Q5E 6R1F 6I2J 5NC4 5NR2 5MZS 5OUT	Moynié et al. (2019). Moynié L, Milenkovic S, Mislin GLA, Gasser V, Malloci G, Baco E, McCaughan RP, Page MGP, Schalk IJ, Ceccarelli M, & Naismith JH (2019). The complex of ferric-enterobactin with its transporter from Pseudomonas aeruginosa suggests a two-site model. Nat Commun 10 1. PubMed Id: 31413254. doi:10.1038/s41467-019-11508-y.
*PfeA ferric enterobactin receptor in complex with TCV: Pseudomonas aeruginosa* E Eukaryota (expressed in E. coli), 2.57 Å** in complex with BCV, 2.71 Å: 6Z33 in complex with TCV-L6, 2.66 Å: 7OBW in complex with TCV_L5, 2.72 Å: 6YY5 in complex with BCV-L6, 3.03 Å: 6Z2N in complex with BCV-L5, 3.04 Å: 6Y47	5NC3	Data File Jmol Viewer 5NC3 6Z2N 6YY5 6Y47 7OBW 6Z33	Moynié et al. (2022). Moynié L, Hoegy F, Milenkovic S, Munier M, Paulen A, Gasser V, Faucon AL, Zill N, Naismith JH, Ceccarelli M, Schalk IJ, & Mislin GLA (2022). Hijacking of the Enterobactin Pathway by a Synthetic Catechol Vector Designed for Oxazolidinone Antibiotic Delivery in Pseudomonas aeruginosa. ACS Infect Dis 8 9:1894-1904. PubMed Id: 35881068. doi:10.1021/acsinfecdis.2c00202.
*BcsC cellulose synthase outer membrane channel: Escherichia coli* B Bacteria, 1.85 Å** See inner membrane components structures: 4HG6	6TZK	Data File Jmol Viewer 6TZK	Acheson et al. (2019). Acheson JF, Derewenda ZS, & Zimmer J (2019). Architecture of the Cellulose Synthase Outer Membrane Channel and Its Association with the Periplasmic TPR Domain. Structure 27 12:1855-1861.e3. PubMed Id: 31604608. doi:10.1016/j.str.2019.09.008.
*ZnuD zinc transporter: Neisseria meningitidis* B Bacteria (expressed in E. coli), 3.20 Å**	4RDT	Data File Jmol Viewer 4RDT	Calmettes et al. (2015). Calmettes C, Ing C, Buckwalter CM, El Bakkouri M, Chieh-Lin Lai C, Pogoutse A, Gray-Owen SD, Pomès R, & Moraes TF (2015). The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD. Nat Commun 6 :7996. PubMed Id: 26282243. doi:10.1038/ncomms8996.
*MtrE Outer Membrane Channel: Neisseria gonorrhoeae* B Bacteria (expressed in E. coli), 3.29 Å** Multidrug efflux transporter. See 4MT1	4MT0	Data File Jmol Viewer 4MT0	Lei et al. (2014). Lei HT, Chou TH, Su CC, Bolla JR, Kumar N, Radhakrishnan A, Long F, Delmar JA, Do SV, Rajashankar KR, Shafer WM, & Yu EW (2014). Crystal structure of the open state of the Neisseria gonorrhoeae MtrE outer membrane channel. PLoS ONE 9 6. PubMed Id: 24901251. doi:10.1371/journal.pone.0097475.
*LetB lipophilic Envelope-spanning Tunnel B, model 1: Escherichia coli* B Bacteria, 3.46 Å** cryo-EM structure model 2, 3.49 Å: 6V0D model 3, 3.06 Å: 6V0E model 4, 2.96 Å: 6V0F model 5, 3.03 Å: 6V0G model 6, 3.60 Å: 6V0H model 7, 3.43 Å: 6V0I model 8, 3.78 Å: 6V0J domains MCE2-MCE3 by x-ray, 2.15 Å: 6VCI	6V0C	Data File Jmol Viewer 6V0C 6V0G 6V0F 6V0J 6V0E 6V0H 6VCI 6V0D 6V0I	Isom et al. (2020). Isom GL, Coudray N, MacRae MR, McManus CT, Ekiert DC, & Bhabha G (2020). LetB Structure Reveals a Tunnel for Lipid Transport across the Bacterial Envelope. Cell 181 3:653-664.e19. PubMed Id: 32359438. doi:10.1016/j.cell.2020.03.030.
*PcoB copper transporter: Escherichia coli* B Bacteria, 2.00 Å**	7PGE	Data File Jmol Viewer 7PGE	Li et al. (2022). Li P, Nayeri N, Górecki K, Becares ER, Wang K, Mahato DR, Andersson M, Abeyrathna SS, Lindkvist-Petersson K, Meloni G, Missel JW, & Gourdon P (2022). PcoB is a defense outer membrane protein that facilitates cellular uptake of copper. Protein Sci 31 7:e4364. PubMed Id: 35762724. doi:10.1002/pro.4364.
Outer Membrane Autotransporters
*NalP autotransporter translocator domain: Neisseria meningitidis* B Bacteria (expressed in E. coli), 2.60 Å** p6₁22 space group. See also 1UYO, C222₁ space group, 3.2 Å resolution.	1UYN	Data File Jmol Viewer 1UYN 1UYO NaIP translocator domain	Oomen et al. (2004). Oomen CJ, Van Ulsen P, Van Gelder P, Feijen M, Tommassen J, & Gros P (2004). Structure of the translocator domain of a bacterial autotransporter. EMBO J 23 :1257-1266. PubMed Id: 15014442.
*Hia_1022-1098 trimeric autotransporter: Haemophilus influenzae* B Bacteria (expressed in E. coli), 2.0 Å** Hia_992-1098, 2.3 Å: 2GR7	2GR8	Data File Jmol Viewer 2GR8 2GR7 Hia autotransporter	Meng et al. (2006). Meng G, Surana NK, St Geme JW 3rd, Waksman G (2006). Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter. EMBO J 25 :2297-2304. PubMed Id: 16688217.
*EspP autotransporter, post-cleavage state: Escherichia coli* B Bacteria, 2.7 Å**	2QOM	Data File Jmol Viewer 2QOM	Barnard et al. (2007). Barnard TJ, Dautin N, Lukacik P, Bernstein HD, & Buchanan SK (2007). Autotransporter structure reveals intra-barrel cleavage followed by conformational changes. Nature Struc Mol Biol 14 :1214-1220. PubMed Id: 17994105.
*EspP autotransporter, pre-cleavage state (N1023A mutant): Escherichia coli* B Bacteria, 2.48 Å** Pre-cleavage structure (N1023D mutant), 2.52 Å: 3SLO Pre-cleavage structure (N1023S mutant), 2.46 Å: 3SLT	3SLJ	Data File Jmol Viewer 3SLJ 3SLT 3SLO	Barnard et al. (2012). Barnard TJ, Gumbart J, Peterson JH, Noinaj N, Easley NC, Dautin N, Kuszak AJ, Tajkhorshid E, Bernstein HD, & Buchanan SK (2012). Molecular Basis for the Activation of a Catalytic Asparagine Residue in a Self-Cleaving Bacterial Autotransporter. J Mol Biol 415 :128-142. PubMed Id: 22094314. doi:10.1016/j.jmb.2011.10.049.
*EspP autotransporter passenger domain: Escherichia coli* B Bacteria, 2.50 Å** Like a number of other auto-cleaved passengers, a parallel β-helix is a characteristic feature.	3SZE	Data File Jmol Viewer 3SZE	Khan et al. (2011). Khan S, Mian HS, Sandercock LE, Chirgadze NY, & Pai EF (2011). Crystal Structure of the Passenger Domain of the Escherichia coli Autotransporter EspP. J Mol Biol 413 :985-1000. PubMed Id: 21964244. doi:10.1016/j.jmb.2011.09.028.
*AIDA-I autotransport unit (AIDA = adhesin involved in diffuse adherence): Escherichia coli* B Bacteria, 3.00 Å**	4MEE	Data File Jmol Viewer 4MEE	Gawarzewski et al. (2014). Gawarzewski I, DiMaio F, Winterer E, Tschapek B, Smits SHJ, Jose J, & Schmitt L (2014). Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli. J Struct Biol 187 1:20-29. PubMed Id: 24841284. doi:10.1016/j.jsb.2014.05.003.
*Hbp (hemoglobin protease) self-cleaving autotransporter with truncated passenger: Escherichia coli* B Bacteria, 2.00 Å** The structure shows the pre-cleavage state.	3AEH	Data File Jmol Viewer 3AEH	Tajima et al. (2010). Tajima N, Kawai F, Park SY, & Tame JR (2010). A novel intein-like autoproteolytic mechanism in autotransporter proteins. J Mol Biol 402 :645-656. PubMed Id: 20615416. doi:10.1016/j.jmb.2010.06.068.
*Hbp (hemoglobin protease) full-length passenger domain: Escherichia coli* B Bacteria, 2.20 Å** The passenger domain has a prominent β-helix domain.	1WXR	Data File Jmol Viewer 1WXR	Otto et al. (2005). Otto BR, Sijbrandi R, Luirink J, Oudega B, Heddle JG, Mizutani K, Park SY, & Tame JR (2005). Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli. J Biol Chem 280 :17339-17345. PubMed Id: 15728184. doi:10.1074/jbc.M412885200.
*EstA Autotransporter, full length: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.50 Å** This is the first full-length structure of an autotransporter. The passenger is not cleaved physiologically, but rather presents an esterase domain to the external world.	3KVN	Data File Jmol Viewer 3KVN	van den Berg (2010). van den Berg B (2010). Crystal Structure of a Full-Length Autotransporter. J Mol Biol 396 :627-633. PubMed Id: 20060837.
*IcsA autotransporter (autochaperone region only): Shigella flexneri* B Bacteria (expressed in E. coli), 2.00 Å**	3ML3	Data File Jmol Viewer 3ML3	Kühnel & Diezmann (2011). Kühnel K & Diezmann D (2011). Crystal structure of the autochaperone region from the Shigella flexneri autotransporter IcsA. J Bacteriol 193 :2042-2045 . PubMed Id: 21335457. doi:10.1128/JB.00790-10.
*Intimin outer membrane β-domain: Escherichia coli* B Bacteria, 1.86 Å** The C-terminal passenger domain, not present in this structure, is involved in adhesion to host cells.	4E1S	Data File Jmol Viewer 4E1S	Fairman et al. (2012). Fairman JW, Dautin N, Wojtowicz D, Liu W, Noinaj N, Barnard TJ, Udho E, Przytycka TM, Cherezov V, & Buchanan SK (2012). Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E. coli and enteropathogenic Y. pseudotuberculosis. Structure 20 :1233-1243. PubMed Id: 22658748. doi:10.1016/j.str.2012.04.011.
*Intimin C-terminal passenger domain in complex with receptor: Escherichia coli* B Bacteria, 2.90 Å**	1F02	Data File Jmol Viewer 1F02	Luo et al. (2000). Luo Y, Frey EA, Pfuetzner RA, Creagh AL, Knoechel DG, Haynes CA, Finlay BB, & Strynadka NC (2000). Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex. Nature 405 :1073-1077. PubMed Id: 10890451. doi:10.1038/35016618. See also: Batchelor et al. (2000). Batchelor M, Prasannan S, Daniell S, Reece S, Connerton I, Bloomberg G, Dougan G, Frankel G, & Matthews S (2000). Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli. EMBO J 19 :2452-2464. PubMed Id: 10835344.
*Invasin outer membrane β-domain: Yersinia pseudotuberculosis* B Bacteria (expressed in E. coli), 2.26 Å** The C-terminal passenger domain, not present in this structure, is involved in adhesion to host cells.	4E1T	Data File Jmol Viewer 4E1T	Fairman et al. (2012). Fairman JW, Dautin N, Wojtowicz D, Liu W, Noinaj N, Barnard TJ, Udho E, Przytycka TM, Cherezov V, & Buchanan SK (2012). Crystal structures of the outer membrane domain of intimin and invasin from enterohemorrhagic E. coli and enteropathogenic Y. pseudotuberculosis. Structure 20 :1233-1243. PubMed Id: 22658748. doi:10.1016/j.str.2012.04.011.
*Invasin C-terminal passenger domain: Yersinia pseudotuberculosis* B Bacteria (expressed in E. coli), 2.30 Å**	1CWV	Data File Jmol Viewer 1CWV	Hamburger et al. (1999). Hamburger ZA, Brown MS, Isberg RR, & Bjorkman PJ (1999). Crystal structure of invasin: a bacterial integrin-binding protein. Science 286 :291-295. PubMed Id: 10514372.
*YadA trimeric adhesin autotransporter: Yersinia enterocolitica subsp. enterocolitica 8081* B Bacteria (expressed in E. coli), NMR Structure** Structure determined from microcrystals using solid-state NMR	2LME	Data File Jmol Viewer 2LME	Shahid et al. (2012). Shahid SA, Bardiaux B, Franks WT, Krabben L, Habeck M, van Rossum BJ, & Linke D (2012). Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals. Nature Methods 9 :1212-1217. PubMed Id: 23142870.
*TamA Autotransporter, full length: Escherichia coli* B Bacteria, 2.25 Å** TamA POTRA domains 1-3, 1.84 Å: 4BZA	4C00	Data File Jmol Viewer 4C00 4BZA	Gruss et al. (2013). Gruss F, Zähringer F, Jakob RP, Burmann BM, Hiller S, & Maier T (2013). The structural basis of autotransporter translocation by TamA. Nat Struct Mol Biol 20 :1318-1320. PubMed Id: 24056943. doi:10.1038/nsmb.2689.
*TibC dodecameric glycosyltransferase (type V secretion system): Escherichia coli ETEC H10407* B Bacteria (expressed in E. coli), 2.88 Å** in complex with ADP-D-beta-D-heptose, 3.88 Å: 4RB4 Cryo-EM structures of the TibC₁₂-TibA₆ are available in the EM Databank with accession numbers EMD-2755, -2756, -2757, and -2758.	4RAP	Data File Jmol Viewer 4RAP 4RB4	Yao et al. (2014). Yao Q, Lu Q, Wan X, Song F, Xu Y, Hu M, Zamyatina A, Liu X, Huang N, Zhu P, & Shao F (2014). A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family. Elife 3 . PubMed Id: 25310236. doi:10.7554/eLife.03714.
*BrkA autotransport β-domain: Bordetella pertussis* B Bacteria (expressed in E. coli), 3.00 Å**	3QQ2	Data File Jmol Viewer 3QQ2	Zhai et al. (2011). Zhai Y, Zhang K, Huo Y, Zhu Y, Zhou Q, Lu J, Black I, Pang X, Roszak AW, Zhang X, Isaacs NW, & Sun F (2011). Autotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the β-domain pore. Biochem J 435 3:577-587. PubMed Id: 21306302. doi:10.1042/BJ20101548.
*CdiB autotransporter: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 2.40 Å** A type Vb secretion system that export CdiA toxins.	6WIL	Data File Jmol Viewer 6WIL	Guerin et al. (2020). Guerin J, Botos I, Zhang Z, Lundquist K, Gumbart JC, & Buchanan SK (2020). Structural insight into toxin secretion by contact-dependent growth inhibition transporters. Elife 9 :e58100. PubMed Id: 33089781. doi:10.7554/eLife.58100.
*CdiB autotransporter: Escherichia coli* B Bacteria, 2.60 Å** A type Vb secretion system that export CdiA toxins.	6WIM	Data File Jmol Viewer 6WIM	Guerin et al. (2020). Guerin J, Botos I, Zhang Z, Lundquist K, Gumbart JC, & Buchanan SK (2020). Structural insight into toxin secretion by contact-dependent growth inhibition transporters. Elife 9 :e58100. PubMed Id: 33089781. doi:10.7554/eLife.58100.
*BpaC, C-terminal head domain of the trimeric autotransporter adhesin fused to a GCN4 anchor: Burkholderia pseudomallei* B Bacteria (expressed in E. coli), 1.40 Å**	7O23	Data File Jmol Viewer 7O23	Kiessling et al. (2022). Kiessling AR, Harris SA, Weimer KM, Wells G, & Goldman A (2022). The C-terminal head domain of Burkholderia pseudomallei BpaC has a striking hydrophilic core with an extensive solvent network. Mol Microbiol 118 :77-91. PubMed Id: 35703459. doi:10.1111/mmi.14953.
Omp85-TpsB Outer Membrane Transporter Superfamily
*FhaC Filamentous Hemagglutinin Transporter: Bordetella pertussis* B Bacteria (expressed in E. coli), 3.15 Å** The first outer membrane protein from the Omp85–two-partner secretion B (TpsB) superfamily. Supersedes 2QDZ.	4QKY	Data File Jmol Viewer 4QKY	Clantin et al. (2007). Clantin B, Delattre AS, Rucktooa P, Saint N, Meli AC, Locht C, Jacob-Dubuisson F, & Villeret V (2007). Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily. Science 317 :957-961. PubMed Id: 17702945.
*FhaC Filamentous Hemagglutinin Transporter, R450A mutant: Bordetella pertussis* B Bacteria (expressed in E. coli), 3.50 Å**	3NJT	Data File Jmol Viewer 3NJT	Delattre et al. (2010). Delattre AS, Clantin B, Saint N, Locht C, Villeret V, & Jacob-Dubuisson F (2010). Functional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamily. FEBS J 277 :4755-4765. PubMed Id: 20955520. doi:10.1111/j.1742-4658.2010.07881.x.
*TeOmp85-N POTRA domains: Thermosynechococcus elongatus* B Bacteria (expressed in E. coli), 1.97 Å** Structure is of complete N-terminus containing three POTRA domains. The polypeptide transport-associated (POTRA) domains link to a transmembrane β-barrel, which is absent in this structure.	2X8X	Data File Jmol Viewer 2X8X	Arnold et al. (2010). Arnold T, Zeth K, & Linke D (2010). Omp85 from the thermophilic cyanobacterium thermosynechococcus elongatus differs from proteobacterial Omp85 in structure and domain composition. J Biol Chem 285 :18003-18015. PubMed Id: 20351097.
*anaOmp85-N POTRA domains (hexagonal crystals): Anabaena sp. PCC7120* B Bacteria (expressed in E. coli), 2.20 Å** Structure is of complete N-terminus containing three POTRA domains. The polypeptide transport-associated (POTRA) domains link to a transmembrane β-barrel, which is absent in this structure. Tetragonal crystals, 2.59 Å: 3MC8	3MC9	Data File Jmol Viewer 3MC9 3MC8	Koenig et al. (2010). Koenig P, Mirus O, Haarmann R, Sommer M, Sinning I, Schleiff E, & Tews I (2010). Conserved properties of POTRA domains derived from cyanobacterial OMP85. J Biol Chem 285 :18016-18024. PubMed Id: 20348103.
*BamA without POTRA domains.: Escherichia coli* B Bacteria, 2.60 Å**	4N75	Data File Jmol Viewer 4N75	Ni et al. (2014). Ni D, Wang Y, Yang X, Zhou H, Hou X, Cao B, Lu Z, Zhao X, Yang K, & Huang Y (2014). Structural and functional analysis of the β-barrel domain of BamA from Escherichia coli. FASEB J 28 6:2677-2685. PubMed Id: 24619089. doi:10.1096/fj.13-248450.
*BamA in complex with darobactin B: Escherichia coli* B Bacteria, 2.50 Å**	7P1C	Data File Jmol Viewer 7P1C	Böhringer et al. (2021). Böhringer N, Green R, Liu Y, Mettal U, Marner M, Modaresi SM, Jakob RP, Wuisan ZG, Maier T, Iinishi A, Hiller S, Lewis K, & Schäberle TF (2021). Mutasynthetic Production and Antimicrobial Characterization of Darobactin Analogs. Microbiol Spectr 9 3:e0153521. PubMed Id: 34937193. doi:10.1128/spectrum.01535-21.
*BamA in complex with dynobactin A: Escherichia coli* B Bacteria, 2.50 Å** X-ray Structure	7R1V	Data File Jmol Viewer 7R1V	Miller et al. (2022). Miller RD, Iinishi A, Modaresi SM, Yoo BK, Curtis TD, Lariviere PJ, Liang L, Son S, Nicolau S, Bargabos R, Morrissette M, Gates MF, Pitt N, Jakob RP, Rath P, Maier T, Malyutin AG, Kaiser JT, Niles S, Karavas B, Ghiglieri M, Bowman SEJ, Rees DC, Hiller S, & Lewis K (2022). Computational identification of a systemic antibiotic for gram-negative bacteria. Nat Microbiol 7 10:1661-1672. PubMed Id: 36163500. doi:10.1038/s41564-022-01227-4.
*BamA with POTRA domains 1 - 5: Neisseria gonorrhoeae* B Bacteria (expressed in E. coli), 3.20 Å** This is the full-length BamA structure.	4K3B	Data File Jmol Viewer 4K3B	Noinaj et al. (2013). Noinaj N, Kuszak AJ, Gumbart JC, Lukacik P, Chang H, Easley NC, Lithgow T, & Buchanan SK (2013). Structural insight into the biogenesis of β-barrel membrane proteins. Nature 501 :385-390. PubMed Id: 23995689. doi:10.1038/nature12521.
*BamA with POTRA domains 4 & 5: Haemophilus ducreyi* B Bacteria (expressed in E. coli), 2.91 Å**	4K3C	Data File Jmol Viewer 4K3C	Noinaj et al. (2013). Noinaj N, Kuszak AJ, Gumbart JC, Lukacik P, Chang H, Easley NC, Lithgow T, & Buchanan SK (2013). Structural insight into the biogenesis of β-barrel membrane proteins. Nature 501 :385-390. PubMed Id: 23995689. doi:10.1038/nature12521.
*BamA_21-351 POTRA domains (periplasmic fragment, P2₁2₁2₁): Escherichia coli* B Bacteria, 2.2 Å** BamA was formerly named YaeT. The polypeptide transport-associated (POTRA) domains link to a transmembrane β-barrel, which is absent in this structure. P2₁2₁2 space group, 2.2 Å: 2QDF	2QCZ	Data File Jmol Viewer 2QCZ 2QDF	Kim et al. (2007). Kim S, Malinverni JC, Sliz P, Silhavy TJ, Harrison SC, & Kahne D (2007). Structure and function of an essential component of the outer membrane protein assembly machine. Science 317 :961-964. PubMed Id: 17702946.
*BamA_21-410 POTRA domains (periplasmic fragment): Escherichia coli* B Bacteria, 3.3 Å** BamA was formerly named YaeT. The polypeptide transport-associated (POTRA) domains link to a transmembrane β-barrel, which is absent in this structure. Structure shows the first four POTRA domains in an extended conformation.	3EFC	Data File Jmol Viewer 3EFC	Gatzeva-Topalova et al. (2008). Gatzeva-Topalova PZ, Walton TA, & Sousa MC (2008). Crystal Structure of YaeT: Conformational flexibility and substrate recognition. Structure 16 :1873-1881. PubMed Id: 19081063.
*BamA_21-174 POTRA domains 1 and 2: Escherichia coli* B Bacteria, NMR Structure** BamA was formerly named YaeT.	2V9H	Data File Jmol Viewer 2V9H	Knowles et al. (2008). Knowles TJ, Jeeves M, Bobat S, Dancea F, McClelland D, Palmer T, Overduin M, & Henderson IR (2008). Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes. Mol Microbiol 68 :1216-1227. PubMed Id: 18430136.
*BamA_264-424 POTRA domains 4 and 5: Escherichia coli* B Bacteria, 2.69 Å** BamA was formerly named YaeT. From this structure and earlier ones (above), Gatzeva-Topalova et al. have constructed a 'spliced' model for the complete POTRA1-5 structure.	3OG5	Data File Jmol Viewer 3OG5	Gatzeva-Topalova et al. (2010). Gatzeva-Topalova PZ, Warner LR, Pardi A, & Sousa MC (2010). Structure and Flexibility of the Complete Periplasmic Domain of BamA: The Protein Insertion Machine of the Outer Membrane. Structure 18 :1492-1501. PubMed Id: 21070948.
*BamA_266-420 POTRA domains 4 and 5: Escherichia coli* B Bacteria, 1.5 Å** BamA formerly named YaeT.	3Q6B	Data File Jmol Viewer 3Q6B	Zhang et al. (2011). Zhang H, Gao ZQ, Hou HF, Xu JH, Li LF, Su XD, & Dong YH (2011). High-resolution structure of a new crystal form of BamA POTRA4-5 from Escherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun F67 :734-738. PubMed Id: 21795783. doi:10.1107/S1744309111014254.
*BamA with POTRA domain 5: Escherichia coli* B Bacteria, 3.00 Å**	4C4V	Data File Jmol Viewer 4C4V	Albrecht et al. (2014). Albrecht R, Schütz M, Oberhettinger P, Faulstich M, Bermejo I, Rudel T, Diederichs K, & Zeth K (2014). Structure of BamA, an essential factor in outer membrane protein biogenesis. Acta Crystallogr D Biol Crystallogr 70 :1779-1789. PubMed Id: 24914988. doi:10.1107/S1399004714007482.
*BamA_421-810 (without POTRA domains) with a 9 AA (MENVALDFS) C-terminal extension: Escherichia coli* B Bacteria, 2.2 Å** This structure was part of an effort to obtain NMR data. The work resulted in 70% complete sequence-specific NMR spectra.	6FSU	Data File Jmol Viewer 6FSU	Hartmann et al. (2018). Hartmann JB, Zahn M, Burmann IM, Bibow S, & Hiller S (2018). Sequence-Specific Solution NMR Assignments of the β-Barrel Insertase BamA to Monitor Its Conformational Ensemble at the Atomic Level. J Am Chem Soc 140 36:11252-11260. PubMed Id: 30125090. doi:10.1021/jacs.8b03220.
*BamA in complex with nanobody E6: Escherichia coli* B Bacteria, 1.94 Å** in complex with nanobody F7, 2.2 Å: 6QGX in complex with nanobody B12, 2.51 Å: 6QGY	6QGW	Data File Jmol Viewer 6QGW 6QGY 6QGX	Kaur et al. (2019). Kaur H, Hartmann JB, Jakob RP, Zahn M, Zimmermann I, Maier T, Seeger MA, & Hiller S (2019). Identification of conformation-selective nanobodies against the membrane protein insertase BamA by an integrated structural biology approach. J Biomol NMR 73 :375-384. PubMed Id: 31073665. doi:10.1007/s10858-019-00250-8.
*BamB component of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 1.80 Å**	3PRW	Data File Jmol Viewer 3PRW	Heuck et al. (2011). Heuck A, Schleiffer A, & Clausen T (2011). Augmenting β-Augmentation: Structural Basis of How BamB Binds BamA and May Support Folding of Outer Membrane Proteins. J Mol Biol 406 :659-666. PubMed Id: 21236263.
*BamB component of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 2.60 Å**	3P1L	Data File Jmol Viewer 3P1L	Kim & Paetzel (2011). Kim KH & Paetzel M (2011). Crystal Structure of Escherichia coli BamB, a Lipoprotein Component of the β-Barrel Assembly Machinery Complex. J Mol Biol 406 :667-678. PubMed Id: 21168416.
*BamB component of the Bam β-barrel assembly machine, I222 space group: Escherichia coli* B Bacteria, 1.65 Å** P2₁2₁2₁ space group, 1.77 Å: 3Q7N P2₁3 space group, 2.09 Å: 3Q7O	3Q7M	Data File Jmol Viewer 3Q7M 3Q7O 3Q7N	Noinaj et al. (2011). Noinaj N, Fairman JW, & Buchanan SK (2011). Crystal structures The Crystal Structure of BamB Suggests Interactions with BamA and Its Role within the BAM Complex. J Mol Biol 407 :248-260. PubMed Id: 21277859.
*BamB component of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 2.60 Å**	2YH3	Data File Jmol Viewer 2YH3	Albrecht & Zeth (2011). Albrecht R & Zeth K (2011). Structural basis of outer membrane protein biogenesis in bacteria. J Biol Chem 286 :27792-27803. PubMed Id: 21586578. doi:10.1074/jbc.M111.238931.
*BamB component of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 2.00 Å**	3Q54	Data File Jmol Viewer 3Q54	Dong et al. (2012). Dong C, Yang X, Hou HF, Shen YQ, & Dong YH (2012). Structure of Escherichia coli BamB and its interaction with POTRA domains of BamA. Acta Crystallogr D Biol Crystallogr D68 :1134-1139. PubMed Id: 22948914. doi:10.1107/S0907444912023141.
*BamB in complex with POTRA 3-4 domains of BamA: Escherichia coli* B Bacteria, 2.15 Å**	4XGA	Data File Jmol Viewer 4XGA	Chen et al. (2016). Chen Z, Zhan LH, Hou HF, Gao ZQ, Xu JH, Dong C, & Dong YH (2016). Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA. Acta Crystallogr D Struct Biol 72 :236-244. PubMed Id: 26894671. doi:10.1107/S2059798315024729.
*BamC component of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 1.55 Å** C-terminal domain, residues 101-212	2YH6	Data File Jmol Viewer 2YH6	Albrecht & Zeth (2011). Albrecht R & Zeth K (2011). Structural basis of outer membrane protein biogenesis in bacteria. J Biol Chem 286 :27792-27803. PubMed Id: 21586578. doi:10.1074/jbc.M111.238931.
*BamC component of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 1.25 Å** N-terminal domain, residues 25-143	2YH5	Data File Jmol Viewer 2YH5	Albrecht & Zeth (2011). Albrecht R & Zeth K (2011). Structural basis of outer membrane protein biogenesis in bacteria. J Biol Chem 286 :27792-27803. PubMed Id: 21586578. doi:10.1074/jbc.M111.238931.
*BamC component of the Bam β-barrel assembly machine (N-term, 101-212): Escherichia coli* B Bacteria, NMR Structure** Structure obtained Using Rosetta with a limited NMR data set. C-term domain, 229-344: 2LAE	2LAF	Data File Jmol Viewer 2LAF 2LAE	Warner et al. (2011). Warner LR, Varga K, Lange OF, Baker SL, Baker D, Sousa MC, & Pardi A (2011). Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set. J Mol Biol 411 :83-95. PubMed Id: 21624375. doi:10.1016/j.jmb.2011.05.022.
*BamC component of the Bam β-barrel assembly machine (C-term, 224-343): Escherichia coli* B Bacteria, 1.50 Å**	3SNS	Data File Jmol Viewer 3SNS	Kim et al. (2011). Kim KH, Aulakh S, Tan W, & Paetzel M (2011). Crystallographic analysis of the C-terminal domain of the Escherichia coli lipoprotein BamC. Acta Crystallogr Sect F Struct Biol Cryst Commun 67 :1350-1358. PubMed Id: 22102230. doi:10.1107/S174430911103363X.
*BamD component of the Bam β-barrel assembly machine: Rhodothermus marinus* B Bacteria (expressed in E. coli), 2.15 Å** BamD associates with the membrane using a lipidated amino-terminal cysteine. BamE and BamC are thought to bind to the C-terminus of BamD.	3QKY	Data File Jmol Viewer 3QKY	Sandoval et al. (2011). Sandoval CM, Baker SL, Jansen K, Metzner SI, & Sousa MC (2011). Crystal Structure of BamD: An Essential Component of the β-Barrel Assembly Machinery of Gram-Negative Bacteria J Mol Biol 409 :348-357. PubMed Id: 21463635. doi:10.1016/j.jmb.2011.03.035.
*BamD component of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 1.80 Å**	2YHC	Data File Jmol Viewer 2YHC	Albrecht & Zeth (2011). Albrecht R & Zeth K (2011). Structural basis of outer membrane protein biogenesis in bacteria. J Biol Chem 286 :27792-27803. PubMed Id: 21586578. doi:10.1074/jbc.M111.238931.
*BamD component of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 2.60 Å**	3Q5M	Data File Jmol Viewer 3Q5M	Dong et al. (2012). Dong C, Hou HF, Yang X, Shen YQ, & Dong YH (2012). Structure of Escherichia coli BamD and its functional implications in outer membrane protein assembly. Acta Crystallogr D68 :95-101. PubMed Id: 22281737. doi:10.1107/S0907444911051031.
*BamD component of the Bam β-barrel assembly machine: Neisseria gonorrhoeae* B Bacteria (expressed in E. coli), 2.50 Å**	5WAQ	Data File Jmol Viewer 5WAQ	Sikora et al. (2018). Sikora AE, Wierzbicki IH, Zielke RA, Ryner RF, Korotkov KV, Buchanan SK, & Noinaj N (2018). Structural and functional insights into the role of BamD and BamE within the ?-barrel assembly machinery in Neisseria gonorrhoeae. J Biol Chem 293 :1106-1119. PubMed Id: 29229778. doi:10.1074/jbc.RA117.000437.
*BamE component of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, NMR structure**	2KM7	Data File Jmol Viewer 2KM7	Knowles et al. (2011). Knowles TJ, Browning DF, Jeeves M, Maderbocus R, Rajesh S, Sridhar P, Manoli E, Emery D, Sommer U, Spencer A, Leyton DL, Squire D, Chaudhuri RR, Viant MR, Cunningham AF, Henderson IR, Overduin M (2011). Structure and function of BamE within the outer membrane and the β-barrel assembly machine. EMBO Rep 12 :123-128. PubMed Id: 21212804.
*BamE component of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 1.80 Å**	2YH9	Data File Jmol Viewer 2YH9	Albrecht & Zeth (2011). Albrecht R & Zeth K (2011). Structural basis of outer membrane protein biogenesis in bacteria. J Biol Chem 286 :27792-27803. PubMed Id: 21586578. doi:10.1074/jbc.M111.238931.
*BamE component of the Bam β-barrel assembly machine: Neisseria gonorrhoeae* B Bacteria (expressed in E. coli), 2.45 Å**	5WAM	Data File Jmol Viewer 5WAM	Sikora et al. (2018). Sikora AE, Wierzbicki IH, Zielke RA, Ryner RF, Korotkov KV, Buchanan SK, & Noinaj N (2018). Structural and functional insights into the role of BamD and BamE within the ?-barrel assembly machinery in Neisseria gonorrhoeae. J Biol Chem 293 :1106-1119. PubMed Id: 29229778. doi:10.1074/jbc.RA117.000437.
*BamCD complex of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 2.90 Å** The BamC component is the N-terminal domain, residues 26-217. The BamD component includes residues 32-240.	3TGO	Data File Jmol Viewer 3TGO	Kim et al. (2011). Kim KH, Aulakh S, & Paetzel M (2011). Crystal Structure of β-Barrel Assembly Machinery BamCD Protein Complex J Biol Chem 286 :39116-39121. PubMed Id: 21937441. doi:10.1074/jbc.M111.298166.
*BamACDE complex of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 3.4 Å**	5EKQ	Data File Jmol Viewer 5EKQ	Bakelar et al. (2016). Bakelar J, Buchanan SK, & Noinaj N (2016). The structure of the β-barrel assembly machinery complex. Science 351 :180-186. PubMed Id: 26744406. doi:10.1126/science.aad3460.
*BepA (YfgC) BAM assembly-enhancing protease: Escherichia coli* B Bacteria, 2.60 Å**	6AIT	Data File Jmol Viewer 6AIT	Shahrizal et al. (2018). Shahrizal M, Daimon Y, Tanaka Y, Hayashi Y, Nakayama S, Iwaki S, Narita SI, Kamikubo H, Akiyama Y, & Tsukazaki T (2018). Structural Basis for the Function of the β-Barrel Assembly-Enhancing Protease BepA. J Mol Biol . PubMed Id: 30521812. doi:10.1016/j.jmb.2018.11.024.
*BamA-POTRA4-5-BamD fusion complex of the Bam β-barrel assembly machine: Rhodothermus marinus* B Bacteria (expressed in E. coli), 2.0 Å**	5EFR	Data File Jmol Viewer 5EFR	Bergal et al. (2016). Bergal HT, Hopkins AH, Metzner SI, & Sousa MC (2016). The Structure of a BamA-BamD Fusion Illuminates the Architecture of the β-Barrel Assembly Machine Core. Structure 24 :243-251. PubMed Id: 26749448. doi:10.1016/j.str.2015.10.030.
*BamABCDE complex of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 2.90 Å** BAM ACDE complex, 3.90 Å: 5D0Q	5D0O	Data File Jmol Viewer 5D0O 5D0Q	Gu et al. (2016). Gu Y, Li H, Dong H, Zeng Y, Zhang Z, Paterson NG, Stansfeld PJ, Wang Z, Zhang Y, Wang W, & Dong C (2016). Structural basis of outer membrane protein insertion by the BAM complex. Nature 531 :64-69. PubMed Id: 26901871. doi:10.1038/nature17199.
*BamABCDE complex of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 3.56 Å**	5AYW	Data File Jmol Viewer 5AYW	Han et al. (2016). Han L, Zheng J, Wang Y, Yang X, Liu Y, Sun C, Cao B, Zhou H, Ni D, Lou J, Zhao Y, & Huang Y (2016). Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins. Nat Struct Mol Biol 23 :192-196. PubMed Id: 26900875. doi:10.1038/nsmb.3181.
*BamABCDE complex of the Bam β-barrel assembly machine: Escherichia coli* B Bacteria, 4.9 Å** cryo-EM structure showing lateral opening of complex	5LGO	Data File Jmol Viewer 5LGO	Iadanza et al. (2016). Iadanza MG, Higgins AJ, Schiffrin B, Calabrese AN, Brockwell DJ, Ashcroft AE, Radford SE, & Ranson NA (2016). Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM. Nat Commun 7 :12865. PubMed Id: 27686148. doi:10.1038/ncomms12865.
*BamABCDE complex of the Bam β-barrel assembly machine engaged in folding BamA: Escherichia coli* B Bacteria, 4.10 Å** cryo-EM structure	6V05	Data File Jmol Viewer 6V05	Tomasek et al. (2020). Tomasek D, Rawson S, Lee J, Wzorek JS, Harrison SC, Li Z, & Kahne D (2020). Structure of a nascent membrane protein as it folds on the BAM complex. Nature 583 7816:473-478. PubMed Id: 32528179. doi:10.1038/s41586-020-2370-1.
*BamA in complex with RcsF: Escherichia coli* B Bacteria, 3.79 Å**	6T1W	Data File Jmol Viewer 6T1W	Rodríguez-Alonso et al. (2020). Rodríguez-Alonso R, Létoquart J, Nguyen VS, Louis G, Calabrese AN, Iorga BI, Radford SE, Cho SH, Remaut H, & Collet JF (2020). Structural insight into the formation of lipoprotein-β-barrel complexes. Nat Chem Biol 16 9:1019-1025. PubMed Id: 32572278. doi:10.1038/s41589-020-0575-0.
*BamABCDE complex in MSP1D1 nanodisc: Escherichia coli* B Bacteria, 6.65 Å** cryo-EM structure ensemble 0-2, 9.50 Å: 6SN2 ensemble 0-3, 8.40 Å: 6SN3 ensemble 0-4, 9.50 Å: 6SN4 ensemble 0-5, 9.80 Å: 6SN5 ensemble 0-6, 8.90 Å: 6SN7 ensemble 0-7, 8.40 Å: 6SN8 ensemble 0-8, 9.80 Å: 6SN9 ensemble 1-4, 8.50 Å: 6SOB ensemble 1-5, 9.00 Å: 6SOC ensemble 1-6, 8.30 Å: 6SOG ensemble 1-6, 9.50 Å: 6SOH ensemble 1-8, 10.40 Å: 6SOJ	6SMX	Data File Jmol Viewer 6SMX 6SOH 6SN9 6SN7 6SN3 6SN5 6SN8 6SOG 6SOJ 6SN2 6SN4 6SOB 6SOC	Iadanza et al. (2020). Iadanza MG, Schiffrin B, White P, Watson MA, Horne JE, Higgins AJ, Calabrese AN, Brockwell DJ, Tuma R, Kalli AC, Radford SE, & Ranson NA (2020). Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs. Commun Biol 3 1:776. PubMed Id: 33318620. doi:10.1038/s42003-020-01419-w.
*BamABCDE complex of the Bam β-barrel assembly machine, Lid-locked (LL), BamA E435C S665C: Escherichia coli* B Bacteria, 4.10 Å** cryo-EM structure BamA E435C S665C, lateral open conformation, 4.80 Å: 7NBX BamABCDE bound to a bactericidal Fab fragment, lateral open state, 5.20 Å: 7ND0 BamA E435C S665C, BamBDCE bound by a bactericidal Fab fragment, lateral open state, 7.10 Å: 7NCS	7BNQ	Data File Jmol Viewer 7BNQ 7NBX 7NCS 7ND0	White et al. (2021). White P, Haysom SF, Iadanza MG, Higgins AJ, Machin JM, Whitehouse JM, Horne JE, Schiffrin B, Carpenter-Platt C, Calabrese AN, Storek KM, Rutherford ST, Brockwell DJ, Ranson NA, & Radford SE (2021). The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding. Nat Commun 12 1:4174. PubMed Id: 34234105. doi:10.1038/s41467-021-24432-x.
*BamABCDE complex: Escherichia coli* B Bacteria, 3.05 Å** BAMA-β12^OmpLABCDE complex, 3.19 Å 6LYQ BAMA-β8^OmpABCDE complex, 3.28 Å 6LYR cryo-EM structure, 4.20 Å 6LYU	6LYS	Data File Jmol Viewer 6LYS 6LYU 6LYR 6LYQ	Xiao et al. (2021). Xiao L, Han L, Li B, Zhang M, Zhou H, Luo Q, Zhang X, & Huang Y (2021). Structures of the β-barrel assembly machine recognizing outer membrane protein substrates. FASEB J 35 1:e21207. PubMed Id: 33368572. doi:10.1096/fj.202001443RR.
*BamABCDE complex with bound darobactin: Escherichia coli* B Bacteria, 3.03 Å** cryo-EM structure x-ray structures: BamA in complex with darobactin (crystal form 1) 2.30 Å 7NRE BamA in complex with darobaction (crystal form 2) 2.20 Å 7NRF	7NRI	Data File Jmol Viewer 7NRI 7NRE 7NRF	Kaur et al. (2021). Kaur H, Jakob RP, Marzinek JK, Green R, Imai Y, Bolla JR, Agustoni E, Robinson CV, Bond PJ, Lewis K, Maier T, & Hiller S (2021). The antibiotic darobactin mimics a β-strand to inhibit outer membrane insertase. Nature 593 7857:125-129. PubMed Id: 33854236. doi:10.1038/s41586-021-03455-w.
*BamABCDE complex in MSP1D1 nanodisc: Escherichia coli* B Bacteria, 8.00 Å** cryo-EM structure in MSP2N2 nanodisc, 7.50 Å 7RI8 in MSP1E3D1 nanodisc, 6.90 Å 7RI9 in MSP1E3D1 nanodisc, 4.00 Å 7RI5 MSP1E3D1 nanodisc using E. coli outer membranes, 5.90 Å 7RI6 in complex with EspP, 7RJ5 BAM/EspP(beta9-12) hybrid-barrel intermediate, 3.40 Å 7RI4	7RI7	Data File Jmol Viewer 7RI7 7RI9 7RJ5 7RI4 7RI8 7RI6 7RI5	Wu et al. (2021). Wu R, Bakelar JW, Lundquist K, Zhang Z, Kuo KM, Ryoo D, Pang YT, Sun C, White T, Klose T, Jiang W, Gumbart JC, & Noinaj N (2021). Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM. Nat Commun 12 1:7131. PubMed Id: 34880256. doi:10.1038/s41467-021-27449-4.
*BamABCDE complex with bound EspP: Escherichia coli* B Bacteria, 3.60 Å** cryo-EM structure class 1, 4.50 Å 7TSZ class 2, 4.30 Å 7TT0 class 3, 4.20 Å 7TT2 class 4, 4.30 Å 7TT1 class 5, 4.30 Å 7TT3 class 6, 4.20 Å 7TT4 open-sheet EspP state, 4.30 Å 7TT5 intermediate-open EspP state, 4.30 Å 7TT6 barrelized EspP/continuous open BamA state, 4.80 Å 7TT7	7TTC	Data File Jmol Viewer 7TTC 7TT3 7TT6 7TT1 7TT5 7TT0 7TT7 7TT2 7TT4 7TSZ	Doyle et al. (2022). Doyle MT, Jimah JR, Dowdy T, Ohlemacher SI, Larion M, Hinshaw JE, & Bernstein HD (2022). Cryo-EM structures reveal multiple stages of bacterial outer membrane protein folding. Cell 185 7:1143-1156.e13. PubMed Id: 35294859. doi:10.1016/j.cell.2022.02.016.
*BamABCDE complex with bound darobactin 22: Escherichia coli* B Bacteria, 3.00 Å** cryo-EM structure with bound darobactin 9, 3.40 Å: 8ADi	8ADG	Data File Jmol Viewer 8ADG 8ADi	Seyfert et al. (2023). Seyfert CE, Porten C, Yuan B, Deckarm S, Panter F, Bader CD, Coetzee J, Deschner F, Tehrani KHME, Higgins PG, Seifert H, Marlovits TC, Herrmann J, & Müller R (2023). Darobactins Exhibiting Superior Antibiotic Activity by Cryo-EM Structure Guided Biosynthetic Engineering. Angew Chem Int Ed Engl 62 2:e202214094. PubMed Id: 36308277. doi:10.1002/anie.202214094.
*BamABCDE complex, wild-type: Escherichia coli* B Bacteria, 3.50 Å** cryo-EM structure with bound darobactin B, 3.30 Å: 8BVQ	8BWC	Data File Jmol Viewer 8BWC 8BVQ	Haysom et al. (2023). Haysom SF, Machin J, Whitehouse JM, Horne JE, Fenn K, Ma Y, El Mkami H, Böhringer N, Schäberle TF, Ranson NA, Radford SE, & Pliotas C (2023). Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex in E. coli Cells. Angew Chem Int Ed Engl :e202218783. PubMed Id: 37162386. doi:10.1002/anie.202218783.
*BamABCDE-EspP complex, G431C/G781C (BamA), N1293C/A1043C (EspP) mutants, in nanodisc: E. coli* B Bacteria, 3.40 Å** cryo-EM structure N427C (BamA), R1297C (EspP) mutants, 3.40 Å: 7YE6 G431C (BamA), N1293C (EspP) mutants, 3.50 Å: 8BNZ S425C (BamA), S1299C (EspP) mutants, 3.10 Å: 8BO2	7YE4	Data File Jmol Viewer 7YE4 8BO2 8BNZ 7YE6	Shen et al. (2023). Shen C, Chang S, Luo Q, Chan KC, Zhang Z, Luo B, Xie T, Lu G, Zhu X, Wei X, Dong C, Zhou R, Zhang X, Tang X, & Dong H (2023). Structural basis of BAM-mediated outer membrane β-barrel protein assembly. Nature 617 7959:185-193. PubMed Id: 37100902. doi:10.1038/s41586-023-05988-8.
*BamABCDE complex with bound dynobactin A: Escherichia coli* B Bacteria, 3.60 Å** cryo-EM structure	7R1W	Data File Jmol Viewer 7R1W	Miller et al. (2022). Miller RD, Iinishi A, Modaresi SM, Yoo BK, Curtis TD, Lariviere PJ, Liang L, Son S, Nicolau S, Bargabos R, Morrissette M, Gates MF, Pitt N, Jakob RP, Rath P, Maier T, Malyutin AG, Kaiser JT, Niles S, Karavas B, Ghiglieri M, Bowman SEJ, Rees DC, Hiller S, & Lewis K (2022). Computational identification of a systemic antibiotic for gram-negative bacteria. Nat Microbiol 7 10:1661-1672. PubMed Id: 36163500. doi:10.1038/s41564-022-01227-4.
Mitochondrial Outer Membrane Beta Barrel Proteins
*VDAC-1 voltage dependent anion channel: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure** Structure determined in LDAO micelles.	2K4T	Data File Jmol Viewer 2K4T	Hiller et al. (2008). Hiller S, Garces RG, Malia TJ, Orekhov VY, Colombini M, & Wagner G (2008). Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. Science 321 :1206-1210. PubMed Id: 18755977.
*VDAC-1 voltage dependent anion channel: Homo sapiens* E Eukaryota (expressed in E. coli), 4 Å** Structure determined by combining x-ray and NMR data.	2JK4	Data File Jmol Viewer 2JK4	Bayrhuber et al. (2008). Bayrhuber M, Meins T, Habeck M, Becker S, Giller K, Villinger S, Vonrhein C, Griesinger C, Zweckstetter M, & Zeth K (2008). Structure of the human voltage-dependent anion channel. Proc Natl Acad Sci USA 105 :15370-15375. PubMed Id: 18832158.
*VDAC-1 voltage dependent anion channel in complex with β-NADH: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure** structure determined in LDAO micelles VDAC-1 alone, refined structure. 6TIQ	6TIQ	Data File Jmol Viewer 6TIQ 6TIQ	Böhm et al. (2020). Böhm R, Amodeo GF, Murlidaran S, Chavali S, Wagner G, Winterhalter M, Brannigan G, & Hiller S (2020). The Structural Basis for Low Conductance in the Membrane Protein VDAC upon β-NADH Binding and Voltage Gating. Structure 28 2:206-214.e4. PubMed Id: 31862297. doi:10.1016/j.str.2019.11.015.
*VDAC-1 voltage dependent anion channel, E73V/C127A/C232S mutant in DMPC: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure**	7QI2	Data File Jmol Viewer 7QI2	Najbauer et al. (2022). Najbauer EE, Tekwani Movellan K, Giller K, Benz R, Becker S, Griesinger C, & Andreas LB (2022). Structure and Gating Behavior of the Human Integral Membrane Protein VDAC1 in a Lipid Bilayer. J Am Chem Soc 144 7:2953-2967. PubMed Id: 35164499. doi:10.1021/jacs.1c09848.
*VDAC-1 voltage dependent anion channel: Mus musculus* E Eukaryota (expressed in E. coli), 2.3 Å** Reveals the voltage-sensing N-terminal α-helix.	3EMN	Data File Jmol Viewer 3EMN	Ujwal et al. (2008). Ujwal R, Cascio D, Colletier JP, Faham S, Zhang J, Toro L, Ping P, & Abramson J (2008). The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating. Proc Natl Acad Sci USA 105 :17742-17747. PubMed Id: 18988731.
*VDAC-1 voltage dependent anion channel with bound ATP: Mus musculus* E Eukaryota (expressed in E. coli), 2.28 Å**	4C69	Data File Jmol Viewer 4C69	Choudhary et al. (2014). Choudhary OP, Paz A, Adelman JL, Colletier JP, Abramson J, & Grabe M (2014). Structure-guided simulations illuminate the mechanism of ATP transport through VDAC1. Nat Struct Mol Biol 21 7:626-632. PubMed Id: 24908397. doi:10.1038/nsmb.2841.
*VDAC-1 voltage dependent anion channel by micro electron diffraction (microED): Mus musculus* E Eukaryota (expressed in E. coli), 3.12 Å**	7KUH	Data File Jmol Viewer 7KUH	Martynowycz et al. (2020). Martynowycz MW, Khan F, Hattne J, Abramson J, & Gonen T (2020). MicroED structure of lipid-embedded mammalian mitochondrial voltage-dependent anion channel. Proc Natl Acad Sci U S A 117 51:32380-32385. PubMed Id: 33293416. doi:10.1073/pnas.2020010117.
*VDAC-2 voltage dependent anion channel: Danio rerio* E Eukaryota (expressed in E. coli), 2.80 Å** Double electron-electron resonance measurements indicate a population of oligomers.	4BUM	Data File Jmol Viewer 4BUM	Schredelseker et al. (2014). Schredelseker J, Paz A, López CJ, Altenbach C, Leung CS, Drexler MK, Chen JN, Hubbell WL, & Abramson J (2014). High-Resolution Structure and Double Electron-Electron Resonance of the Zebrafish Voltage Dependent Anion Channel 2 Reveal an Oligomeric Population. J Biol Chem 289 :12566-12577. PubMed Id: 24627492. doi:10.1074/jbc.M113.497438.
*Translocase of outer mitochondrial membrane (TOM) complex, model: Neurospora crassa* E Eukaryota, 6.8 Å** single-particle cryo-EM structure	5O8O	Data File Jmol Viewer 5O8O	Bausewein et al. (2017). Bausewein T, Mills DJ, Langer JD, Nitschke B, Nussberger S, & Kühlbrandt W (2017). Cryo-EM Structure of the TOM Core Complex from Neurospora crassa. Cell 170 :693-700.e7. PubMed Id: 28802041. doi:10.1016/j.cell.2017.07.012.
*Translocase of outer mitochondrial membrane (TOM) core complex: Neurospora crassa* E Eukaryota, 3.30 Å** cryo-EM structure	8B4I	Data File Jmol Viewer 8B4I	Ornelas et al. (2023). Ornelas P, Bausewein T, Martin J, Morgner N, Nussberger S, & Kühlbrandt W (2023). Two conformations of the Tom20 preprotein receptor in the TOM holo complex. Proc Natl Acad Sci U S A 120 34:e2301447120. PubMed Id: 37579144. doi:10.1073/pnas.2301447120.
*translocase of the outer mitochondrial membrane (TOM) complex: Saccharomyces cerevisiae* E Eukaryota, 3.81 Å** cryo-EM structure The TOM complex is comprised of the Tom40, Tom20, Tom22, and Tom70 receptors and the Tom5, Tom6, and Tom70 regulators.	6JNF	Data File Jmol Viewer 6JNF	Araiso et al. (2019). Araiso Y, Tsutsumi A, Qiu J, Imai K, Shiota T, Song J, Lindau C, Wenz LS, Sakaue H, Yunoki K, Kawano S, Suzuki J, Wischnewski M, Schütze C, Ariyama H, Ando T, Becker T, Lithgow T, Wiedemann N, Pfanner N, Kikkawa M, & Endo T (2019). Structure of the mitochondrial import gate reveals distinct preprotein paths. Nature 575 7782:395-401. PubMed Id: 31600774. doi:10.1038/s41586-019-1680-7.
*translocase of the outer mitochondrial membrane (TOM) complex, dimer: Saccharomyces cerevisiae* E Eukaryota, 3.06 Å** cryo-EM structure tetramer, 4.1 Å: 6UCV	6UCU	Data File Jmol Viewer 6UCU 6UCV	Tucker & Park (2019). Tucker K, & Park E (2019). Cryo-EM structure of the mitochondrial protein-import channel TOM complex at near-atomic resolution. Nat Struct Mol Biol 26 12:1158-1166. PubMed Id: 31740857. doi:10.1038/s41594-019-0339-2.
*Translocase of outer mitochondrial membrane (TOM) complex, SAM-Tom40 complex: Saccharomyces cerevisiae* E Eukaryota (expressed in HEK293 cells), 3.01 Å** cryo-EM structure SAM-Tom40/Tom5/Tom6 complex, 3.05 Å 7E4I	7E4H	Data File Jmol Viewer 7E4H 7E4I	Wang et al. (2021). Wang Q, Guan Z, Qi L, Zhuang J, Wang C, Hong S, Yan L, Wu Y, Cao X, Cao J, Yan J, Zou T, Liu Z, Zhang D, Yan C, & Yin P (2021). Structural insight into the SAM-mediated assembly of the mitochondrial TOM core complex. Science 373 6561:1377-1381. PubMed Id: 34446444. doi:10.1126/science.abh0704.
*translocase of the outer mitochondrial membrane (TOM) core complex: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure	7CK6	Data File Jmol Viewer 7CK6	Wang et al. (2020). Wang W, Chen X, Zhang L, Yi J, Ma Q, Yin J, Zhuo W, Gu J, & Yang M (2020). Atomic structure of human TOM core complex. Cell Discov 6 :67. PubMed Id: 33083003. doi:10.1038/s41421-020-00198-2.
*translocase of the outer mitochondrial membrane (TOM) core complex, dimeric complex: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure	7CP9	Data File Jmol Viewer 7CP9	Guan et al. (2021). Guan Z, Yan L, Wang Q, Qi L, Hong S, Gong Z, Yan C, & Yin P (2021). Structural insights into assembly of human mitochondrial translocase TOM complex. Cell Discov 7 1:22. PubMed Id: 33846286. doi:10.1038/s41421-021-00252-7.
*translocase of the outer mitochondrial membrane (TOM) including TOM22 and TOM20 cytosolic domains: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.53 Å** cryo-EM structure complex with cross-linking, 3.74 Å: 7VDD	7VD2	Data File Jmol Viewer 7VD2 7VDD	Su et al. (2022). Su J, Liu D, Yang F, Zuo MQ, Li C, Dong MQ, Sun S, & Sui SF (2022). Structural basis of Tom20 and Tom22 cytosolic domains as the human TOM complex receptors. Proc Natl Acad Sci U S A 119 26:e2200158119. PubMed Id: 35733257. doi:10.1073/pnas.2200158119.
Sorting & assembly Machinery (SAM) complex (Sam35, Sam37, Sam50) in nanodiscs (monomer): Thermothelomyces thermophilus (Myceliophthora thermophila) E Eukaryota (expressed in S. cerevisiae), 3.4 Å cryoEM structure dimer 1, 3.2 Å: 6WUL monomer from dimer 1, 3.0 Å: 6WUT in detergent, dimer 2, 3.6 Å: 6WUM in detergent, dimer 3, 3.9 Å: 6WUN in detergent, monomer, 3.7 Å: 6WUJ	6WUH	Data File Jmol Viewer 6WUH 6WUN 6WUJ 6WUL 6WUT 6WUM	Diederichs et al. (2020). Diederichs KA, Ni X, Rollauer SE, Botos I, Tan X, King MS, Kunji ERS, Jiang J, & Buchanan SK (2020). Structural insight into mitochondrial β-barrel outer membrane protein biogenesis. Nat Commun 11 1:3290. PubMed Id: 32620929. doi:10.1038/s41467-020-17144-1.
Lipopolysaccharide (LPS) Transport Proteins
*LptD-LptE lipopolysaccharide transport complex: Salmonella enterica* B Bacteria (expressed in E. coli), 2.80 Å** Structure provides the basis for LPS translocation across the outer membrane. LptD comprises residues 226-786. LptE comprises residues 19 - 169.	4N4R	Data File Jmol Viewer 4N4R	Dong et al. (2014). Dong H, Xiang Q, Gu Y, Wang Z, Paterson NG, Stansfeld PJ, He C, Zhang Y, Wang W, & Dong C (2014). Structural basis for outer membrane lipopolysaccharide insertion. Nature 511 :52-56. PubMed Id: 24990744. doi:10.1038/nature13464.
*LptD-LptE lipopolysaccharide transport complex: Shigella flexneri* B Bacteria (expressed in E. coli), 2.39 Å**	4Q35	Data File Jmol Viewer 4Q35	Qiao et al. (2014). Qiao S, Luo Q, Zhao Y, Zhang XC, & Huang Y (2014). Structural basis for lipopolysaccharide insertion in the bacterial outer membrane. Nature 511 :108-111. PubMed Id: 24990751. doi:10.1038/nature13484.
*LptE lipopolysaccharide transport protein: Escherichia coli* B Bacteria, 2.34 Å**	4NHR	Data File Jmol Viewer 4NHR	Malojčić et al. (2014). Malojčić G, Andres D, Grabowicz M, George AH, Ruiz N, Silhavy TJ, & Kahne D (2014). LptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface. Proc. Natl. Acad. Sci. U.S.A. 111 26:9467-9472. PubMed Id: 24938785. doi:10.1073/pnas.1402746111.
*PgaA exopolysaccharide transporter: Escherichia coli* B Bacteria, 2.82 Å**	4Y25	Data File Jmol Viewer 4Y25	Wang et al. (2016). Wang Y, Andole Pannuri A, Ni D, Zhou H, Cao X, Lu X, Romeo T, & Huang Y (2016). Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane. J Biol Chem 291 19:10046-10057. PubMed Id: 26957546. doi:10.1074/jbc.M115.711762.
*LptD-LptE lipopolysaccharide transport complex: Yersinia pestis* B Bacteria (expressed in E. coli), 2.75 Å**	5IXM	Data File Jmol Viewer 5IXM	Botos et al. (2016). Botos I, Majdalani N, Mayclin SJ, McCarthy JG, Lundquist K, Wojtowicz D, Barnard TJ, Gumbart JC, & Buchanan SK (2016). Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens. Structure 24 :965-976. PubMed Id: 27161977. doi:10.1016/j.str.2016.03.026.
*LptD-LptE lipopolysaccharide transport complex: Klebsiella pneumoniae* B Bacteria (expressed in E. coli), 2.94 Å** full-length protein, 4.37 Å: 5IV9	5IV8	Data File Jmol Viewer 5IV8 5IV9	Botos et al. (2016). Botos I, Majdalani N, Mayclin SJ, McCarthy JG, Lundquist K, Wojtowicz D, Barnard TJ, Gumbart JC, & Buchanan SK (2016). Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens. Structure 24 :965-976. PubMed Id: 27161977. doi:10.1016/j.str.2016.03.026.
*LptD-LptE lipopolysaccharide transport complex: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.99 Å**	5IVA	Data File Jmol Viewer 5IVA	Botos et al. (2016). Botos I, Majdalani N, Mayclin SJ, McCarthy JG, Lundquist K, Wojtowicz D, Barnard TJ, Gumbart JC, & Buchanan SK (2016). Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens. Structure 24 :965-976. PubMed Id: 27161977. doi:10.1016/j.str.2016.03.026.
*LptD-LptE lipopolysaccharide transport complex, in complex with ProMacrobodies: Neisseria gonorrhoeae* B Bacteria (expressed in E. coli), 3.40 Å** cryo-EM structure x-ray: structure of ProMacrobody 21 with bound maltose, 2.00 Å 7OMT	7OMM	Data File Jmol Viewer 7OMM 7OMT	Botte et al. (2022). Botte M, Ni D, Schenck S, Zimmermann I, Chami M, Bocquet N, Egloff P, Bucher D, Trabuco M, Cheng RKY, Brunner JD, Seeger MA, Stahlberg H, & Hennig M (2022). Cryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation. Nat Commun 13 1:1826. PubMed Id: 35383177. doi:10.1038/s41467-022-29459-2.
Polysaccharide Utilization Proteins Genes of this family are part of the starch utilization system (SUS)
*SusCD complex BT2261-2264, space group P1: Bacteroides thetaiotaomicron* B Bacteria, 2.75 Å** Space group P2₁2₁2₁, 3.4 Å: 5QF7 Space group P2₁, 2.8 Å: 5FQ6 BT2262 complex, 3.1 Å: 5QF3 BT2263 complex, 1.9 Å: 5FQ4 BT1762, 1.76 Å: 5LX8 BT1762-1763, 3.1 Å: 5T3R BT1762-1763, 3.1 Å: 5T4Y	5FQ8	Data File Jmol Viewer 5FQ8 5QF7 5LX8 5FQ6 5T3R 5FQ4 5QF3 5T4Y	Glenwright et al. (2017). Glenwright AJ, Pothula KR, Bhamidimarri SP, Chorev DS, Baslé A, Firbank SJ, Zheng H, Robinson CV, Winterhalter M, Kleinekathöfer U, Bolam DN, & van den Berg B (2017). Structural basis for nutrient acquisition by dominant members of the human gut microbiota. Nature 541 7637:407-411. PubMed Id: 28077872. doi:10.1038/nature20828.
*SusCD Fructo-oligosaccharide transporter BT 1762-63: Bacteroides thetaiotaomicron* B Bacteria, 2.69 Å** Fructo-oligosaccharide transporter BT 1762-63, 2.62 Å: 6Z8I Fructo-oligosaccharide transporter BT 1762-63, 3.10 Å: 6Z9A Open-open state of the Bt1762-Bt1763 levan transport system, 6ZLT Cryo_EM: Open-closed state of the Bt1762-Bt1763 levan transport system, 4.70 Å: 6ZM1 Cryo_EM: Closed-closed state of the Bt1762-Bt1763 levan transport system, 4.20 Å: 6ZLU	6ZAZ	Data File Jmol Viewer 6ZAZ 6ZLU 6Z9A 6ZM1 6Z8I 6ZLT	Gray et al. (2021). Gray DA, White JBR, Oluwole AO, Rath P, Glenwright AJ, Mazur A, Zahn M, Baslé A, Morland C, Evans SL, Cartmell A, Robinson CV, Hiller S, Ranson NA, Bolam DN, & van den Berg B (2021). Insights into SusCD-mediated glycan import by a prominent gut symbiont. Nat Commun 12 1:44. PubMed Id: 33398001. doi:10.1038/s41467-020-20285-y.
*RagAB peptide transporter: Porphyromonas gingivalis* B Bacteria, 3.04 Å** KRAB RagAB, 3.38 Å: 6SLI WT RagAB+P21, 2.61 Å: 6SLN	6SLJ	Data File Jmol Viewer 6SLJ 6SLI 6SLN	Madej et al. (2020). Madej M, White JBR, Nowakowska Z, Rawson S, Scavenius C, Enghild JJ, Bereta GP, Pothula K, Kleinekathoefer U, BasléA, Ranson NA, Potempa J, & van den Berg B (2020). Structural and functional insights into oligopeptide acquisition by the RagAB transporter from Porphyromonas gingivalis. Nat Microbiol 5 :1016-1025. PubMed Id: 32393857. doi:10.1038/s41564-020-0716-y.
Type II Secretion Systems
*GspD secretin: Escherichia coli* B Bacteria, 3.04 Å** cryo-EM structure	5WQ7	Data File Jmol Viewer 5WQ7	Yan et al. (2017). Yan Z, Yin M, Xu D, Zhu Y, & Li X (2017). Structural insights into the secretin translocation channel in the type II secretion system. Nat Struct Mol Biol 24 :177-183. PubMed Id: 28067918. doi:10.1038/nsmb.3350.
*GspD secretin: Vibrio cholerae* B Bacteria (expressed in E. coli), 3.26 Å** cryo-EM structure partially open state without the cap gate, 4.22 Å: 5WQ9	5WQ8	Data File Jmol Viewer 5WQ8 5WQ9	Yan et al. (2017). Yan Z, Yin M, Xu D, Zhu Y, & Li X (2017). Structural insights into the secretin translocation channel in the type II secretion system. Nat Struct Mol Biol 24 :177-183. PubMed Id: 28067918. doi:10.1038/nsmb.3350.
*bacterial type II secretion system, core architecture: Klebsiella pneumoniae* B Bacteria (expressed in E.coli), 4.3 Å** cryo-EM structure The inner membrane assembly platform consists of PulC, PulE, PulL, PulM, & PulN (2:1:1:1:1)	6HCG	Data File Jmol Viewer 6HCG	Chernyatina & Low (2019). Chernyatina AA, & Low HH (2019). Core architecture of a bacterial type II secretion system. Nat Commun 10 1. PubMed Id: 31780649. doi:10.1038/s41467-019-13301-3.
*secretin pore pIV: Enterobacteria phage f1* V Viruses (expressed in E. coli), 2.70 Å** cryo-EM structure	7OFH	Data File Jmol Viewer 7OFH	Conners et al. (2021). Conners R, McLaren M, Łapińska U, Sanders K, Stone MRL, Blaskovich MAT, Pagliara S, Daum B, Rakonjac J, & Gold VAM (2021). CryoEM structure of the outer membrane secretin channel pIV from the f1 filamentous bacteriophage. Nat Commun 12 1:6316. PubMed Id: 34728631. doi:10.1038/s41467-021-26610-3.
Type III Secretion Systems
*T3S injectisome basal body: Salmonella enterica* B Bacteria, 6.3 Å** cryo-EM structure periplasmic domains of PrgH and PrgK, 4.3 Å: 5TCP secretin InvG, 3.6 Å: 5TCQ	5TCR	Data File Jmol Viewer 5TCR 5TCQ 5TCP	Worrall et al. (2016). Worrall LJ, Hong C, Vuckovic M, Deng W, Bergeron JR, Majewski DD, Huang RK, Spreter T, Finlay BB, Yu Z, & Strynadka NC (2016). Near-atomic-resolution cryo-EM analysis of the Salmonella T3S injectisome basal body. Nature 540 :597-601. PubMed Id: 27974800. doi:10.1038/nature20576.
*MS-ring of the flagellar rotor protein FliF, 33mer: Salmonella enterica* B Bacteria (expressed in E. coli), 3.10 Å** cryo-EM structure RBM3/collar region, 2.60 Å: 6SD1 RBM2 inner region (21-fold symmetry applied), 3.10 Å: 6SD2 34mer structure, 3.30 Å: 6SD3 RBM3/collar region (34-fold symmetry applied), 2.80 Å: 6SD4 RBM2 inner ring (22-fold symmetry applied), 3.10 Å: 6SD5 RBM3/collar region (32-fold symmetry applied), 3.30 Å: 6TRE	6SCN	Data File Jmol Viewer 6SCN 6SD5 6SD4 6TRE 6SD1 6SD3 6SD2	Johnson et al. (2020). Johnson S, Fong YH, Deme JC, Furlong EJ, Kuhlen L, & Lea SM (2020). Symmetry mismatch in the MS-ring of the bacterial flagellar rotor explains the structural coordination of secretion and rotation. Nat Microbiol 5 7:966-975. PubMed Id: 32284565. doi:10.1038/s41564-020-0703-3.
*Type III secretion pilotin InvH: Salmonella enterica* B Bacteria (expressed in E. coli), 1.20 Å** pilotin-secretin complex InvH-InvG, 1.85 Å: 6XFK pilotin-secretin complex InvH-InvG, NMR structure: 6XFL	6XFJ	Data File Jmol Viewer 6XFJ 6XFL 6XFK	Majewski et al. (2021). Majewski DD, Okon M, Heinkel F, Robb CS, Vuckovic M, McIntosh LP, & Strynadka NCJ (2021). Characterization of the Pilotin-Secretin Complex from the Salmonella enterica Type III Secretion System Using Hybrid Structural Methods. Structure 29 2:125-138.e5. PubMed Id: 32877645. doi:10.1016/j.str.2020.08.006.
*type III secretion system export apparatus, apo state: Salmonella enterica* B Bacteria, 3.60 Å** cryo-EM structure needle complex, SpaR state 1, 3.30 Å: 7AH9 needle complex, SpaR state 2, 3.30 Å: 7AHI	7AGX	Data File Jmol Viewer 7AGX 7AHI 7AH9	Miletic et al. (2021). Miletic S, Fahrenkamp D, Goessweiner-Mohr N, Wald J, Pantel M, Vesper O, Kotov V, & Marlovits TC (2021). Substrate-engaged type III secretion system structures reveal gating mechanism for unfolded protein translocation. Nat Commun 12 1:1546. PubMed Id: 33750771. doi:10.1038/s41467-021-21143-1.
*nonameric SsaV cytosolic domain in the context of the InvA-SsaV chimeric protein: Salmonella enterica* B Bacteria (expressed in E. coli), 2.11 Å** cryo-EM structure nonameric SsaV cytosolic domain with C9 symmetry, 3.64 Å 7FEC nonameric SsaV cytosolic domain with D9 symmetry, 3.55 Å 7FED	7FEB	Data File Jmol Viewer 7FEB 7FEC 7FED	Xu et al. (2021). Xu J, Wang J, Liu A, Zhang Y, & Gao X (2021). Structural and Functional Analysis of SsaV Cytoplasmic Domain and Variable Linker States in the Context of the InvA-SsaV Chimeric Protein. Microbiol Spectr 9 3:e01251-21. PubMed Id: 34851139. doi:10.1128/Spectrum.01251-21.
*T3S FliP-FliQ-FliR core complex: Salmonella typhimurium* B Bacteria (expressed in E. coli), 4.2 Å** cryo-EM structure	6F2D	Data File Jmol Viewer 6F2D	Kuhlen et al. (2018). Kuhlen L, Abrusci P, Johnson S, Gault J, Deme J, Caesar J, Dietsche T, Mebrhatu MT, Ganief T, Macek B, Wagner S, Robinson CV, & Lea SM (2018). Structure of the core of the type III secretion system export apparatus. Nat Struct Mol Biol 25 7:583-590. PubMed Id: 29967543. doi:10.1038/s41594-018-0086-9.
*T3S injectisome needle complex: Periplasmic domains of PrgH and PrgK: Salmonella typhimurium* B Bacteria, 3.6 Å** cryo-EM structure injectisome secretin InvG in the open gate state, 4.1 Å: 6DV3 injectisome secretin InvG (residues 176-end) in the open gate state, 3.9 Å: 6DV6 injectisome needle filament, 3.3 Å: 6DWB	6DUZ	Data File Jmol Viewer 6DUZ 6DV6 6DWB 6DV3	Hu et al. (2018). Hu J, Worrall LJ, Hong C, Vuckovic M, Atkinson CE, Caveney N, Yu Z, & Strynadka NCJ (2018). Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin. Nat Commun 9 1. PubMed Id: 30242280. doi:10.1038/s41467-018-06298-8.
*T3S injectisome needle complex: Salmonella typhimurium* B Bacteria, 5.15 Å** cryo-EM structure InvG secretin domain beta-barrel, 3.42 Å: 6PEE Focused refinement of InvGN0N1:SpaPQR:PrgHK, 3.5 Å: 6PEM Focused refinement of InvGN0N1:SpaPQR:PrgIJ, 3.8 Å: 6PEP injectisome NC-base, 3.8 Å: 6Q14 Focused refinement of InvGN0N1:PrgHK:SpaPQR:PrgIJ, 4.1 Å: 6Q16	6Q15	Data File Jmol Viewer 6Q15 6Q16 6Q14 6PEM 6PEE 6PEP	Hu et al. (2019). Hu J, Worrall LJ, Vuckovic M, Hong C, Deng W, Atkinson CE, Brett Finlay B, Yu Z, & Strynadka NCJ (2019). T3S injectisome needle complex structures in four distinct states reveal the basis of membrane coupling and assembly. Nat Microbiol 4 11:2010-2019. PubMed Id: 31427728. doi:10.1038/s41564-019-0545-z.
*Type III secretion system (T3SS): MxiD N0 N1 and MxiG C-terminal domains: Shigella flexneri* B Bacteria, 3.86 Å** cryo-EM structure Periplasmic inner membrane ring, 3.55 Å: 6RWX Export apparatus core and inner rod, 5.11 Å: 6RWY	6RWK	Data File Jmol Viewer 6RWK 6RWY 6RWX	Lunelli et al. (2020). Lunelli M, Kamprad A, Bürger J, Mielke T, Spahn CMT, & Kolbe M (2020). Cryo-EM structure of the Shigella type III needle complex. PLoS Pathog 16 2. PubMed Id: 32092125. doi:10.1371/journal.ppat.1008263.
*Type III secretion system (T3SS): Export apparatus core, inner rod and needle: Shigella flexneri* B Bacteria, 4.05 Å** cryo-EM structure Outer membrane secretin pore, 3.42 Å: 8AXL Inner membrane ring and secretin N0 N1 domains, 3.34 Å: 8AXN	8AXK	Data File Jmol Viewer 8AXK 8AXN 8AXL	Flacht et al. (2023). Flacht L, Lunelli M, Kaszuba K, Chen ZA, O' Reilly FJ, Rappsilber J, Kosinski J, & Kolbe M (2023). Integrative structural analysis of the type III secretion system needle complex from Shigella flexneri. Protein Sci :e4595. PubMed Id: 36790757. doi:10.1002/pro.4595.
*T3S FliP-FliQ complex: Vibrio mimicus* B Bacteria (expressed in E. coli), 4.10 Å** cryo-EM structure TS3 FliPQR-FlhB complex, 3.20 Å: 6S3L	6S3S	Data File Jmol Viewer 6S3S 6S3L	Kuhlen et al. (2020). Kuhlen L, Johnson S, Zeitler A, Bäurle S, Deme JC, Caesar JJE, Debo R, Fisher J, Wagner S, & Lea SM (2020). The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion. Nat Commun 11 1:1296. PubMed Id: 32157081. doi:10.1038/s41467-020-15071-9.
*T3S FliPQR complex: Pseudomonas savastanoi* B Bacteria (expressed in E. coli), 3.50 Å** cryo-EM structure	6S3R	Data File Jmol Viewer 6S3R	Kuhlen et al. (2020). Kuhlen L, Johnson S, Zeitler A, Bäurle S, Deme JC, Caesar JJE, Debo R, Fisher J, Wagner S, & Lea SM (2020). The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion. Nat Commun 11 1:1296. PubMed Id: 32157081. doi:10.1038/s41467-020-15071-9.
*type III secretion system EspA filament: Escherichia coli* B Bacteria, 3.40 Å** cryo-EM structure	7KHW	Data File Jmol Viewer 7KHW	Zheng et al. (2021). Zheng W, Peña A, Ilangovan A, Clark JN, Frankel G, Egelman EH, & Costa TRD (2021). Cryoelectron-microscopy structure of the enteropathogenic Escherichia coli type III secretion system EspA filament. Proc Natl Acad Sci U S A 118 2:e2022826118. PubMed Id: 33397726. doi:10.1073/pnas.2022826118.
*type III secretion system EspA filament: Escherichia coli* B Bacteria, 3.56 Å** cryo-EM structure	7K7K	Data File Jmol Viewer 7K7K	Lyons et al. (2021). Lyons BJE, Atkinson CE, Deng W, Serapio-Palacios A, Finlay BB, & Strynadka NCJ (2021). Cryo-EM structure of the EspA filament from enteropathogenic Escherichia coli: Revealing the mechanism of effector translocation in the T3SS. Structure 29 5:479-487.e4. PubMed Id: 33453150. doi:10.1016/j.str.2020.12.009.
*Type III secretion export gate YscV with substrate:chaperone complex YscX:YscY: Yersinia enterocolitica* B Bacteria (expressed in E. coli), 4.10 Å** secretion proteins YscX₅₀:YscY, 1.92 Å: 7QIH secretion proteins YscX₃₂:YscY, 3.29 Å: 7QII	7QIJ	Data File Jmol Viewer 7QIJ 7QIH 7QII	Gilzer et al. (2022). Gilzer D, Schreiner M, & Niemann HH (2022). Direct interaction of a chaperone-bound type III secretion substrate with the export gate. Nat Commun 13 1:2858. PubMed Id: 35654781. doi:10.1038/s41467-022-30487-1.
Type IV Secretion Systems
*Type IV outer membrane secretion complex: Escherichia coli* B Bacteria, 2.60 Å** Comprised of 14 copies each of TraF, TraO, and TraN; 590 kDa.	3JQO	Data File Jmol Viewer 3JQO	Chandran et al. (2009). Chandran V, Fronzes R, Duquerroy S, Cronin N, Navaza J, & Waksman G (2009). Structure of the outer membrane complex of a type IV secretion system. Nature 462 :1011-1015. PubMed Id: 19946264.
*Cag type IV secretion system, periplasmic ring complex (PRC): Helicobacter pylori* B Bacteria, 3.5 Å** cryo-EM structure CagT, 3.8 Å: 6OEE CagX, 3.8 Å: 6OEG CagY, 3.8 Å: 6ODI O-layer, 3.8 Å: 6OEF I-layer, 3.8 Å: 6OEH	6ODJ	Data File Jmol Viewer 6ODJ 6OEH 6OEE 6ODI 6OEF 6OEG	Chung et al. (2019). Chung JM, Sheedlo MJ, Campbell AM, Sawhney N, Frick-Cheng AE, Lacy DB, Cover TL, & Ohi MD (2019). Structure of the Helicobacter pylori Cag type IV secretion system. Elife 8 :e47644. PubMed Id: 31210639. doi:10.7554/eLife.47644.
*Cagβ₁ ATPase: Helicobacter pylori* B Bacteria (expressed in E. coli), 2.80 Å** Cagβ-AAD₁/CagZ, 2.10 Å: 6JHO	8DOL	Data File Jmol Viewer 8DOL 6JHO	Wu et al. (2023). Wu X, Zhao Y, Zhang H, Yang W, Yang J, Sun L, Jiang M, Wang Q, Wang Q, Ye X, Zhang X, & Wu Y (2023). Mechanism of regulation of the Helicobacter pylori Cagβ ATPase by CagZ. Nat Commun 14 1:479. PubMed Id: 36717564. doi:10.1038/s41467-023-36218-4.
*PilQ Type IV competence pilus secretin: Vibrio cholerae* B Bacteria, 2.70 Å** cryo-EM structure	6W6M	Data File Jmol Viewer 6W6M	Weaver et al. (2020). Weaver SJ, Ortega DR, Sazinsky MH, Dalia TN, Dalia AB, & Jensen GJ (2020). CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae. Nat Commun 11 1:5080. PubMed Id: 33033258. doi:10.1038/s41467-020-18866-y.
*Dot T4SS OMC type IV secretion system: Legionella pneumophila* B Bacteria, 3.50 Å** cryo-EM structure Dot T4SS PR, 3.70 Å: 6X64 Dot/Icm T4SS, 3.70 Å: 6X65 dDot T4SS OMC, 4.20 Å: 6X66	6X62	Data File Jmol Viewer 6X62 6X66 6X64 6X65	Durie et al. (2020). Durie CL, Sheedlo MJ, Chung JM, Byrne BG, Su M, Knight T, Swanson M, Lacy DB, & Ohi MD (2020). Structural analysis of the Legionella pneumophila Dot/Icm type IV secretion system core complex. Elife 9 :e59530. PubMed Id: 32876045. doi:10.7554/eLife.59530.
*PilQ Type IV competence pilus secretin tetramer bound by TsaP heptamer: Pseudomonas aeruginosa* B Bacteria, 4.30 Å** cryo-EM structure Tetradecameric PilQ, 4.30 Å: 6VE3 Pentadecameric PilQ, 6.90 Å: 6VE4	6VE2	Data File Jmol Viewer 6VE2 6VE3 6VE4	McCallum et al. (2021). McCallum M, Tammam S, Rubinstein JL, Burrows LL, & Howell PL (2021). CryoEM map of Pseudomonas aeruginosa PilQ enables structural characterization of TsaP. Structure 29 5:457-466.e4. PubMed Id: 33338410. doi:10.1016/j.str.2020.11.019.
*outer-membrane core complex (inner ring) from a conjugative type IV secretion system: Salmonella enterica* B Bacteria (expressed in E. coli), 3.34 Å** cryo-EM structure outer ring complex, 3.40 Å 7OKO	7OKN	Data File Jmol Viewer 7OKN 7OKO	Amin et al. (2021). Amin H, Ilangovan A, & Costa TRD (2021). Architecture of the outer-membrane core complex from a conjugative type IV secretion system. Nat Commun 12 1:6834. PubMed Id: 34824240. doi:10.1038/s41467-021-27178-8.
*outer-membrane core complex (inner ring) encoded by multi-drug resistance F plasmids, models for C13 reconstruction: Salmonella enterica* B Bacteria, 3.31 Å** cryo-EM structure Models for C17 reconstruction, 2.95 Å 7SPC Models for C13 reconstruction encoded by a plasmid overproducing TraV, TraK and TraB of pED208, 2.97 Å 7SPI Models for C17 reconstruction encoded by a plasmid overproducing TraV, TraK and TraB of pED208, 3.56 Å 7SPJ models for C16 reconstruction encoded by a plasmid overproducing TraV, TraK and TraB of pED208, 3.90 Å 7SPK	7SPB	Data File Jmol Viewer 7SPB 7SPI 7SPJ 7SPC 7SPK	Liu et al. (2022). Liu X, Khara P, Baker ML, Christie PJ, & Hu B (2022). Structure of a type IV secretion system core complex encoded by multi-drug resistance F plasmids. Nat Commun 13 1:379. PubMed Id: 35046412. doi:10.1038/s41467-022-28058-5.
Type VI Secretion Systems
*Type VI secretion system, TssK-TssF-TssG baseplate subcomplex: Escherichia coli* B Bacteria, 3.7 Å** cryo-EM structure	6N38	Data File Jmol Viewer 6N38	Park et al. (2018). Park YJ, Lacourse KD, Cambillau C, DiMaio F, Mougous JD, & Veesler D (2018). Structure of the type VI secretion system TssK-TssF-TssG baseplate subcomplex revealed by cryo-electron microscopy. Nat Commun 9 1. PubMed Id: 30568167. doi:10.1038/s41467-018-07796-5.
*Type VI secretion system, Tle1 effector bound to the VgrG spike: Escherichia coli* B Bacteria, 2.60 Å** cryo-EM structure VgrG spike, 2.30 Å: 6SK0 Tle hydrolase bound to the TTR domain of the VgrG spike, 2.60 Å: 6SKI	6SJL	Data File Jmol Viewer 6SJL 6SKI 6SK0	Flaugnatti et al. (2020). Flaugnatti N, Rapisarda C, Rey M, Beauvois SG, Nguyen VA, Canaan S, Durand E, Chamot-Rooke J, Cascales E, Fronzes R, & Journet L (2020). Structural basis for loading and inhibition of a bacterial T6SS phospholipase effector by the VgrG spike. EMBO J 39 11. PubMed Id: 32350888. doi:10.15252/embj.2019104129.
*PbuCsx28 protein, homo-octamer: Prevotella buccae* B Bacteria (expressed in E. coli), 3.65 Å** cryo-EM structure	8GI1	Data File Jmol Viewer 8GI1	VanderWal et al. (2023). VanderWal AR, Park JU, Polevoda B, Nicosia JK, Molina Vargas AM, Kellogg EH, & O'Connell MR (2023). Csx28 is a membrane pore that enhances CRISPR-Cas13b-dependent antiphage defense. Science 380 6643:410-415. PubMed Id: 37104586. doi:10.1126/science.abm1184.
Type IX Secretion Systems
*SprA-based type IX (type 9) secretion system translocon: Flavobacterium johnsoniae* B Bacteria, 3.5 Å** cryo-EM structure translocon plug-complex, 3.7 Å: 6H3J	6H3I	Data File Jmol Viewer 6H3I 6H3J	Lauber et al. (2018). Lauber F, Deme JC, Lea SM, & Berks BC (2018). Type 9 secretion system structures reveal a new protein transport mechanism. Nature 564 7734:77-82. PubMed Id: 30405243. doi:10.1038/s41586-018-0693-y.
Forespore Sporulation Channels These are ring-shaped conduits that connect the mother cell and forespore during sporulation.
*SpoIIIAG sporolation channel: Bacillus subtilis* B Bacteria (expressed in E. coli), 3.5 Å** cryo-EM structure	5WC3	Data File Jmol Viewer 5WC3	Zeytuni et al. (2017). Zeytuni N, Hong C, Flanagan KA, Worrall LJ, Theiltges KA, Vuckovic M, Huang RK, Massoni SC, Camp AH, Yu Z, & Strynadka NC (2017). Near-atomic resolution cryoelectron microscopy structure of the 30-fold homooligomeric SpoIIIAG channel essential to spore formation in Bacillus subtilis. Proc Natl Acad Sci USA 114 34:E7073-E7081. PubMed Id: 28784753. doi:10.1073/pnas.1704310114.
Gasdermin (GSDM) Family Gasdermins are multi-subunit β-barrel forming proteins The gasdermins are expressed in the skin, mucosa, and immune antigen-presenting cells.
*Gasdermin GSDMA3-NT pore: Mus musculus* E Eukaryota (expressed in E. coli), 3.8 Å** cryo-EM structure. C27-symmetry. monomer crystal structure, 1.90 Å: 5B5R	6CB8	Data File Jmol Viewer 6CB8 5B5R	Ruan et al. (2018). Ruan J, Xia S, Liu X, Lieberman J, & Wu H (2018). Cryo-EM structure of the gasdermin A3 membrane pore. Nature 557 7703:62-67. PubMed Id: 29695864. doi:10.1038/s41586-018-0058-6.
*Gasdermin D pore: Homo sapiens* E Eukaryota (expressed in E. coli), 3.90 Å** cryo-EM structure	6VFE	Data File Jmol Viewer 6VFE	Xia et al. (2021). Xia S, Zhang Z, Magupalli VG, Pablo JL, Dong Y, Vora SM, Wang L, Fu TM, Jacobson MP, Greka A, Lieberman J, Ruan J, & Wu H (2021). Gasdermin D pore structure reveals preferential release of mature interleukin-1. Nature 593 7860:607-611. PubMed Id: 33883744. doi:10.1038/s41586-021-03478-3.
*Gasdermin GSDMB pore: Homo sapiens* E Eukaryota (expressed in E. coli), 4.96 Å** cryo-EM structure pore without transmembrane β-barrel, 4.48 Å: 8ET1 in complex with shigella IpaH7.8, 3.80 Å: 8EFP	8ET2	Data File Jmol Viewer 8ET2 8EFP 8ET1	Wang et al. (2023). Wang C, Shivcharan S, Tian T, Wright S, Ma D, Chang J, Li K, Song K, Xu C, Rathinam VA, & Ruan J (2023). Structural basis for GSDMB pore formation and its targeting by IpaH7.8. Nature 616 7957:590-597. PubMed Id: 36991122. doi:10.1038/s41586-023-05832-z.
*Gasdermin GSDMB pore:: Homo sapiens* E Eukaryota (expressed in E. coli), 3.17 Å** cryo-EM structure x-ray: IpaH7.8-LRR and GSDMB isoform-4 complex, 2.70 Å: 8GTJ x-ray: IpaH7.8-LRR and GSDMB isoform-1 complex, 3.10 Å: 8GTK	8GTN	Data File Jmol Viewer 8GTN 8GTJ 8GTK	Zhong et al. (2023). Zhong X, Zeng H, Zhou Z, Su Y, Cheng H, Hou Y, She Y, Feng N, Wang J, Shao F, & Ding J (2023). Structural mechanisms for regulation of GSDMB pore-forming activity. Nature 616 7957:598-605. PubMed Id: 36991125. doi:10.1038/s41586-023-05872-5.
TRANSMEMBRANE PROTEINS: ALPHA-HELICAL
Adventitious Membrane Proteins: Alpha-helical Pore-forming Toxins.
*Cytolysin A (ClyA, aka HlyE): Escherichia coli* B Bacteria, 3.29 Å**	2WCD	Data File Jmol Viewer 2WCD	Mueller et al. (2009). Mueller M, Grauschopf U, Maier T, Glockshuber R, & Ban N (2009). The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism. Nature 459 :726-730. PubMed Id: 19421192.
*tripartite α-pore forming toxin, decameric pore of AhlB: Aeromonas hydrophila* B Bacteria (expressed in E. coli), 2.94 Å** pre-pore AhlB, 2.55 Å: 6H2F soluble AhlB, 2.33 Å: 6GRK AhlC, form 1, 2.35 Å: 6H2E AhlC, form 2, 2.62 Å: 6H2D AhlC triple head mutant, 1.92 Å: 6R1J	6GRJ	Data File Jmol Viewer 6GRJ 6R1J 6H2E 6GRK 6H2F 6H2D	Wilson et al. (2019). Wilson JS, Churchill-Angus AM, Davies SP, Sedelnikova SE, Tzokov SB, Rafferty JB, Bullough PA, Bisson C, & Baker PJ (2019). Identification and structural analysis of the tripartite α-pore forming toxin of Aeromonas hydrophila. Nat Commun 10 1. PubMed Id: 31263098. doi:10.1038/s41467-019-10777-x.
*SmhB pore of the tripartite α-pore forming toxin, Smh: Serratia marcescens* B Bacteria (expressed in E. coli), 6.98 Å** soluble SmhA, crystal form 1 2.98 Å: 7A26 soluble SmhA crystal, form 2 2.57 Å: 7A27 soluble SmhB, 1.84 Å: 1.84 Å: 6ZZ5 soluble SmhB crystal form 2, 1.86 Å: 6ZZH	7A0G	Data File Jmol Viewer 7A0G 7A26 7A27 6ZZ5 6ZZH	Churchill-Angus et al. (2021). Churchill-Angus AM, Schofield THB, Marlow TR, Sedelnikova SE, Wilson JS, Rafferty JB, & Baker PJ (2021). Characterisation of a tripartite ?-pore forming toxin from Serratia marcescens. Sci Rep 11 1:6447. PubMed Id: 33742033. doi:10.1038/s41598-021-85726-0.
*Cry6Aa toxin: Bacillus thuringiensis* B Bacteria (expressed in Pseudomonas fluorescens), 2.7 Å** trypsin-cleaved, 2.0 Å: 5KUC supersedes 5J65.	5KUD	Data File Jmol Viewer 5KUD 5KUC	Dementiev et al. (2016). Dementiev A, Board J, Sitaram A, Hey T, Kelker MS, Xu X, Hu Y, Vidal-Quist C, Chikwana V, Griffin S, McCaskill D, Wang NX, Hung SC, Chan MK, Lee MM, Hughes J, Wegener A, Aroian RV, Narva KE, & Berry C (2016). The pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE-family alpha pore-forming toxins. BMC Biol 14 :71. PubMed Id: 27576487. doi:10.1186/s12915-016-0295-9.
*FraC eukaryotic pore-forming toxin from sea anemone: Actinia fragacea* E Eukaryota, 1.80 Å**	3LIM	Data File Jmol Viewer 3LIM	Mechaly et al. (2011). Mechaly AE, Bellomio A, Gil-Cartón D, Morante K, Valle M, González-Mañas JM, & Guérin DM (2011). Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins. Structure 19 :181-191. PubMed Id: 21300287.
*FraC toxin pore with bound lipids: Actinia fragacea* E Eukaryota (expressed in E. coli), 3.14 Å** Water soluble monomer (I), 1.70 Å: 3VWI Water soluble monomer (II), 2.10 Å: 3W9P Dimer with phosphorylcholine (I), 1.60 Å: 4TSL Dimer with phosphorylcholine (II), 1.57 Å: 4TSN Lipid (DHPC) bound (I), 2.30 Å: 4TSO Lipid (DHPC) bound (II), 2.15 Å: 4TSP Lipid (DHPC) bound (III), 1.60 Å: 4TSQ	4TSY	Data File Jmol Viewer 4TSY 3VWI 4TSN 3W9P 4TSP 4TSL 4TSO 4TSQ	Tanaka et al. (2015). Tanaka K, Caaveiro JM, Morante K, González-Mañas JM, & Tsumoto K (2015). Structural basis for self-assembly of a cytolytic pore lined by protein and lipid. Nat Commun 6 :6337. PubMed Id: 25716479. doi:10.1038/ncomms7337.
*Dermicidin hexameric anti-microbial peptide channel: Homo sapiens* E Eukaryota (expressed in Synthetic construct), 2.49 Å**	2YMK	Data File Jmol Viewer 2YMK	Song et al. (2013). Song C, Weichbrodt C, Salnikov ES, Dynowski M, Forsberg BO, Bechinger B, Steinem C, de Groot BL, Zachariae U, & Zeth K (2013). Crystal structure and functional mechanism of a human antimicrobial membrane channel. Proc Natl Acad Sci USA 110 :4586-4591. PubMed Id: 23426625. doi:10.1073/pnas.1214739110.
*Tc Toxin, TcA prepore (TcdA1) subunit: Photorhabdus luminescens* B Bacteria (expressed in E. coli), 3.50 Å** TcB-TcC (TcdB2-TccC3) subunits, 2.17 Å: 4O9X See also EM structures deposited in Electron Microscopy Data Bank under accession numbers EMD-2551 and EMD-2552.	4O9Y	Data File Jmol Viewer 4O9Y 4O9X	Meusch et al. (2014). Meusch D, Gatsogiannis C, Efremov RG, Lang AE, Hofnagel O, Vetter IR, Aktories K, & Raunser S (2014). Mechanism of Tc toxin action revealed in molecular detail. Nature 508 :61-65. PubMed Id: 24572368. doi:10.1038/nature13015.
*Tc Toxin, TcA pore (TcdA1) embedded in lipid nanodiscs using flexible fitting: Photorhabdus luminescens* B Bacteria (expressed in E. coli), 3.46 Å** cryo-EM structure. without flexible fitting, 3.46 Å: 5LKI	5LKH	Data File Jmol Viewer 5LKH 5LKI	Gatsogiannis et al. (2016). Gatsogiannis C, Merino F, Prumbaum D, Roderer D, Leidreiter F, Meusch D, & Raunser S (2016). Membrane insertion of a Tc toxin in near-atomic detail. Nat Struct Mol Biol 23 :884-890. PubMed Id: 27571177. doi:10.1038/nsmb.3281.
*Tc holo toxin: Photorhabdus luminescens* B Bacteria (expressed in E. coli), 3.4 Å** cryo-EM structure TccC3-D651A mutant, 3.4 Å: 6SUE	6SUF	Data File Jmol Viewer 6SUF 6SUE	Roderer et al. (2019). Roderer D, Hofnagel O, Benz R, & Raunser S (2019). Structure of a Tc holotoxin pore provides insights into the translocation mechanism. Proc Natl Acad Sci USA 116 46:23083-23090. PubMed Id: 31666324. doi:10.1073/pnas.1909821116.
*Listeriolysin O pore-forming toxin: Listeria monocytogenes* B Bacteria, 2.15 Å** A model of the assembled pore contains 36 monomers. In that configuration, the membrane-spanning region of the toxin is a mix of α-helices and β-sheets	4CDB	Data File Jmol Viewer 4CDB	Köster et al. (2014). Köster S, van Pee K, Hudel M, Leustik M, Rhinow D, Kühlbrandt W, Chakraborty T, & Yildiz O (2014). Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation. Nat Commun 5 :3690. PubMed Id: 24751541. doi:10.1038/ncomms4690.
*XaxAB pore complex: Xenorhabdus nematophila* B Bacteria (expressed in E. coli), 4 Å** cryo-EM structure x-ray structure of XaxA monomer, 2.5 Å: 6GY8 x-ray structure of XaxB monomer, 3.4 Å: 6GY7	6GY6	Data File Jmol Viewer 6GY6 6GY7 6GY8	Schubert et al. (2018). Schubert E, Vetter IR, Prumbaum D, Penczek PA, & Raunser S (2018). Membrane insertion of α-xenorhabdolysin in near-atomic detail. Elife 7 :e38017. PubMed Id: 30010541. doi:10.7554/eLife.38017.
*VacA vacuolating cytotoxin A oligomeric assembly OA-1: Helicobacter pylori* B Bacteria, 3.2 Å** cryo-EM structure. The main structural elements are β-helices, but the pore is formed by transmembrane α-helices assembly OA-2a, 3.9 Å: 6NYG assembly OA-2b, 3.2 Å: 6NYJ assembly OA-2c, 3.7 Å: 6NYL assembly OA-2d, 3.6 Å: 6NYM assembly OA-2e, 3.5 Å: 6NYN	6NYF	Data File Jmol Viewer 6NYF 6NYL 6NYN 6NYG 6NYJ 6NYM	Zhang et al. (2019). Zhang K, Zhang H, Li S, Pintilie GD, Mou TC, Gao Y, Zhang Q, van den Bedem H, Schmid MF, Au SWN, & Chiu W (2019). Cryo-EM structures of Helicobacter pylori vacuolating cytotoxin A oligomeric assemblies at near-atomic resolution. Proc Natl Acad Sci USA 116 14:6800-6805. PubMed Id: 30894496. doi:10.1073/pnas.1821959116.
*VacA toxin oligomer: Helicobacter pylori* B Bacteria, 3.8 Å** cryo-EM structure	6ODY	Data File Jmol Viewer 6ODY	Su et al. (2019). Su M, Erwin AL, Campbell AM, Pyburn TM, Salay LE, Hanks JL, Lacy DB, Akey DL, Cover TL, & Ohi MD (2019). Cryo-EM Analysis Reveals Structural Basis of Helicobacter pylori VacA Toxin Oligomerization. J Mol Biol 431 10:1956-1965. PubMed Id: 30954575. doi:10.1016/j.jmb.2019.03.029.
*RhopH erythrocyte invasion protein complex, soluble form: Plasmodium falciparum* E Eukaryota, 2.92 Å** cryo-EM structure	7KIY	Data File Jmol Viewer 7KIY	Schureck et al. (2021). Schureck MA, Darling JE, Merk A, Shao J, Daggupati G, Srinivasan P, Olinares PDB, Rout MP, Chait BT, Wollenberg K, Subramaniam S, & Desai SA (2021). Malaria parasites use a soluble RhopH complex for erythrocyte invasion and an integral form for nutrient uptake. Elife 10 :e65282. PubMed Id: 33393463. doi:10.7554/eLife.65282.
*Vip3 vegetable insecticidal protein Vip3Bc1 tetramer: Bacillus thuringiensis* B Bacteria (expressed in Pseudomonas fluorescens), 3.90 Å** cryo-EM structure in processed activated state, 4.80 Å: 6YRG tetramer in processed activated state, 4.75 Å: 7NTX	6YRF	Data File Jmol Viewer 6YRF 7NTX 6YRG	Byrne et al. (2021). Byrne MJ, Iadanza MG, Perez MA, Maskell DP, George RM, Hesketh EL, Beales PA, Zack MD, Berry C, & Thompson RF (2021). Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane. Nat Commun 12 1:2791. PubMed Id: 33990582. doi:10.1038/s41467-021-23146-4.
De novo Designed Membrane Proteins Functional Proteins Designed from First Principles
*Zn²⁺-transporting four-helix bundle (space group P4₃2₁2): De novo designed* U Unclassified, 2.80 Å** Space group I4₁22, 2.70 Å: 4P6K Space group I2₁3, 2.80 Å: 4P6L NMR structure: 2MUZ	4P6J	Data File Jmol Viewer 4P6J 2MUZ 4P6K 4P6L	Joh et al. (2014). Joh NH, Wang T, Bhate MP, Acharya R, Wu Y, Grabe M, Hong M, Grigoryan G, & DeGrado WF (2014). De novo design of a transmembrane Zn²⁺-transporting four-helix bundle. Science 346 6216:1520-1524. PubMed Id: 25525248. doi:10.1126/science.1261172.
*Transmembrane protein TMHC2_E: De novo designed protein* U Unclassified (expressed in E. coli), 2.95 Å** Transmembrane protein TMHC4_R, 3.89 Å: 6B85	6B87	Data File Jmol Viewer 6B87 6B85	Lu et al. (2018). Lu P, Min D, DiMaio F, Wei KY, Vahey MD, Boyken SE, Chen Z, Fallas JA, Ueda G, Sheffler W, Mulligan VK, Xu W, Bowie JU, & Baker D (2018). Accurate computational design of multipass transmembrane proteins. Science 359 6379:1042-1046. PubMed Id: 29496880. doi:10.1126/science.aaq1739.
*PL5 synthetic transmembrane domain variant of human phospholamban: De novo designed* U Unclassified (expressed in E. coli), 3.17 Å** For wild-type phospholamban homopentamer, see 1ZLL PL5 was expressed in E. coli as a C-terminal fusion to T4-Lysozyme . protein stabilized by van der Waals interaction, 1.9 Å: 6MCT mini-eVgL membrane protein, C222₁ form-1, 2.5 Å: 6MPW mini-eVgL membrane protein, C222₁ form-2, 2.5 Å: 6MQ2	6MQU	Data File Jmol Viewer 6MQU 6MCT 6MPW 6MQ2 1ZLL phospholamban pentamer	Mravic et al. (2019). Mravic M, Thomaston JL, Tucker M, Solomon PE, Liu L, & DeGrado WF (2019). Packing of apolar side chains enables accurate design of highly stable membrane proteins. Science 363 6434:1418-1423. PubMed Id: 30923216. doi:10.1126/science.aav7541.
*Designed transmembrane pore, hexameric: De novo designed* U Unclassified (expressed in E. coli), 2.40 Å** hexameric helical-bundle protein, 2.70 Å: 6TMS octameric helical-bundle protein, 2.40 Å: 6O35 transmembrane nanopore, TMH4C4 by cryo-EM, 5.90 Å: 6M6Z	6TJ1	Data File Jmol Viewer 6TJ1 6O35 6TMS 6M6Z	Xu et al. (2020). Xu C, Lu P, Gamal El-Din TM, Pei XY, Johnson MC, Uyeda A, Bick MJ, Xu Q, Jiang D, Bai H, Reggiano G, Hsia Y, Brunette TJ, Dou J, Ma D, Lynch EM, Boyken SE, Huang PS, Stewart L, DiMaio F, Kollman JM, Luisi BF, Matsuura T, Catterall WA, & Baker D (2020). Computational design of transmembrane pores. Nature 585 7823:129-134. PubMed Id: 32848250. doi:10.1038/s41586-020-2646-5.
Novel Membrane Proteins Membrane proteins that are not readily classified
*Cathelicidin LL-37 antimicrobial peptide, C-terminal extension tetramer: Homo sapiens* E Eukaryota (expressed in chemical synthesis), 1.83 Å**	5G1J	Data File Jmol Viewer 5G1J	Sancho-Vaello et al. (2020). Sancho-Vaello E, Gil-Carton D, François P, Bonetti EJ, Kreir M, Pothula KR, Kleinekathöfer U, & Zeth K (2020). The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics. Sci Rep 10 1:17356. PubMed Id: 33060695. doi:10.1038/s41598-020-74401-5.
*YeeE thiosulfate transporter: Spirochaeta thermophila* B Bacteria (expressed in E. coli), 2.52 Å** inactive mutant C91A, 2.60 Å: 6LEP	6LEO	Data File Jmol Viewer 6LEO 6LEP	Tanaka et al. (2020). Tanaka Y, Yoshikaie K, Takeuchi A, Ichikawa M, Mori T, Uchino S, Sugano Y, Hakoshima T, Takagi H, Nonaka G, & Tsukazaki T (2020). Crystal structure of a YeeE/YedE family protein engaged in thiosulfate uptake. Sci Adv 6 35:eaba7637. PubMed Id: 32923628. doi:10.1126/sciadv.aba7637.
*Tweety homologs (TTYHs), TTYH2 in GDN: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure TTYH2 in lipid nanodiscs, 3.92 Å 7P5M TTYH1 in GDN, 4.00 Å 7PJ5 TTYH3 in Ca²⁺ and GDN, 3.20 Å 7P5C	7P54	Data File Jmol Viewer 7P54 7P5M 7P5C 7PJ5	Sukalskaia et al. (2021). Sukalskaia A, Straub MS, Deneka D, Sawicka M, & Dutzler R (2021). Cryo-EM structures of the TTYH family reveal a novel architecture for lipid interactions. Nat Commun 12 1:4893. PubMed Id: 34385445. doi:10.1038/s41467-021-25106-4.
*Tweety homolog (TTYH) proteins. TTYH2 cis-dimer: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure TTYH2 trans-dimer, 3.89 Å 7RTU monomeric TTYH2, 3.96 Å 7RTV TTYH3 cis-dimer, 3.23 Å 7RTW	7RTT	Data File Jmol Viewer 7RTT 7RTV 7RTW 7RTU	Li et al. (2021). Li B, Hoel CM, & Brohawn SG (2021). Structures of tweety homolog proteins TTYH2 and TTYH3 reveal a Ca²⁺-dependent switch from intra- to intermembrane dimerization. Nat Commun 12 1:6913. PubMed Id: 34824283. doi:10.1038/s41467-021-27283-8.
*TACAN (TMEM120A) protein, apo form: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure H196A H197A mutant form, 2.80 Å 7N0L	7N0K	Data File Jmol Viewer 7N0K 7N0L	Niu et al. (2021). Niu Y, Tao X, Vaisey G, Olinares PDB, Alwaseem H, Chait BT, & MacKinnon R (2021). Analysis of the mechanosensor channel functionality of TACAN. Elife 10 :e71188. PubMed Id: 34374644. doi:10.7554/eLife.71188.
*TACAN (TMEM120A) protein: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.24 Å** cryo-EM structure	7N7P	Data File Jmol Viewer 7N7P	Xue et al. (2021). Xue J, Han Y, Baniasadi H, Zeng W, Pei J, Grishin NV, Wang J, Tu BP, & Jiang Y (2021). TMEM120A is a coenzyme A-binding membrane protein with structural similarities to ELOVL fatty acid elongase. Elife 10 :e71220. PubMed Id: 34374645. doi:10.7554/eLife.71220.
*TACAN (TMEM120A) protein in CoASH-bound state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.69 Å** cryo-EM structure CoASH-free state, 4.00 Å 7F3U	7F3T	Data File Jmol Viewer 7F3T 7F3U	Rong et al. (2021). Rong Y, Jiang J, Gao Y, Guo J, Song D, Liu W, Zhang M, Zhao Y, Xiao B, & Liu Z (2021). TMEM120A contains a specific coenzyme A-binding site and might not mediate poking- or stretch-induced channel activities in cells. Elife 10 :e71474. PubMed Id: 34409941. doi:10.7554/eLife.71474.
*TACAN (TMEM120A) protein in a closed state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.66 Å** cryo-EM structure	7F6V	Data File Jmol Viewer 7F6V	Chen et al. (2022). Chen X, Wang Y, Li Y, Lu X, Chen J, Li M, Wen T, Liu N, Chang S, Zhang X, Yang X, & Shen Y (2022). Cryo-EM structure of the human TACAN in a closed state. Cell Rep 38 9:110445. PubMed Id: 35235791. doi:10.1016/j.celrep.2022.110445.
*marker of self 5-TM receptor CD47: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.40 Å** cryo-EM structure	7MYZ	Data File Jmol Viewer 7MYZ	Fenalti et al. (2021). Fenalti G, Villanueva N, Griffith M, Pagarigan B, Lakkaraju SK, Huang RY, Ladygina N, Sharma A, Mikolon D, Abbasian M, Johnson J, Hadjivassiliou H, Zhu D, Chamberlain PP, Cho H, & Hariharan K (2021). Structure of the human marker of self 5-transmembrane receptor CD47. Nat Commun 12 1:5218. PubMed Id: 34471125. doi:10.1038/s41467-021-25475-w.
*Meckel-Gruber protein Meckelin: Homo spiens* E Eukaryota (expressed in HEK293 cells), 3.34 Å** cryo-EM structure	7FH1	Data File Jmol Viewer 7FH1	Liu et al. (2021). Liu D, Qian D, Shen H, & Gong D (2021). Structure of the human Meckel-Gruber protein Meckelin. Sci Adv 7 45:eabj9748. PubMed Id: 34731008. doi:10.1126/sciadv.abj9748.
*endoplasmic reticulum protein Jagunal (JAGN1): Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 2.25 Å** The protein was stabilized for crystallization using a split superfolder green fluorescent protein (from Aequorea victoria) attached to N- and C-termini of JAGN1.	6WVD	Data File Jmol Viewer 6WVD	Liu et al. (2020). Liu S, Li S, Yang Y, & Li W (2020). Termini restraining of small membrane proteins enables structure determination at near-atomic resolution. Sci Adv 6 51:eabe3717. PubMed Id: 33355146. doi:10.1126/sciadv.abe3717.
*YejM/LapB complex involved in lipopolysaccharide synthesis: Escherichia coli* B Bacteria, 3.90 Å** cryo-EM structure	7T6D	Data File Jmol Viewer 7T6D	Shu & Mi (2022). Shu S & Mi W (2022). Regulatory mechanisms of lipopolysaccharide synthesis in Escherichia coli. Nat Commun 13 1:4576. PubMed Id: 35931690. doi:10.1038/s41467-022-32277-1.
*Voltage-sensor protein TMEM266, coiled-coiled region: Mus musculus* E Eukaryota (expressed in E. coli), 2.30 Å**	7WJT	Data File Jmol Viewer 7WJT	Kawai et al. (2022). Kawai T, Narita H, Konno K, Akter S, Andriani RT, Iwasaki H, Nishikawa S, Yokoi N, Fukata Y, Fukata M, Wiriyasermkul P, Kongpracha P, Nagamori S, Takao K, Miyakawa T, Abe M, Sakimura K, Watanabe M, Nakagawa A, & Okamura Y (2022). Insight into the function of a unique voltage-sensor protein (TMEM266) and its short form in mouse cerebellum. Biochem J 479 11:1127-1145. PubMed Id: 35574701. doi:10.1042/BCJ20220033.
Mammalian Cell Entry (MCE) Proteins These protein are involved in lipid trafficking between inner and outer bacterial membranes. The name originates from the erroneous early belief that they mediate mammalian cell entry in M. tuberculosis
*MlaD, core MCE domain: Escherichia coli* B Bacteria, 2.15 Å** MlaD, periplasmic domain, 2.85 Å: 5UW2 MlaC phospholipid binding protein, 1.50 Å: 5UWA lipid-bound toluene-tolerance protein from Pseudomonas putida, 2.60 Å: 5UWB PqiB, periplasmic domain from Pseudomonas putida by cryo-EM, 3.96 Å: 5UVN	5UW8	Data File Jmol Viewer 5UW8 5UWA 5UW2 5UVN 5UWB	Ekiert et al. (2017). Ekiert DC, Bhabha G, Isom GL, Greenan G, Ovchinnikov S, Henderson IR, Cox JS, & Vale RD (2017). Architectures of Lipid Transport Systems for the Bacterial Outer Membrane. Cell 169 2:273-285.e17. PubMed Id: 28388411. doi:10.1016/j.cell.2017.03.019.
*MlaFB component of MlaFEDB ABC transporter complex (dimer): Escherichia coli* B Bacteria, 2.90 Å** monomeric state, 2.60 Å: 6XGZ	6XGY	Data File Jmol Viewer 6XGY 6XGZ	Kolich et al. (2020). Kolich LR, Chang YT, Coudray N, Giacometti SI, MacRae MR, Isom GL, Teran EM, Bhabha G, & Ekiert DC (2020). Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation. Elife 9 . PubMed Id: 32602838. doi:10.7554/eLife.60030.
*MlaFEDB in nanodiscs with phospholipid substrates: Escherichia coi* B Bacteria, 3.05 Å** cryo-EM structure	6XBD	Data File Jmol Viewer 6XBD	Coudray et al. (2020). Coudray N, Isom GL, MacRae MR, Saiduddin MN, Bhabha G, & Ekiert DC (2020). Structure of bacterial phospholipid transporter MlaFEDB with substrate bound. Elife 9 :e62518. PubMed Id: 33236984. doi:10.7554/eLife.62518.
*MlaFEDB phospholipid transport system, apo protein: Escherichia coli* B Bacteria, 3.60 Å** cryo-EM structure in complex with phospholipid, 3.30 Å: 6ZY3 in complex with AMP-PNP, 3.30 Å: 6ZY9 in complex with ADP, 4.10 Å: 6ZY4	6ZY2	Data File Jmol Viewer 6ZY2 6ZY9 6ZY3 6ZY4	Tang et al. (2021). Tang X, Chang S, Qiao W, Luo Q, Chen Y, Jia Z, Coleman J, Zhang K, Wang T, Zhang Z, Zhang C, Zhu X, Wei X, Dong C, Zhang X, & Dong H (2021). Structural insights into outer membrane asymmetry maintenance in Gram-negative bacteria by MlaFEDB. Nat Struct Mol Biol 28 1:81-91. PubMed Id: 33199922. doi:10.1038/s41594-020-00532-y.
*MlaFEDB phospholipid transport system, nucleotide free: Escherichia coli* B Bacteria, 2.90 Å** cryo-EM structure ATP-bound EQtall conformation (Mutation of E170Q on MlaF), 4.30 Å: 7CGN ATP-bound EQclose conformation (Mutation of E170Q on MlaF), 3.70 Å: 7CH0	7CGE	Data File Jmol Viewer 7CGE 7CGN 7CH0	Chi et al. (2020). Chi X, Fan Q, Zhang Y, Liang K, Wan L, Zhou Q, & Li Y (2020). Structural mechanism of phospholipids translocation by MlaFEDB complex. Cell Res 30 12:1127-1135. PubMed Id: 32884137. doi:10.1038/s41422-020-00404-6.
*MlaFEDB phospholipid transport system, nucleotide free: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 3.10 Å** cryo-EM structure ATP-bound Vtrans1 conformation, 4.00 Å: 7D08 ATP-bound Vtrans2 conformation, 3.60 Å: 7D09 ADP-vanadate trapped Vclose conformation, 4.00 Å: 7D0A	7D06	Data File Jmol Viewer 7D06 7D0A 7D08 7D09	Zhang et al. (2020). Zhang Y, Fan Q, Chi X, Zhou Q, & Li Y (2020). Cryo-EM structures of Acinetobacter baumannii glycerophospholipid transporter. Cell Discov 6 1:86. PubMed Id: 33298869. doi:10.1038/s41421-020-00230-5.
*MlaFEBD phospholipid transport system: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 3.50 Å** cryo-EM structure with ADP-V, 3.90 Å 7CH8 with AMPPNP, 3.90 Å 7CHA E. coli MlaFEB, 3.90 Å 7CH7 E. coli MlaFEB with AMPPNP, 3.40 Å 7CH6	7CH9	Data File Jmol Viewer 7CH9 7CHA 7CH8 7CH7 7CH6	Zhou et al. (2021). Zhou C, Shi H, Zhang M, Zhou L, Xiao L, Feng S, Im W, Zhou M, Zhang X, & Huang Y (2021). Structural Insight into Phospholipid Transport by the MlaFEBD Complex from P. aeruginosa. J Mol Biol 433 13:166986. PubMed Id: 33845086. doi:10.1016/j.jmb.2021.166986.
*Mycobacterial lipid transporter Mce1 in complex with LucB, map 0: Mycolicibacterium smegmatis* B Bacteria, 2.71 Å** cryo-EM structure map 1, 2.76 Å: 8FED in the absence of LucB (Map2), 2.90 Å: 8FEE	8FEF	Data File Jmol Viewer 8FEF 8FEE 8FED	Chen et al. (2023). Chen J, Fruhauf A, Fan C, Ponce J, Ueberheide B, Bhabha G, & Ekiert DC (2023). Structure of an endogenous mycobacterial MCE lipid transporter. Nature 620 7973:445-452. PubMed Id: 37495693. doi:10.1038/s41586-023-06366-0.
Outer Membrane Proteins
*Wza translocon for capsular polysaccharides: Escherichia coli* B Bacteria, 2.25 Å** The first outer membrane protein that penetrates the membrane as an alpha-helix bundle. The intact protein is comprised of eight monomers.	2J58	Data File Jmol Viewer 2J58	Dong et al. (2006). Dong C, Beis K, Nesper J, Brunkan-LaMontagne AL, Clarke BR JM, Whitfield C, & Naismith JH (2006). Wza the translocon for E. coli. capsular polysaccharides defines a new class of membrane protein. Nature 444 :226-229. PubMed Id: 17086202.
*Porin B monomer: Corynebacterium glutamicum* B Bacteria (expressed in Escherichia coli), 1.82 Å** Putative helical porin, probably comprised of five monomers. Crystal form I. Crystal form II, 2.89 Å: 2VQH Crystal form IV, 4.20 Å: 2VQK Crystal form III, 3.16 Å: 2VQL	2VQG	Data File Jmol Viewer 2VQG 2VQH 2VQK 2VQL	Ziegler et al. (2008). Ziegler K, Benz R, & Schulz GE (2008). A putative alpha-helical porin from Corynebacterium glutamicum. J Mol Biol 379 :482-491. PubMed Id: 18462756.
*MlaA lipid transport protein in complex with OmpF: Klebsiella pneumoniae* B Bacteria (expressed in E. coli), 3.2 Å** in complex with OmpK36, 2.9 Å: 5NUP Serratia marcescens MlaA in complex with OmpF, 3.2 Å: 5NUQ in complex with OmpF and LPS, 3.29 Å: 5NUR	5NUO	Data File Jmol Viewer 5NUO 5NUR 5NUQ 5NUP	Abellón-Ruiz et al. (2017). Abellón-Ruiz J, Kaptan SS, Baslé A, Claudi B, Bumann D, Kleinekathöfer U, & van den Berg B (2017). Structural basis for maintenance of bacterial outer membrane lipid asymmetry. Nat Microbiol 2 12:1616-1623. PubMed Id: 29038444. doi:10.1038/s41564-017-0046-x.
Bacterial Cell Divison Proteins These proteins comprise the so-called 'divisome'
*CrgA cell division structural & regulatory protein: Mycobacterium tuberculosis* B Bacteria (expressed in E. coli), NMR Structure** Structure of protein determined using both oriented sample and magic-angle spinning NMR data from liquid-crystalline lipid bilayer preparation.	2MMU	Data File Jmol Viewer 2MMU	Das et al. (2015). Das N, Dai J, Hung I, Rajagopalan MR, Zhou HX, & Cross TA (2015). Structure of CrgA, a cell division structural and regulatory protein from Mycobacterium tuberculosis, in lipid bilayers. Proc Natl Acad Sci USA 112 2:E119-E126. PubMed Id: 25548160. doi:10.1073/pnas.1415908112.
*FtsB-FtsL-FtsQ (FtsBLQ) divisome complex: Escherichia coli* B Bacteria, 3.10 Å** FtsB (D59H mutant)-FtsL-FtsQ complex, 3.04 Å: 8HHF FtsB (E56A mutant)-FtsL-FtsQ complex, 3.30 Å: 8HHH	8HHG	Data File Jmol Viewer 8HHG 8HHH 8HHF	Nguyen et al. (2023). Nguyen HTV, Chen X, Parada C, Luo AC, Shih O, Jeng US, Huang CY, Shih YL, & Ma C (2023). Structure of the heterotrimeric membrane protein complex FtsB-FtsL-FtsQ of the bacterial divisome. Nat Commun 14 1:1903. PubMed Id: 37019934. doi:10.1038/s41467-023-37543-4.
Chemotaxis Protein Complexes
*Core Chemotaxis Signaling Unit, carrying QQQQ receptor mutation: Escherichia coli* B Bacteria, 8.38 Å** cryo-EM structure 2D array with subtomogram averaging	6S1K	Data File Jmol Viewer 6S1K	Cassidy et al. (2020). Cassidy CK, Himes BA, Sun D, Ma J, Zhao G, Parkinson JS, Stansfeld PJ, Luthey-Schulten Z, & Zhang P (2020). Structure and dynamics of the E. coli chemotaxis core signaling complex by cryo-electron tomography and molecular simulations. Commun Biol 3 1. PubMed Id: 31925330. doi:10.1038/s42003-019-0748-0.
Autoinducer Export Superfamily Proteins in this family are involved in cell-to-cell comminications, such as quorum sensing (QS)
*TqsA autoinducer-2 exporter: Escherichia coli* B Bacteria, 3.30 Å** cryo-EM structure	7NB6	Data File Jmol Viewer 7NB6	Khera et al. (2022). Khera R, Mehdipour AR, Bolla JR, Kahnt J, Welsch S, Ermler U, Muenke C, Robinson CV, Hummer G, Xie H, & Michel H (2022). Cryo-EM structures of pentameric autoinducer-2 exporter from Escherichia coli reveal its transport mechanism. EMBO J 41 18:e109990. PubMed Id: 35698912. doi:10.15252/embj.2021109990.
*YdiK autoinducer-2 exporter: Escherichia coli* B Bacteria, 2.80 Å** cryo-EM structure	7OT9	Data File Jmol Viewer 7OT9	Khera et al. (2022). Khera R, Mehdipour AR, Bolla JR, Kahnt J, Welsch S, Ermler U, Muenke C, Robinson CV, Hummer G, Xie H, & Michel H (2022). Cryo-EM structures of pentameric autoinducer-2 exporter from Escherichia coli reveal its transport mechanism. EMBO J 41 18:e109990. PubMed Id: 35698912. doi:10.15252/embj.2021109990.
Tetraspanins Mediate essential functions in the immune, reproductive, genitourinary, and auditory systems
*CD53 full-length tetraspanin: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 2.90 Å**	6WVG	Data File Jmol Viewer 6WVG	Yang et al. (2020). Yang Y, Liu XR, Greenberg ZJ, Zhou F, He P, Fan L, Liu S, Shen G, Egawa T, Gross ML, Schuettpelz LG, & Li W (2020). Open conformation of tetraspanins shapes interaction partner networks on cell membranes. EMBO J 39 18:e105246. PubMed Id: 32974937. doi:10.15252/embj.2020105246.
*CD81 full-length tetraspanin: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.95 Å**	5TCX	Data File Jmol Viewer 5TCX	Zimmerman et al. (2016). Zimmerman B, Kelly B, McMillan BJ, Seegar TC, Dror RO, Kruse AC, & Blacklow SC (2016). Crystal Structure of a Full-Length Human Tetraspanin Reveals a Cholesterol-Binding Pocket. Cell 167 4:1041-1051. PubMed Id: 27881302. doi:10.1016/j.cell.2016.09.056.
*CD81 full-length tetraspanin in complex with CD19 bound to coltuximab Fab fragment: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.80 Å** cryo-EM structure	7JIC	Data File Jmol Viewer 7JIC	Susa et al. (2021). Susa KJ, Rawson S, Kruse AC, & Blacklow SC (2021). Cryo-EM structure of the B cell co-receptor CD19 bound to the tetraspanin CD81. Science 371 6526:300-305. PubMed Id: 33446559. doi:10.1126/science.abd9836.
*CD9 full-length tetraspanin: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.70 Å**	6K4J	Data File Jmol Viewer 6K4J	Umeda et al. (2020). Umeda R, Satouh Y, Takemoto M, Nakada-Nakura Y, Liu K, Yokoyama T, Shirouzu M, Iwata S, Nomura N, Sato K, Ikawa M, Nishizawa T, & Nureki O (2020). Structural insights into tetraspanin CD9 function. Nat Commun 11 1. PubMed Id: 32231207. doi:10.1038/s41467-020-15459-7.
Membrane-Spanning 4-Domain (MS4) Family
*Integral membrane protein cluster of differentiation 20 (CD20) in complex with rituximab Fab: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.30 Å** cryo-EM structure	6VJA	Data File Jmol Viewer 6VJA	Rougé et al. (2020). Rougé L, Chiang N, Steffek M, Kugel C, Croll TI, Tam C, Estevez A, Arthur CP, Koth CM, Ciferri C, Kraft E, Payandeh J, Nakamura G, Koerber JT, & Rohou A (2020). Structure of CD20 in complex with the therapeutic monoclonal antibody rituximab. Science 367 6483:1224-1230. PubMed Id: 32079680. doi:10.1126/science.aaz9356.
Autonomously Folding "Membrane Proteins" (Sec-independent)
*Mistic membrane-integrating protein: Bacillus subtilis* B Bacteria, NMR structure** Note: This is not a membrane protein. It is included here because of general interest.	1YGM	Data File Jmol Viewer 1YGM	Roosild et al. (2005). Roosild TP, Greenwald J, Vega M, Castronovo S, Riek R, & Choe S (2005). NMR structure of Mistic, a membrane-integrating protein for membrane protein expression. Science 307 :1317-1321. PubMed Id: 15731457.
Virus Coat Proteins
*M13 Major Coat Protein in Dodecylphosphocholine micelles: Enterobacteria phage m13* V Viruses (expressed in E. coli), NMR Structure** In SDS micelles: 2CPS	2CPB	Data File Jmol Viewer 2CPB 2CPS M13 coat protein	Papavoine et al. (1998). Papavoine CH, Christiaans BE, Folmer RH, Konings RN, & Hilbers CW (1998). Solution structure of the M13 major coat protein in detergent micelles: a basis for a model of phage assembly involving specific residues. J Mol Biol 282 :401-419. PubMed Id: 9735296. doi:10.1006/jmbi.1998.1860.
*Pf1 Major Coat Protein: Pseudomonas phage Pf1* V Viruses, NMR Structure** The structure was determined by solid-state NMR using magnetically aligned bacteriophage particles.	1PJF	Data File Jmol Viewer 1PJF	Thiriot et al. (2004). Thiriot DS, Nevzorov AA, Zagyanskiy L, Wu CH, & Opella SJ (2004). Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy. J Mol Biol 341 :869-879. PubMed Id: 15288792. doi:10.1016/j.jmb.2004.06.038.
*Pf1 Major Coat Protein in lipid bilayers: Pseudomonas phage Pf1* V Viruses, NMR Structure**	2KSJ	Data File Jmol Viewer 2KSJ	Park et al. (2010). Park SH, Marassi FM, Black D, & Opella SJ (2010). Structure and dynamics of the membrane-bound form of Pf1 coat protein: implications of structural rearrangement for virus assembly. Biophys J 99 :1465-1474. PubMed Id: 20816058. doi:10.1016/j.bpj.2010.06.009.
*fd bacteriophage pVIII coat protein in lipid bilayers: Enterobacteria phage fd* V Viruses, NMR Structure**	1MZT	Data File Jmol Viewer 1MZT	Marassi & Opella (2003). Marassi FM & Opella SJ (2003). Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints. Protein Sci 12 :403-411. PubMed Id: 12592011. doi:10.1110/ps.0211503.
*fd bacteriophage pVIII coat protein in SDS micelles: Enterobacteria phage fd* V Viruses, NMR Structure**	1FDM	Data File Jmol Viewer 1FDM	Almeida & Opella (1997). Almeida FC & Opella SJ (1997). fd coat protein structure in membrane environments: structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix. J Mol Biol 270 :481-495. PubMed Id: 9237913. doi:10.1006/jmbi.1997.1114.
*HIV-1 Envelope spike (Env) protein: Human immunodeficiency virus 1* V Viruses (expressed in E. coli), NMR structure** Reconstituted in bicelles. Well-ordered trimer.	5JYN	Data File Jmol Viewer 5JYN	Dev et al. (2016). Dev J, Park D, Fu Q, Chen J, Ha HJ, Ghantous F, Herrmann T, Chang W, Liu Z, Frey G, Seaman MS, Chen B, & Chou JJ (2016). Structural basis for membrane anchoring of HIV-1 envelope spike. Science 353 :172-175. PubMed Id: 27338706. doi:10.1126/science.aaf7066.
Glycoproteins
*Glycophorin A (GpA) transmembrane-domain dimer: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure** GpA in dodecylphosphocholine micelles.	1AFO	Data File Jmol Viewer 1AFO glycophorin A	MacKenzie et al. (1997). MacKenzie KR, Prestegard JH, & Engelman DM (1997). A transmembrane helix dimer: structure and implications. Science 276 :131-133. PubMed Id: 9082985.
*Glycophorin A (GpA) transmembrane-domain dimer: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure** GpA in DMPC/DHPC bicelles. in DPC micelles, 2KPE	2KPF	Data File Jmol Viewer 2KPF 2KPE	Mineev et al. (2011). Mineev KS, Bocharov EV, Volynsky PE, Goncharuk MV, Tkach EN, Ermolyuk YS, Schulga AA, Chupin VV, Maslennikov IV, Efremov RG, & Arseniev AS (2011). Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments. Acta Naturae 3 2:90-98. PubMed Id: 22649687.
*Glycophorin A (GpA) transmembrane-domain dimer: Homo sapiens* E Eukaryota (expressed in E. coli), 2.81 Å** Type 1 Lipidic cubic phase crystals showing GpA in bilayer environment	5EH4	Data File Jmol Viewer 5EH4	Trenker et al. (2015). Trenker R, Call ME, & Call MJ (2015). Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase. J Am Chem Soc 137 50:15676-15679. PubMed Id: 26642914. doi:10.1021/jacs.5b11354.
*Influenza Hemagglutinin, full length: Influenza A* V Viruses, 4.2 Å** cryo-EM structure ectodomain, 3.3 Å: 6HJN in complex with FISW84 Fab Fragment, 4.1 Å: 6HJQ FISW84 Fab Fragment by x-ray diffraction, 1.87 Å: 6HKG	6HJR	Data File Jmol Viewer 6HJR 6HJN 6HJQ 6HKG	Benton et al. (2018). Benton DJ, Nans A, Calder LJ, Turner J, Neu U, Lin YP, Ketelaars E, Kallewaard NL, Corti D, Lanzavecchia A, Gamblin SJ, Rosenthal PB, & Skehel JJ (2018). Influenza hemagglutinin membrane anchor. Proc Natl Acad Sci USA 115 40:10112-10117. PubMed Id: 30224494. doi:10.1073/pnas.1810927115.
*Influenza Hemagglutinin, ectodomain of X-31 Haemagglutinin at pH 8: influenza virus* V Viruses (expressed in Gallus gallus), 3.00 Å** cryo-EM structure. Influenza virus unidentified. at pH 5 (State I), 3.00 Å: 6Y5H at pH 5 (State II), 5.50 Å: 6Y5I form 2 at pH 5 (State III), 5.60 Å: 6Y5J extended intermediate at pH5 (State IV), 4.20 Å: 6Y5K Signal Subtracted Extended Intermediate form at pH 5 (State IV), 3.60 Å: 6Y5L	6Y5G	Data File Jmol Viewer 6Y5G 6Y5I 6Y5J 6Y5K 6Y5H 6Y5L	Benton et al. (2020). Benton DJ, Gamblin SJ, Rosenthal PB, & Skehel JJ (2020). Structural transitions in influenza haemagglutinin at membrane fusion pH. Nature 583 7814:150-153. PubMed Id: 32461688. doi:10.1038/s41586-020-2333-6.
High-Density Lipoprotein (HDL) Receptors
*C-terminal transmembrane domain of scavenger receptor BI (SR-BI): Mus musculus* E Eukaryota (expressed in E. coli), NMR structure** The C-terminal domain contains a leucine zipper dimerization motif	5KTF	Data File Jmol Viewer 5KTF	Chadwick et al. (2017). Chadwick AC, Jensen DR, Hanson PJ, Lange PT, Proudfoot SC, Peterson FC, Volkman BF, & Sahoo D (2017). NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif. Structure 25 :446-457. PubMed Id: 28162952. doi:10.1016/j.str.2017.01.001.
Tumor Necrosis Factor (TNF) Receptor Superfamily
*p75 neurotrophin receptor transmembrane domain: Rattus norvegicus* E Eukaryota (expressed in E. coli), NMR structure** Structure determined in DPC micelles. The transmembrane domain includes residues 245-284 from the complete receptor. C257A mutant, 2MJO	2MIC	Data File Jmol Viewer 2MIC 2MJO	Nadezhdin et al. (2016). Nadezhdin KD, García-Carpio I, Goncharuk SA, Mineev KS, Arseniev AS, & Vilar M (2016). Structural Basis of p75 Transmembrane Domain Dimerization. J Biol Chem 291 23:12346-12357. PubMed Id: 27056327. doi:10.1074/jbc.M116.723585.
*Tumor necrosis factor receptor 1 (TNFR1) in lipid bicelles: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure**	7K7A	Data File Jmol Viewer 7K7A	Zhao et al. (2020). Zhao L, Fu Q, Pan L, Piai A, & Chou JJ (2020). The Diversity and Similarity of Transmembrane Trimerization of TNF Receptors. Front Cell Dev Biol 8 . PubMed Id: 33163490. doi:10.3389/fcell.2020.569684.
*Glucocorticoid-induced TNF receptor (GITR): Mus musculus* E Eukaryota (expressed in HEK293 cells), 4.40 Å** cryo-EM structure	7RFP	Data File Jmol Viewer 7RFP	He et al. (2022). He C, Maniyar RR, Avraham Y, Zappasodi R, Rusinova R, Newman W, Heath H, Wolchok JD, Dahan R, Merghoub T, & Meyerson JR (2022). Therapeutic antibody activation of the glucocorticoid-induced TNF receptor by a clustering mechanism. Sci Adv 8 8:eabm4552. PubMed Id: 35213218. doi:10.1126/sciadv.abm4552.
B Cell Receptor Complexes These complexes are involved B cell development and immune responses
*B-Cell receptor in complex with IgG: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.03 Å** cryo-EM structure	7WSO	Data File Jmol Viewer 7WSO	Ma et al. (2022). Ma X, Zhu Y, Dong D, Chen Y, Wang S, Yang D, Ma Z, Zhang A, Zhang F, Guo C, & Huang Z (2022). Cryo-EM structures of two human B cell receptor isotypes. Science 377 6608:880-885. PubMed Id: 35981028. doi:10.1126/science.abo3828.
*B-Cell receptor in complex with IgM: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.63 Å** cryo-EM structure	7XT6	Data File Jmol Viewer 7XT6	Ma et al. (2022). Ma X, Zhu Y, Dong D, Chen Y, Wang S, Yang D, Ma Z, Zhang A, Zhang F, Guo C, & Huang Z (2022). Cryo-EM structures of two human B cell receptor isotypes. Science 377 6608:880-885. PubMed Id: 35981028. doi:10.1126/science.abo3828.
*B-Cell receptor in complex with IgM: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	7XQ8	Data File Jmol Viewer 7XQ8	Su et al. (2022). Su Q, Chen M, Shi Y, Zhang X, Huang G, Huang B, Liu D, Liu Z, & Shi Y (2022). Cryo-EM structure of the human IgM B cell receptor. Science 377 6608:875-880. PubMed Id: 35981043. doi:10.1126/science.abo3923.
Receptor Tyrosine Kinase (RTK) Family Single-span TM proteins important in cellular signalling
*Insulin receptor TM domain (AAs 940-980): Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure**	2MFR	Data File Jmol Viewer 2MFR	Li et al. (2014). Li Q, Wong YL, & Kang C (2014). Solution structure of the transmembrane domain of the insulin receptor in detergent micelles. Biochim Biophys Acta 1838 :1313-1321. PubMed Id: 24440425. doi:10.1016/j.bbamem.2014.01.005.
*insulin receptor bound with A62 DNA aptamer: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.18 Å** cryo-EM structure bound with A62 DNA aptamer and insulin, 4.27 Å: 7YQ5 aptamer and insulin - locally refined, 3.95 Å: 7QY4 bound with A43 DNA aptamer and insulin, 3.60 Å: 7YQ3 bound with two insulin molecules, 4.18 Å: 8GUY	7YQ6	Data File Jmol Viewer 7YQ6 7YQ3 7YQ5 7QY4 8GUY	Kim et al. (2022). Kim J, Yunn NO, Park M, Kim J, Park S, Kim Y, Noh J, Ryu SH, & Cho Y (2022). Functional selectivity of insulin receptor revealed by aptamer-trapped receptor structures. Nat Commun 13 1:6500. PubMed Id: 36310231. doi:10.1038/s41467-022-34292-8.
Epidermal Growth Factor Receptors (EGFRs) ErbB (or HER) family of receptor tyrosine kinases (RTKs)
*ErbB2 transmembrane segment dimer: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure** TM fragment 641-684 of ErbB2 gene. Structure determined in DMPC/DHPC bicelles.	2JWA	Data File Jmol Viewer 2JWA	Bocharov et al. (2008). Bocharov EV, Mineev KS, Volynsky PE, Ermolyuk YS, Tkach EN, Sobol AG, Chupin VV, Kirpichnikov MP, Efremov RG, & Arseniev AS (2008). Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state. J Biol Chem 283 :6950-6956. PubMed Id: 18178548. doi:10.1074/jbcM709202200.
*ErbB2 (HER2) transmembrane segment dimer with juxtamembrane region: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure** in DPC micelles	2N2A	Data File Jmol Viewer 2N2A	Bragin et al. (2016). Bragin PE, Mineev KS, Bocharova OV, Volynsky PE, Bocharov EV, & Arseniev AS (2016). HER2 Transmembrane Domain Dimerization Coupled with Self-Association of Membrane-Embedded Cytoplasmic Juxtamembrane Regions. J Mol Biol 428 :52-61. PubMed Id: 26585403. doi:10.1016/j.jmb.2015.11.007.
*ErbB1/ErbB2 transmembrane segment heterodimer: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure** TM fragment 634-677 of ErbB1 gene. TM fragment 641-685 of ErbB2 gene. Structure determined in DMPC/DHPC bicelles.	2KS1	Data File Jmol Viewer 2KS1	Mineev et al. (2010). Mineev KS, Bocharov EV, Pustovalova YE, Bocharova OV, Chupin VV, & Arseniev AS (2010). Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 receptor tyrosine kinases. J Mol Biol 400 :231-243. PubMed Id: 20471394. doi:10.1016/j.jmb.2010.05.016.
*ErbB1 transmembrane segment homodimer: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure**	5LV6	Data File Jmol Viewer 5LV6	Bocharov et al. (2017). Bocharov EV, Bragin PE, Pavlov KV, Bocharova OV, Mineev KS, Polyansky AA, Volynsky PE, Efremov RG, & Arseniev AS (2017). The Conformation of the Epidermal Growth Factor Receptor Transmembrane Domain Dimer Dynamically Adapts to the Local Membrane Environment. Biochemistry 56 12:1697-1705. PubMed Id: 28291355. doi:10.1021/acs.biochem.6b01085.
*ErbB3 transmembrane segment dimer: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure** TM fragment 639-667 of ErbB3 gene. Structure determined in DPC micelles.	2L9U	Data File Jmol Viewer 2L9U	Mineev et al. (2011). Mineev KS, Khabibullina NF, Lyukmanova EN, Dolgikh DA, Kirpichnikov MP, & Arseniev AS (2011). Spatial structure and dimer--monomer equilibrium of the ErbB3 transmembrane domain in DPC micelles. Biochim Biophys Acta 1808 :2081-2088. PubMed Id: 21575594. doi:10.1016/j.bbamem.2011.04.017.
*ErbB4 transmembrane segment dimer: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure** TM fragment 651-678 of ErbB4 gene. Structure determined in DMPC/DHPC bicelles.	2LCX	Data File Jmol Viewer 2LCX	Bocharov et al. (2012). Bocharov EV, Mineev KS, Goncharuk MV, & Arseniev AS (2012). Structural and thermodynamic insight into the process of "weak" dimerization of the ErbB4 transmembrane domain by solution NMR. Biochim Biophys Acta 1818 :2158-2170. PubMed Id: 22579757. doi:10.1016/j.bbamem.2012.05.001.
Erythropoietin-Producing Hepatocellular Receptors Eph family of receptor tyrosine kinases (RTKs)
*EphA1 transmembrane segment dimer, pH 6.3: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure** TM fragment 536-573 of EphA1 gene. Structure determined in DMPC/DHPC bicelles. Structure at pH 4.3: 2K1K	2K1L	Data File Jmol Viewer 2K1L 2K1K	Bocharov et al. (2008). Bocharov EV, Mayzel ML, Volynsky PE, Goncharuk MV, Ermolyuk YS, Schulga AA, Artemenko EO, Efremov RG, & Arseniev AS (2008). Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1. J Biol Chem 283 :29385-29395. PubMed Id: 18728013. doi:10.1074/jbc.M803089200.
*EphA2 transmembrane segment dimer: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure** TM fragment 523-563 of EphA2 gene. Structure determined in DMPC/DHPC bicelles.	2K9Y	Data File Jmol Viewer 2K9Y	Bocharov et al. (2010). Bocharov EV, Mayzel ML, Volynsky PE, Mineev KS, Tkach EN, Ermolyuk YS, Schulga AA, Efremov RG, & Arseniev AS (2010). Left-handed dimer of EphA2 transmembrane domain: Helix packing diversity among receptor tyrosine kinases. Biophys J 98 :881-889. PubMed Id: 20197042. doi:10.1016/j.bpj.2009.11.008.
Fibroblast Growth Factor Receptors FGFR family of receptor tyrosine kinases (RTKs)
*FGFR3 Fibroblast growth factor receptor 3 transmembrane dimer: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure**	2LZL	Data File Jmol Viewer 2LZL	Bocharov et al. (2013). Bocharov EV, Lesovoy DM, Goncharuk SA, Goncharuk MV, Hristova K, & Arseniev AS (2013). Structure of FGFR3 Transmembrane Domain Dimer: Implications for Signaling and Human Pathologies. Structure 21 :2087-2093. PubMed Id: 24120763. doi:10.1016/j.str.2013.08.026.
Vascular Endothelial Growth Factor Receptors VEGFR family of receptor tyrosine kinases (RTKs)
*VEGFR2 vascular endothelial growth factor receptor 2 transmembrane dimer: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure** TM fragment residues 759-795. Structure determined in DPC micelles. V769E trimeric mutant: 2MET G770E/F777E dimeric mutant: 2MEU	2M59	Data File Jmol Viewer 2M59 2MET 2MEU	Manni et al. (2014). Manni S, Mineev KS, Usmanova D, Lyukmanova EN, Shulepko MA, Kirpichnikov MP, Winter J, Matkovic M, Deupi X, Arseniev AS, & Ballmer-Hofer K (2014). Structural and functional characterization of alternative transmembrane domain conformations in VEGF receptor 2 activation. Structure 22 8:1077-1089. PubMed Id: 24980797. doi:10.1016/j.str.2014.05.010.
Integrin Adhesion Receptors
*Human Integrin αIIbβ3 transmembrane-cytoplasmic heterodimer: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure**	2KNC	Data File Jmol Viewer 2KNC	Yang et al. (2009). Yang J, Ma YQ, Page RC, Misra S, Plow EF, & Qin J (2009). Structure of an integrin αIIbβ3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation. Proc Natl Acad Sci U S A 106 :17729-17734. PubMed Id: 19805198.
*integrin αIIb(W968V)β3 transmembrane complex: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure**	7KN0	Data File Jmol Viewer 7KN0	Situ et al. (2021). Situ AJ, Kim J, An W, Kim C, & Ulmer TS (2021). Insight Into Pathological Integrin αIIbβ3 Activation From Safeguarding The Inactive State. J Mol Biol 433 7:166832. PubMed Id: 33539882. doi:10.1016/j.jmb.2021.166832.
*full-length integrin αIIbβ3 in native lipid: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure with bound Eptifibatide, 3.10 Å: 8T2U	8T2V	Data File Jmol Viewer 8T2V 8T2U	Adair et al. (2023). Adair BD, Xiong JP, Yeager M, & Arnaout MA (2023). Cryo-EM structures of full-length integrin αIIbβ3 in native lipids. Nat Commun 14 1:4168. PubMed Id: 37443315. doi:10.1038/s41467-023-39763-0.
*Human Integrin αvβ6, in complex with minibinder B6_BP_dslf: Homo sapiens* E Eukaryota (expressed in E. coli), 3.40 Å** cryo-EM structure	8TCG	Data File Jmol Viewer 8TCG	Roy et al. (2023). Roy A, Shi L, Chang A, Dong X, Fernandez A, Kraft JC, Li J, Le VQ, Winegar RV, Cherf GM, Slocum D, Poulson PD, Casper GE, Vallecillo-Zúniga ML, Valdoz JC, Miranda MC, Bai H, Kipnis Y, Olshefsky A, Priya T, Carter L, Ravichandran R, Chow CM, Johnson MR, Cheng S, Smith M, Overed-Sayer C, Finch DK, Lowe D, Bera AK, Matute-Bello G, Birkland TP, DiMaio F, Raghu G, Cochran JR, Stewart LJ, Campbell MG, Van Ry PM, Springer T, & Baker D (2023). De novo design of highly selective miniprotein inhibitors of integrins αvβ6 and αvβ8. Nat Commun 14 1:5660. PubMed Id: 37704610. doi:10.1038/s41467-023-41272-z.
*Human Integrin αvβ8, in complex with minibinder B8_BP_dsulf: Homo sapiens* E Eukaryota (expressed in E. coli), 2.90 Å** cryo-EM structure	8TCF	Data File Jmol Viewer 8TCF	Roy et al. (2023). Roy A, Shi L, Chang A, Dong X, Fernandez A, Kraft JC, Li J, Le VQ, Winegar RV, Cherf GM, Slocum D, Poulson PD, Casper GE, Vallecillo-Zúniga ML, Valdoz JC, Miranda MC, Bai H, Kipnis Y, Olshefsky A, Priya T, Carter L, Ravichandran R, Chow CM, Johnson MR, Cheng S, Smith M, Overed-Sayer C, Finch DK, Lowe D, Bera AK, Matute-Bello G, Birkland TP, DiMaio F, Raghu G, Cochran JR, Stewart LJ, Campbell MG, Van Ry PM, Springer T, & Baker D (2023). De novo design of highly selective miniprotein inhibitors of integrins αvβ6 and αvβ8. Nat Commun 14 1:5660. PubMed Id: 37704610. doi:10.1038/s41467-023-41272-z.
Adiponectin Receptors 7TM receptors with inverted topology relative to GPCR receptors Adiponectin is a protein hormone that is important in glucose & fatty acid metabolism
*AdipoR1 adiponectin 1 receptor in complex with an Fv fragment: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.90 Å** This protein and AdipoR2 enclose a large cavity where 3 His residues coördinate a Zn ion. AdipoR2 adiponectin 2 receptor in complex with Fv fragment, 2.40 Å: 3WXW	3WXV	Data File Jmol Viewer 3WXV 3WXW	Tanabe et al. (2015). Tanabe H, Fujii Y, Okada-Iwabu M, Iwabu M, Nakamura Y, Hosaka T, Motoyama K, Ikeda M, Wakiyama M, Terada T, Ohsawa N, Hato M, Ogasawara S, Hino T, Murata T, Iwata S, Hirata K, Kawano Y, Yamamoto M, Kimura-Someya T, Shirouzu M, Yamauchi T, Kadowaki T, & Yokoyama S (2015). Crystal structures of the human adiponectin receptors. Nature 520 7547:312-316. PubMed Id: 25855295. doi:10.1038/nature14301.
*AdipoR1 adiponectin 1 receptor in complex with an Fv fragment: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.73 Å** 5LXG supersedes 3WXV. AdipoR2 adiponectin 2 receptor in complex with Fv fragment, 2.4 Å: 5LWY 5LWY supersedes 3WXW AdipoR2 in complex with a C18 free fatty acid, 2.4 Å: 5LX9 AdipoR2 in complex with a C18 free fatty acid, 3.0 Å: 5LXA	5LXG	Data File Jmol Viewer 5LXG 5LXA 5LWY 5LX9	Vasiliauskaité-Brooks et al. (2017). Vasiliauskaité-Brooks I, Sounier R, Rochaix P, Bellot G, Fortier M, Hoh F, De Colibus L, Bechara C, Saied EM, Arenz C, Leyrat C, & Granier S (2017). Structural insights into adiponectin receptors suggest ceramidase activity. Nature 544 :120-123. PubMed Id: 28329765. doi:10.1038/nature21714.
*AdipoR1 adiponectin 1 receptor, D208A mutant: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.05 Å** Three molecules in the asymmetric unit. Two in closed form, one in open form. AdipoR1 (D208), 2.78 Å: 6KS0 AdipoR2 (D219), 2.4 Å: 6KS1 6KS0 replaces 3WVV. 6KS1 replaces 3WXW.	6KRZ	Data File Jmol Viewer 6KRZ 6KS0 6KS1	Tanabe et al. (2020). Tanabe H, Fujii Y, Okada-Iwabu M, Iwabu M, Kano K, Kawana H, Hato M, Nakamura Y, Terada T, Kimura-Someya T, Shirouzu M, Kawano Y, Yamamoto M, Aoki J, Yamauchi T, Kadowaki T, & Yokoyama S (2020). Human adiponectin receptor AdipoR1 assumes closed and open structures. Commun Biol 3 1. PubMed Id: 32796916. doi:10.1038/s42003-020-01160-4.
*AdipoR2 Adiponectin receptor, cryogenic Serial Crystallography (SSX) using CrystalDirect: Homo sapiens* E Eukaryota (expressed in Drosophila melanogaster), 2.40 Å** Room temperature structure using CrystalDirect, 2.90 Å 6YXD Cryogenic with Tb-XO4 ligand using CrystalDirect, 3.01 Å 6YXG Cryogenic with Gd-DO3 ligand using CrystalDirect, 3.02 Å 6YXF	6YX9	Data File Jmol Viewer 6YX9 6YXG 6YXD 6YXF	Healey et al. (2021). Healey RD, Basu S, Humm AS, Leyrat C, Cong X, Golebiowski J, Dupeux F, Pica A, Granier S, & Márquez JA (2021). An automated platform for structural analysis of membrane proteins through serial crystallography. Cell Rep Methods 1 6:100102. PubMed Id: 34723237. doi:10.1016/j.crmeth.2021.100102.
Cytokine Receptors
*Cytokine receptor IL-17RC ECD in complex with human IL-17F: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.32 Å** These receptors are anchored to the membrane by a single TM segment, not shown in the structure IL-17RC ECD in complex with human IL-17F, Crystal form II, 3.62 Å: 6HG9 IL-17RC D2-D3-D4 domains in complex with an anti-APP tag Fab, 2.60 Å: 6HGA human IL-17F, 2.10 Å: 6HGO anti-APP-tag Fab, 1.50 Å: 6HGU	6HG4	Data File Jmol Viewer 6HG4 6HGA 6HGO 6HG9 6HGU	Goepfert et al. (2020). Goepfert A, Lehmann S, Blank J, Kolbinger F, & Rondeau JM (2020). Structural Analysis Reveals that the Cytokine IL-17F Forms a Homodimeric Complex with Receptor IL-17RC to Drive IL-17RA-Independent Signaling. Immunity 52 3:499-512.e5. PubMed Id: 32187518. doi:10.1016/j.immuni.2020.02.004.
*Dimeric/trimeric IL-25-IL/17 complexes: IL-17RB-IL-25 (2:2): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure IL-17RB-IL-25 (6:6), 4.40 Å: 7UWK IL-25-IL-17RB-IL-17RA ternary complex, 3.70 Å: 7UWL IL-17A-IL-17RA binary complex, 2.50 Å: 7UWM IL-17A-IL-17RA-IL-17RC ternary complex, 3.01 Å: 7UWN	7UWJ	Data File Jmol Viewer 7UWJ 7UWL 7UWM 7UWN 7UWK	Wilson et al. (2022). Wilson SC, Caveney NA, Yen M, Pollmann C, Xiang X, Jude KM, Hafer M, Tsutsumi N, Piehler J, & Garcia KC (2022). Organizing structural principles of the IL-17 ligand-receptor axis. Nature 609 7927:622-629. PubMed Id: 35863378. doi:10.1038/s41586-022-05116-y.
*leptin receptor (LepR)-full ECD (D1-D7) in complex with leptin: Mus musculus* E Eukaryota (expressed in HEK293 cells), 5.90 Å** cryo-EM structure LepR-partial ECD (D3-D7) in complex with leptin , 4.50 Å: 8DH9 LepR-leptin interaction focused refinement, 3.80 Å: 8DHA	8DH8	Data File Jmol Viewer 8DH8 8DH9 8DHA	Saxton et al. (2023). Saxton RA, Caveney NA, Moya-Garzon MD, Householder KD, Rodriguez GE, Burdsall KA, Long JZ, & Garcia KC (2023). Structural insights into the mechanism of leptin receptor activation. Nat Commun 14 1:1797. PubMed Id: 37002197. doi:10.1038/s41467-023-37169-6.
Toll-Like Receptors (TLR) and TLR Signalling Regulators
*Toll-like receptor TLR3 in complex with UNC93B1: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure TLR7 in complex with UNC93B1, 4.20 Å 7CYN	7C76	Data File Jmol Viewer 7C76 7CYN	Ishida et al. (2021). Ishida H, Asami J, Zhang Z, Nishizawa T, Shigematsu H, Ohto U, & Shimizu T (2021). Cryo-EM structures of Toll-like receptors in complex with UNC93B1. Nat Struct Mol Biol 28 2:173-180. PubMed Id: 33432245. doi:10.1038/s41594-020-00542-w.
*Toll-like receptor TLR3 in complex with UNC93B1: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	7C77	Data File Jmol Viewer 7C77	Ishida et al. (2021). Ishida H, Asami J, Zhang Z, Nishizawa T, Shigematsu H, Ohto U, & Shimizu T (2021). Cryo-EM structures of Toll-like receptors in complex with UNC93B1. Nat Struct Mol Biol 28 2:173-180. PubMed Id: 33432245. doi:10.1038/s41594-020-00542-w.
Novel Receptors
*Sigma-1 (σ₁) receptor, with bound PD144418: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.51 Å** with bound 4-IBP, 3.2 Å: 5HK2	5HK1	Data File Jmol Viewer 5HK1 5HK2	Schmidt et al. (2016). Schmidt HR, Zheng S, Gurpinar E, Koehl A, Manglik A, & Kruse AC (2016). Crystal structure of the human σ₁ receptor. Nature 532 :527-530. PubMed Id: 27042935. doi:10.1038/nature17391.
*Sigma-1 (σ₁) receptor, closed conformation: Xenopus laevis* E Eukaryota (expressed in Komagataella pastoris), 3.20 Å** complexed with PRE084, 3.33 Å 7W2C complexed with S1RA, 3.47 Å 7W2D open-like conformation, 3.56 Å 7W2E open-like conformation complexed with PRE084 by co-crystallization, 3.10 Å 7W2F open-like conformation complexed with PRE084 by soaking, 2.85 Å 7W2G double cysteine variant complexed with S1RA, 3.80 Å 7W2H	7W2B	Data File Jmol Viewer 7W2B 7W2H 7W2E 7W2C 7W2D 7W2G 7W2F	Meng et al. (2022). Meng F, Xiao Y, Ji Y, Sun Z, & Zhou X (2022). An open-like conformation of the sigma-1 receptor reveals its ligand entry pathway. Nat Commun 13 1:1267. PubMed Id: 35273182. doi:10.1038/s41467-022-28946-w.
*sigma 2 (σ₂) receptor bound to PB28: Bos taurus* E Eukaryota (expressed in Spodoptera frugiperda), 2.94 Å** bound to Roluperidone, 2.71 Å 7M94 bound to Z1241145220, 2.41 Å 7M95 bound to Z4857158944, 2.41 Å 7M96 bound to cholesterol, 2.81 Å 7MFI	7M93	Data File Jmol Viewer 7M93 7M95 7M94 7MFI 7M96	Alon et al. (2021). Alon A, Lyu J, Braz JM, Tummino TA, Craik V, O'Meara MJ, Webb CM, Radchenko DS, Moroz YS, Huang XP, Liu Y, Roth BL, Irwin JJ, Basbaum AI, Shoichet BK, & Kruse AC (2021). Structures of the σ₂ receptor enable docking for bioactive ligand discovery. Nature 600 7890:759-764. PubMed Id: 34880501. doi:10.1038/s41586-021-04175-x.
*STRA6 retinol-uptake receptor in complex with calmodulin (CaM): Danio rerio* E Eukaryota (expressed in sf9 cells), 3.9 Å** cryo-EM structure	5SY1	Data File Jmol Viewer 5SY1	Chen et al. (2016). Chen Y, Clarke OB, Kim J, Stowe S, Kim YK, Assur Z, Cavalier M, Godoy-Ruiz R, von Alpen DC, Manzini C, Blaner WS, Frank J, Quadro L, Weber DJ, Shapiro L, Hendrickson WA, & Mancia F (2016). Structure of the STRA6 receptor for retinol uptake. Science 353 . PubMed Id: 27563101. doi:10.1126/science.aad8266.
Bacterial, Algal, Viral, and Unusual Rhodopsins
*Bacteriorhodopsin (BR): Halobacterium salinarum* A Archaea, 3.5 Å** Electron Diffraction. The first atomic-resolution structure of bacteriorhodopsin	2BRD	Data File Jmol Viewer 2BRD bacteriorhodopsin	Grigorieff et al. (1996). Grigorieff N, Ceska TA, Downing KH, Baldwin JM, & Henderson R (1996). Electron-crystallographic refinement of the structure of bacteriorhodopsin. J Mol Biol 259 :393-421. PubMed Id: 8676377.
*Bacteriorhodopsin (BR): Halobacterium salinarum* A Archaea, 3.0 Å** Electron Diffraction	1AT9	Data File Jmol Viewer 1AT9 bacteriorhodopsin	Kimura et al. (1997). Kimura Y, Vassylyev DG, Miyazawa A, Kidera A, Matsushima M, Mitsuok a K, Murata K, Hirai T, & Fujiyoshi Y (1997). Surface of bacteriorhodopsin revealed by high-resolution electron crystallography. Nature 389 :206-211. PubMed Id: 8676377.
*Bacteriorhodopsin (BR): Halobacterium salinarum* A Archaea, 2.35 Å** The first x-ray structure of bacteriorhodopsin	1AP9	Data File Jmol Viewer 1AP9 bacteriorhodopsin	Pebay-Peyroula et al. (1997). Pebay-Peyroula E, Rummel G, Rosenbusch JP, & Landau EM (1997). X-ray structure of bacteriorhodopsin at 2.5 Å from microcrystals grown in lipidic cubic phases. Science 277 :1676-1681. PubMed Id: 9287223.
*Bacteriorhodopsin (BR): Halobacterium salinarum* A Archaea, 2.90 Å**	1BRR	Data File Jmol Viewer 1BRR	Essen et al. (1998). Essen L, Siegert R, Lehmann WD, & Oesterhelt D (1998). Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex. Proc Natl Acad Sci U S A 95 :11673-11678. PubMed Id: 9751724.
*Bacteriorhodopsin (BR): Halobacterium salinarum* A Archaea, 2.30 Å**	1BRX	Data File Jmol Viewer 1BRX bacteriorhodopsin	Luecke et al. (1998). Luecke H, Richter HT, & Lanyi JK (1998). Proton transfer pathways in bacteriorhodopsin at 2.3 Angstrom resolution. Science 280 :1934-1937. PubMed Id: 9632391.
*Bacteriorhodopsin (BR) dark-adapted: Halobacterium salinarum* A Archaea, NMR structure**	1R84	Data File Jmol Viewer 1R84	Patzelt et al. (2002). Patzelt H, Simon B, terLaak A, Kessler B, Kühne R, Schmieder P, Oesterhelt D, & Oschkinat H (2002). The structures of the active center in dark-adapted bacteriorhodopsin by solution-state NMR spectroscopy. Proc Natl Acad Sci USA 99 :9765-9770. PubMed Id: 12119389.
*Bacteriorhodopsin (BR), K intermediate: Halobacterium salinarum* A Archaea, 2.10 Å** R-free = O.255. R-free = 0.303, 2.1 Å: 1QKO	1QKP	Data File Jmol Viewer 1QKP 1QKO	Edman et al. (1999). Edman K, Nollert P, Royant A, Belrhali H, Pebay-Peyroula E, Hajdu J, Neutze R, & Landau EM (1999). High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle. Nature 401 :822-826. PubMed Id: 10548112.
*Bacteriorhodopsin (BR), K intermediate (illuminated): Halobacterium salinarum* A Archaea, 1.43 Å** Non-illuminated, 1.47 Å: 1M0L	1M0K	Data File Jmol Viewer 1M0K 1M0L	Schobert et al. (2002). Schobert B, Cupp-Vickery J, Hornak V, Smith S, & Lanyi J (2002). Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal. J. Mol. Biol. 321 :715-726. PubMed Id: 12206785.
*Bacteriorhodopsin in an early-M intermediate state: Halobacterium salinarum* A Archaea, 2.00 Å** In "mock-trapped" early-M intermediate state, 1.81 Å: 1KG9 In ground state, 1.65 Å: 1KGB	1KG8	Data File Jmol Viewer 1KG8 1KG9 1KGB	Facciotti et al. (2001). Facciotti MT, Rouhani S, Burkard FT, Betancourt FM, Downing KH, Rose RB, McDermott G, & Glaeser RM (2001). Structure of an early intermediate in the M-state phase of the bacteriorhodopsin photocycle Biophys J 81 :3442-3455. PubMed Id: 11721006. doi:10.1016/S0006-3495(01)75976-0.
*Bacteriorhodopsin (BR): Halobacterium salinarum* A Archaea, 1.90 Å**	1QHJ	Data File Jmol Viewer 1QHJ	Belrhali et al. (1999). Belrhali H, Nollert P, Royant A, Menzel C, Rosenbusch JP, Landau EH, & Pebay-Peyroula E (1999). Protein, lipid, and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 Å resolution. Structure 7 :909-917. PubMed Id: 10467143.
*Bacteriorhodopsin (BR): Halobacterium salinarum* A Archaea, 1.55 Å**	1C3W	Data File Jmol Viewer 1C3W	Luecke et al. (1999). Luecke H, Schobert B, Richter HT, Cartailler P, & Lanyi JK (1999). Structure of bacteriorhodopsin at 1.55 angstrom resolution. J. Mol. Biol 291 :899-911. PubMed Id: 10452895.
*Bacteriorhodopsin (BR), D96N in bR state: Halobacterium salinarum* A Archaea, 1.80 Å** D96N in M-state, 2.00 Å: 1C8S.	1C8R	Data File Jmol Viewer 1C8R 1C8S	Luecke et al. (1999). Luecke H, Schobert B, Richter HT, Cartailler P, & Lanyi JK (1999). Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution. Science 286 :255-260. PubMed Id: 10514362.
*Bacteriorhodopsin in ground state: Halobacterium salinarum* A Archaea, 1.78 Å** Ground state, after x-ray modification, 1.78 Å: 3NSB	3NS0	Data File Jmol Viewer 3NS0 3NSB	Borshchevskiy et al. (2011). Borshchevskiy VI, Round ES, Popov AN, Büldt G, & Gordeliy VI (2011). X-ray-Radiation-Induced Changes in Bacteriorhodopsin Structure J Mol Biol 409 :813-825. PubMed Id: 21530535. doi:10.1016/j.jmb.2011.04.038.
*Bacteriorhodopsin phototaxis signalling mutant (A215T): Halobacterium sp. nrc-1* A Archaea (expressed in Halobacterium salinarum), 3.01 Å** This mutant enables BR's photochemical reactions to transmit signals to the transducer HtrII.	3T45	Data File Jmol Viewer 3T45	Spudich et al. (2012). Spudich EN, Ozorowski G, Schow EV, Tobias DJ, Spudich JL, & Luecke H (2012). A transporter converted into a sensor, a phototaxis signaling mutant of bacteriorhodopsin at 3.0 Å. J Mol Biol 415 :455-463. PubMed Id: 22123198. doi:10.1016/j.jmb.2011.11.025.
*Bacteriorhodopsin (BR); D96/F171C/F219L mutant: Halobacterium salinarum* A Archaea, 2.65 Å**	4FPD	Data File Jmol Viewer 4FPD	Wang et al. (2013). Wang T, Sessions AO, Lunde CS, Rouhani S, Glaeser RM, Duan Y, & Facciotti MT (2013). Deprotonation of D96 in bacteriorhodopsin opens the proton uptake pathway. Structure 21 :290-297. PubMed Id: 23394942. doi:10.1016/j.str.2012.12.018.
*Bacteriorhodopsin (BR) determined using serial ms crystallography (SMX): Halobacterium salinarum* A Archaea, 2.40 Å** Structure by conventional crystallography, 1.90 Å:4X32	4X31	Data File Jmol Viewer 4X31 4X32	Nogly et al. (2015). Nogly P, James D, Wang D, White TA, Zatsepin N, Shilova A, Nelson G, Liu H, Johansson L, Heymann M, Jaeger K, Metz M, Wickstrand C, Wu W, Båth P, Berntsen P, Oberthuer D, Panneels V, Cherezov V, Chapman H, Schertler G, Neutze R, Spence J, Moraes I, Burghammer M, Standfuss J, & Weierstall U (2015). Lipidic cubic phase serial millisecond crystallography using synchrotron radiation. IUCrJ 2 :168-176. PubMed Id: 25866654. doi:10.1107/S2052252514026487.
*Bacteriorhodopsin (BR) native: Halobacterium salinarum* A Archaea, 2.35 Å** Structure determind by XFEL. Crystallized from bicelles. Crystallized from Bicelles in Complex with Iodine-labeled Detergent HAD13a, 2.1 Å: 5B34	5B35	Data File Jmol Viewer 5B35 5B34	Nakane et al. (2016). Nakane T, Hanashima S, Suzuki M, Saiki H, Hayashi T, Kakinouchi K, Sugiyama S, Kawatake S, Matsuoka S, Matsumori N, Nango E, Kobayashi J, Shimamura T, Kimura K, Mori C, Kunishima N, Sugahara M, Takakyu Y, Inoue S, Masuda T, Hosaka T, Tono K, Joti Y, Kameshima T, Hatsui T, Yabashi M, Inoue T, Nureki O, Iwata S, Murata M, & Mizohata E (2016). Membrane protein structure determination by SAD, SIR, or SIRAS phasing in serial femtosecond crystallography using an iododetergent. Proc Natl Acad Sc. USA 113 :13039-13044. PubMed Id: 27799539.
*Bacteriorhodopsin (BR) 3D movie, ground state: Halobacterium salinarum* A Archaea, 2.0 Å** See the movie: Science Magazine structures at: 16 nsec, 2.1 Å: 5B6W 40 nsec, 2.1 Å: 5H2H 110 nsec, 2.1 Å: 5H2I 290 nsec, 2.1 Å: 5H2J 760 nsec, 2.1 Å: 5B6X 2 μsec, 2.1 Å: 5H2K 5.25 μsec, 2.1 Å: 5H2L 13.8 μsec, 2.1 Å: 5H2M 36.2 μsec, 2.1 Å: 5B6Y 95.2 μsec, 2.1 Å: 5H2N 250 μsec, 2.1 Å: 5H2O 657 μsec, 2.1 Å: 5H2P 1.725 msec, 2.1 Å: 5B6Z	5B6V	Data File Jmol Viewer 5B6V 5B6W 5H2P 5H2M 5B6X 5B6Z 5H2L 5B6Y 5H2K 5H2H 5H2O 5H2N 5H2I 5H2J	Nango et al. (2016). Nango E, Royant A, Kubo M, Nakane T, Wickstrand C, Kimura T, Tanaka T, Tono K, Song C, Tanaka R, Arima T, Yamashita A, Kobayashi J, Hosaka T, Mizohata E, Nogly P, Sugahara M, Nam D, Nomura T, Shimamura T, Im D, Fujiwara T, Yamanaka Y, Jeon B, Nishizawa T, Oda K, Fukuda M, Andersson R, Båth P, Dods R, Davidsson J, Matsuoka S, Kawatake S, Murata M, Nureki O, Owada S, Kameshima T, Hatsui T, Joti Y, Schertler G, Yabashi M, Bondar AN, Standfuss J, Neutze R, & Iwata S (2016). A three-dimensional movie of structural changes in bacteriorhodopsin. Science 354 :1552-1557. PubMed Id: 28008064. doi:10.1126/science.aah3497.
*Bacteriorhodopsin (BR) retinal isomerization movie, ground state: Halobacterium salinarum* A Archaea, 1.5 Å** see the movie: Science Magazine Δt 49 - 406 fs, 1.9 Å: 6G7I Δt 457-646 fs, 1.9 Å: 6G7J Δt 10 ps, 1.9 Å: 1.9 Å: 6G7K Δt 8.3 ms, 1.9 Å: 6G7L	6G7H	Data File Jmol Viewer 6G7H 6G7J 6G7K 6G7I 6G7L	Nogly et al. (2018). Nogly P, Weinert T, James D, Carbajo S, Ozerov D, Furrer A, Gashi D, Borin V, Skopintsev P, Jaeger K, Nass K, Båth P, Bosman R, Koglin J, Seaberg M, Lane T, Kekilli D, Brünle S, Tanaka T, Wu W, Milne C, White T, Barty A, Weierstall U, Panneels V, Nango E, Iwata S, Hunter M, Schapiro I, Schertler G, Neutze R, & Standfuss J (2018). Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser. Science . PubMed Id: 29903883. doi:10.1126/science.aat0094.
*Bacteriorhodopsin (BR). Ground state. Data set 1.: Halobacterium salinarum* A Archaea, 1.29 Å** Data set 2. 1.25 Å: 5ZIM Data set 3. 1.27 Å: 5ZIN	5ZIL	Data File Jmol Viewer 5ZIL 5ZIN 5ZIM	Hasegawa et al. (2018). Hasegawa N, Jonotsuka H, Miki K, & Takeda K (2018). X-ray structure analysis of bacteriorhodopsin at 1.3 Å resolution. Sci Rep 8 1. PubMed Id: 30177765. doi:10.1038/s41598-018-31370-0.
*Bacteriorhodopsin (BR) using serial synchrotron crystallogarphy, steady-state SMX activated state: Halobacterium salinarum* A Archaea, 2 Å** TR-SMX closed state (0 to 5 msec), 2.6 Å: 6RNJ TR-SMX open state (10 to 15 msec), 2.6 Å: 6RPH	6RQO	Data File Jmol Viewer 6RQO 6RPH 6RNJ	Weinert et al. (2019). Weinert T, Skopintsev P, James D, Dworkowski F, Panepucci E, Kekilli D, Furrer A, Brünle S, Mous S, Ozerov D, Nogly P, Wang M, & Standfuss J (2019). Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography. Science 365 6448:61-65. PubMed Id: 31273117. doi:10.1126/science.aaw8634.
*Bacteriorhodopsin (BR) 3D view of ultrafast dynamics, dark state cell 1: Halobacterium salinarum* A Archaea, 1.7 Å** dark state cell 2, 1.8 Å: 6GA2 dark state, cell 2, refined using the same protocol as sub-ps time delays, 1.8 Å: 6RMK 33 msec state, ensemble refinement, 2.1 Å: 6GA3 1 ps state, 1.8 Å: 6GA4 3 ps state, 1.9 Å: 6GA5 10 ps state, 1.8 Å: 6GA6 0.24 ps state, 1.8 Å: 6GA7 0.33 ps state, 1.8 Å:6GA8 0.39 ps state, 1.8 Å: 6GA9 0.43 ps state, 1.8 Å: 6GAA 0.46 ps state, 1.8 Å: 6GAB 0.49 ps state, 1.8 Å: 6GAC 0.53 ps state, 1.8 Å: 6GAD 0.56 ps state, 1.8 Å: 6GAE 0.59 ps state, 1.8 Å: 6GAF 0.63 ps state, 1.8 Å: 6GAG 0.68 ps state, 1.8 Å: 6GAH 0.74 ps state, 1.8 Å: 6AGI	6GA1	Data File Jmol Viewer 6GA1 6GA6 6GAC 6GAA 6GAF 6GA9 6GAE 6RMK 6GAH 6GA5 6GA2 6GA4 6GAD 6AGI 6GAB 6GA7 6GA8 6GA3 6GAG	Nass Kovacs et al. (2019). Nass Kovacs G, Colletier JP, Grünbein ML, Yang Y, Stensitzki T, Batyuk A, Carbajo S, Doak RB, Ehrenberg D, Foucar L, Gasper R, Gorel A, Hilpert M, Kloos M, Koglin JE, Reinstein J, Roome CM, Schlesinger R, Seaberg M, Shoeman RL, Stricker M, Boutet S, Haacke S, Heberle J, Heyne K, Domratcheva T, Barends TRM, & Schlichting I (2019). Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin. Nat Commun 10 1:3177. PubMed Id: 31320619. doi:10.1038/s41467-019-10758-0.
*Bacteriorhodopsin Crystallized from Bicelles in Complex with HAD16, Determined Using 7-keV X-ray Free Electron Laser (XFEL) at SACLA: Halobacterium salinarum* B Bacteria, 2.35 Å**	7VSO	Data File Jmol Viewer 7VSO	Hanashima et al. (2021). Hanashima S, Nakane T, & Mizohata E (2021). Heavy Atom Detergent/Lipid Combined X-ray Crystallography for Elucidating the Structure-Function Relationships of Membrane Proteins. Membranes (Basel) 11 11:823. PubMed Id: 34832053. doi:10.3390/membranes11110823.
*Bacteriorhodopsin (BR). ground state.: Halobacterium salinarum* A Archaea, 1.05 Å** ground state, 1.22 Å 7Z0A K state, 1.53 Å 7Z0C L state, 1.20 Å 7Z0D M state, 1.22 Å 7Z0E	7Z09	Data File Jmol Viewer 7Z09 7Z0A 7Z0C 7Z0D 7Z0E	Borshchevskiy et al. (2022). Borshchevskiy V, Kovalev K, Round E, Efremov R, Astashkin R, Bourenkov G, Bratanov D, Balandin T, Chizhov I, Baeken C, Gushchin I, Kuzmin A, Alekseev A, Rogachev A, Willbold D, Engelhard M, Bamberg E, Büldt G, & Gordeliy V (2022). True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins. Nat Struct Mol Biol 29 5:440-450. PubMed Id: 35484235. doi:10.1038/s41594-022-00762-2.
*Bacteriorhodopsin (BR), ground and K states after green laser irradiation: Halobacterium salinarum* A Archaea, 1.33 Å** ground state by red laser irradiation, 1.33 Å: 7XJD K state refined against the extrapolated dataset, 1.33 Å:7XJE	7XJC	Data File Jmol Viewer 7XJC 7XJE 7XJD	Taguchi et al. (2023). Taguchi S, Niwa S, Dao HA, Tanaka Y, Takeda R, Fukai S, Hasegawa K, & Takeda K (2023). Detailed analysis of distorted retinal and its interaction with surrounding residues in the K intermediate of bacteriorhodopsin. Commun Biol 6 1:190. PubMed Id: 36808185. doi:10.1038/s42003-023-04554-2.
*Bacteriorhodopsin (BR), trimer in asymmetric unit: Haloquadratum walsbyi* A Archaea (expressed in E. coli), 1.85 Å** This BR pumps protons efficiently under acid conditions. antiparallel dimer in asymmetric unit, 2.57 Å: 4QID	4QI1	Data File Jmol Viewer 4QI1 4QID	Hsu et al. (2015). Hsu MF, Fu HY, Cai CJ, Yi HP, Yang CS, & Wang AH (2015). Structural and Functional Studies of a Newly Grouped Haloquadratum walsbyi Bacteriorhodopsin Reveal the Acid-resistant Light-driven Proton Pumping Activity. J Biol Chem 290 :29567-29577. PubMed Id: 26483542. doi:10.1074/jbc.M115.685065.
*Bacteriorhodopsin (BR) crystallized from octylglucoside (OG) detergent micelles: Haloquadratum walsbyi* A Archaea (expressed in E. coli), 2.18 Å** crystallized from styrene maleic acid (SMA) polymer nanodiscs, 2.0 Å: 5ITC	5ITE	Data File Jmol Viewer 5ITE 5ITC	Broecker et al. (2017). Broecker J, Eger BT, & Ernst OP (2017). Crystallogenesis of Membrane Proteins Mediated by Polymer-Bounded Lipid Nanodiscs. Structure 25 :384-392. PubMed Id: 28089451. doi:10.1016/j.str.2016.12.004.
*Halorhodopsin (HR): Halobacterium salinarum* A Archaea, 1.8 Å**	1E12	Data File Jmol Viewer 1E12 halorhodopsin	Kolbe et al. (2000). Kolbe M, Besir H, Essen L-O, & Oesterhelt D (2000). Structure of the light-driven chloride pump halorhodopsin at 1.8 Å. Science 288 :1390-1396. PubMed Id: 10827943.
*bacteriorhodopsin C9A,G12A mutant pressurized with argon: Halobacterium salinarum* B Bacteria (expressed in E. coli), 1.65 Å** pressurized with krypton, 2.00 Å 7Q35 KR2 sodium pump rhodopsin pressurized with krypton, 2.60 Å 7Q36 MAR rhodopsin pressurized with krypton, 2.25 Å 7Q37	7Q38	Data File Jmol Viewer 7Q38 7Q35 7Q37 7Q36	Melnikov et al. (2022). Melnikov I, Orekhov P, Rulev M, Kovalev K, Astashkin R, Bratanov D, Ryzhykau Y, Balandin T, Bukhdruker S, Okhrimenko I, Borshchevskiy V, Bourenkov G, Mueller-Dieckmann C, van der Linden P, Carpentier P, Leonard G, Gordeliy V, & Popov A (2022). High-pressure crystallography shows noble gas intervention into protein-lipid interaction and suggests a model for anaesthetic action. Commun Biol 5 1:360. PubMed Id: 35422073. doi:10.1038/s42003-022-03233-y.
*Halorhodopsin (HR): Natronomonas pharaonis* A Archaea, 2.0 Å**	3A7K	Data File Jmol Viewer 3A7K	Kouyama et al. (2010). Kouyama T, Kanada S, Takeguchi Y, Narusawa A, Murakami M, Ihara K. (2010). Crystal Structure of the Light-Driven Chloride Pump Halorhodopsin from Natronomonas pharaonis. J Mol Biol 396 :564-579. PubMed Id: 19961859.
*Halorhodopsin (SyHR), Cl-pumping mode, ground state: Synechocystis sp. PCC 7509* B Bacteria (expressed in E. coli), 1.58 Å** Cl-pumping mode, K state, 1.70 Å: 7ZOV Cl-pumping mode, O state, 1.60 Å: 7ZOW SO₄⁻-bound form, ground state, 1.91 Å: 7ZOY	7ZOU	Data File Jmol Viewer 7ZOU 7ZOW 7ZOV 7ZOY	Astashkin et al. (2022). Astashkin R, Kovalev K, Bukhdruker S, Vaganova S, Kuzmin A, Alekseev A, Balandin T, Zabelskii D, Gushchin I, Royant A, Volkov D, Bourenkov G, Koonin E, Engelhard M, Bamberg E, & Gordeliy V (2022). Structural insights into light-driven anion pumping in cyanobacteria. Nat Commun 13 1:6460. PubMed Id: 36309497. doi:10.1038/s41467-022-34019-9.
*light-driven cyanobacterial chloride importer: Mastigocladopsis repens* A Archaea (expressed in E. coli), 1.90 Å** with bromide ion, 2.50 Å: 6K6J N63A/P118A mutant, 2.20 Å: 6K6K	6K6I	Data File Jmol Viewer 6K6I 6K6K 6K6J	Yun et al. (2020). Yun JH, Park JH, Jin Z, Ohki M, Wang Y, Lupala CS, Liu H, Park SY, & Lee W (2020). Structure-Based Functional Modification Study of a Cyanobacterial Chloride Pump for Transporting Multiple Anions. J Mol Biol 432 :5273-5286. PubMed Id: 32721401. doi:10.1016/j.jmb.2020.07.016.
*Sensory Rhodopsin: Anabaena (Nostoc) sp. PCC7120* B Bacteria, 2.0 Å**	1XIO	Data File Jmol Viewer 1XIO sensory rhodopsin	Vogeley et al. (2004). Vogeley L, Sineshchekov OA, Trivedi VD, Sasaki J, Spudich JL, & Luecke H (2004). Anabaena sensory rhodopsin: a photochromic color sensor at 2.0 Å. Science 306 :1390-1393. PubMed Id: 15459346.
*Sensory Rhodopsin: Anabaena (Nostoc) sp. PCC7120* B Bacteria (expressed in E. coli), NMR Structure**	2M3G	Data File Jmol Viewer 2M3G	Wang et al. (2013). Wang S, Munro RA, Shi L, Kawamura I, Okitsu T, Wada A, Kim SY, Jung KH, Brown LS, & Ladizhansky V (2013). Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein. Nat Methods 10 :1007-1012. PubMed Id: 24013819. doi:10.1038/nmeth.2635.
*Sensory Rhodopsin II (SRII): Natronomonas pharaonis* A Archaea, 2.40 Å**	1JGJ	Data File Jmol Viewer 1JGJ sensory rhodopsin II	Luecke et al. (2001). Luecke H, Schobert B, Lanyi JK, Spudich EN, & Spudich JL (2001). Crystal structure of sensory rhodopsin II at 2.4 Å: Insights into color tuning and transducer interaction. Science 293 :1499-1503. PubMed Id: 11452084.
*Sensory Rhodopsin II (SRII): Natronomonas pharaonis* A Archaea (expressed in E. coli), 2.10 Å**	1H68	Data File Jmol Viewer 1H68 sensory rhodopsin II	Royant et al. (2001). Royant A, Nollert P, Edman K, Neutze R, Landau EM, & Pebay-Peyroula E. (2001). X-ray structure of sensory rhodopsin II at 2.1 Å resolution. Proc Natl Acad Sci USA 98 :10131-10136. PubMed Id: 11504917.
*Sensory Rhodopsin II (SRII) with transducer: Natronomonas pharaonis* A Archaea (expressed in E. coli), 1.93 Å**	1H2S	Data File Jmol Viewer 1H2S sensory rhodopsin transducer	Gordeliy et al. (2002). Gordeliy VI, Labahn J, Moukhametzianov R, Efremov R, Granzin J, Schlesinger R, Büldt G, Savopol T, Scheidig AJ, Klare JP, & Engelhard M. (2002). Molecular basis of transmembrane signalling by sensory rhodopsin II-transducer complex. Nature 419 :484-487. PubMed Id: 12368857.
*Sensory Rhodopsin II (SRII): Natronomonas pharaonis* A Archaea (expressed in E. coli), NMR structure**	2KSY	Data File Jmol Viewer 2KSY	Gautier et al. (2010). Gautier A, Mott HR, Bostock MJ, Kirkpatrick JP, & Nietlispach D (2010). Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy. Nat Struct Mol Biol 17 :768-774. PubMed Id: 20512150.
*Sensory Rhodopsin II (SRII) in active state: Natronomonas pharaonis* A Archaea (expressed in E. coli), 2.50 Å** SR II in ground state, 1.90 Å: 3QAP	3QDC	Data File Jmol Viewer 3QDC 3QAP	Gushchin et al. (2011). Gushchin I, Reshetnyak A, Borshchevskiy V, Ishchenko A, Round E, Grudinin S, Engelhard M, Büldt G, & Gordeliy V (2011). Active state of sensory rhodopsin II: structural determinants for signal transfer and proton pumping. J Mol Biol 412 :591-600. PubMed Id: 21840321. doi:10.1016/j.jmb.2011.07.022.
*Archaerhodopsin-1 (aR-1): Halorubrum sp. aus-1* A Archaea, 3.4 Å**	1UAZ	Data File Jmol Viewer 1UAZ	Enami et al. (2006). Enami N, Yoshimura K, Murakami M, Okumura H, Ihara K, & Kouyama T. (2006). Crystal Structures of Archaerhodopsin-1 and -2: Common Structural Motif in Archaeal Light-driven Proton Pumps. J Mol Biol 356 :675-685. PubMed Id: 16540121.
*Archaerhodopsin-2 (aR-2): Haloroubrum sp. aus-2* A Archaea, 2.5 Å**	1VGO	Data File Jmol Viewer 1VGO	Enami et al. (2006). Enami N, Yoshimura K, Murakami M, Okumura H, Ihara K, & Kouyama T. (2006). Crystal Structures of Archaerhodopsin-1 and -2: Common Structural Motif in Archaeal Light-driven Proton Pumps. J Mol Biol 356 :675-685. PubMed Id: 16540121.
*Archaerhodopsin-2 (aR-2): Haloroubrum sp. aus-2* A Archaea, 2.10 Å** Crystallized with the carotenoid bacterioruberin, space group P321. Space group P6₃, 2.50 Å: 2Z55.	2EI4	Data File Jmol Viewer 2EI4 2Z55	Yoshimura & Kouyama. (2008). Yoshimura K & Kouyama T (2008). Structural role of bacterioruberin in the trimeric structure of archaerhodopsin-2. J Mol Biol 375 :1267-1281. PubMed Id: 18082767.
*Archaerhodopsin-2 (aR-2): Haloroubrum sp. aus-2* A Archaea, 1.80 Å**	3WQJ	Data File Jmol Viewer 3WQJ	Kouyama et al. (2014). Kouyama T, Fujii R, Kanada S, Nakanishi T, Chan SK, & Murakami M (2014). Structure of archaerhodopsin-2 at 1.8?Å resolution. Acta Crystallogr D Biol Crystallogr 70 :2692-2701. PubMed Id: 25286853. doi:10.1107/S1399004714017313.
*Archaerhodopsin-3 (aR-3), Dark-adapted state at 100 K: Halorubrum sodomense* A Archaea, 1.30 Å** Ground state structure at 100 K, 1.07 Å: 6S6C	6GUX	Data File Jmol Viewer 6GUX 6S6C	Bada Juarez et al. (2021). Bada Juarez JF, Judge PJ, Adam S, Axford D, Vinals J, Birch J, Kwan TOC, Hoi KK, Yen HY, Vial A, Milhiet PE, Robinson CV, Schapiro I, Moraes I, & Watts A (2021). Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization. Nat Commun 12 1:629. PubMed Id: 33504778. doi:10.1038/s41467-020-20596-0.
*Archaerhodopsin-3 (aR-3) in the ground state from LCP crystals using a thin-film sandwich at room temperature: Halorubrum sodomense* A Archaea, 1.90 Å** Dark-adapted structure, 1.85 Å 6S63	6GUZ	Data File Jmol Viewer 6GUZ 6S63	Axford et al. (2022). Axford D, Judge PJ, Bada Juarez JF, Kwan TOC, Birch J, Vinals J, Watts A, & Moraes I (2022). Two states of a light-sensitive membrane protein captured at room temperature using thin-film sample mounts. Acta Crystallogr D Struct Biol 78 :52-58. PubMed Id: 34981761. doi:10.1107/S2059798321011220.
*Xanthorhodopsin: Salinibacter ruber* B Bacteria, 1.90 Å** Contains bound carotenoid.	3DDL	Data File Jmol Viewer 3DDL	Luecke et al. (2008). Luecke H, Schobert B, Stagno J, Imasheva ES, Wang JM, Balashov SP, & Lanyi JK (2008). Crystallographic structure of xanthorhodopsin, the light-driven proton pump with a dual chromophore. Proc Natl Acad Sci USA 105 :16561-16565. PubMed Id: 18922772.
Acetabularia Rhodopsin II (ARII): Acetabularia acetabulum E Eukaryota (expressed in cell-free expression), 3.20 Å This the first structure of a eukaryotic light-driven proton pump	3AM6	Data File Jmol Viewer 3AM6	Wada et al. (2011). Wada T, Shimono K, Kikukawa T, Hato M, Shinya N, Kim SY, Kimura-Someya T, Shirouzu M, Tamogami J, Miyauchi S, Jung KH, Kamo N, & Yokoyama S (2011). Crystal Structure of the Eukaryotic Light-Driven Proton-Pumping Rhodopsin, Acetabularia Rhodopsin II, from Marine Alga J Mol Biol 411 :986-998. PubMed Id: 21726566. doi:10.1016/j.jmb.2011.06.028.
*Channelrhodopsin (ChR) chimera between ChR1 & ChR2: Chlamydomonas reinhardtii* E Eukaryota (expressed in S. frugiperda), 2.30 Å** First ChR structure. Reveals cation conduction pathway.	3UG9	Data File Jmol Viewer 3UG9	Kato et al. (2012). Kato HE, Zhang F, Yizhar O, Ramakrishnan C, Nishizawa T, Hirata K, Ito J, Aita Y, Tsukazaki T, Hayashi S, Hegemann P, Maturana AD, Ishitani R, Deisseroth K, & Nureki O (2012). Crystal structure of the channelrhodopsin light-gated cation channel. Nature 482 :369-374. PubMed Id: 22266941. doi:10.1038/nature10870.
*Channelrhodopsin (ChR) chimera between ChR1 & ChR2, T198G/G202A mutant: Chlamydomonas reinhardtii* E Eukaryota (expressed in S. frugiperda), 2.50 Å** Blue-shifted mutant	4YZI	Data File Jmol Viewer 4YZI	Kato et al. (2015). Kato HE, Kamiya M, Sugo S, Ito J, Taniguchi R, Orito A, Hirata K, Inutsuka A, Yamanaka A, Maturana AD, Ishitani R, Sudo Y, Hayashi S, & Nureki O (2015). Atomistic design of microbial opsin-based blue-shifted optogenetics tools. Nat Commun 6 :7177. PubMed Id: 25975962. doi:10.1038/ncomms8177.
*Channelrhodopsin (ChR) chimera between ChR1 & ChR2 by serial femtosecond crystallogrphy, dark state: Chlamydomonas reinhardtii* E Eukaryota (expressed in Spodoptera frugiperda), 2.30 Å** 1 μsec structure, 2.50 Å: 7E6Y 50 μ structure, 2.50 Å: 7E6Z 250 μsec structure, 2.50 Å: 7E70 1 msec structure, 2.50 Å: 7E71 4 msec structure, 2.50 Å: 7E6X	7C86	Data File Jmol Viewer 7C86 7E71 7E6Z 7E6Y 7E70 7E6X	Oda et al. (2021). Oda K, Nomura T, Nakane T, Yamashita K, Inoue K, Ito S, Vierock J, Hirata K, Maturana AD, Katayama K, Ikuta T, Ishigami I, Izume T, Umeda R, Eguma R, Oishi S, Kasuya G, Kato T, Kusakizako T, Shihoya W, Shimada H, Takatsuji T, Takemoto M, Taniguchi R, Tomita A, Nakamura R, Fukuda M, Miyauchi H, Lee Y, Nango E, Tanaka R, Tanaka T, Sugahara M, Kimura T, Shimamura T, Fujiwara T, Yamanaka Y, Owada S, Joti Y, Tono K, Ishitani R, Hayashi S, Kandori H, Hegemann P, Iwata S, Kubo M, Nishizawa T, & Nureki O (2021). Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin. Elife 10 :e62389. PubMed Id: 33752801. doi:10.7554/eLife.62389.
*iC++ designed anion channelrhodopsin, pH 8.5: designed* U Unclassified (expressed in S. frugiperda), 2.9 Å** pH 6.5, 3.2 Å: 6CSO	6CSN	Data File Jmol Viewer 6CSN 6CSO	Kato et al. (2018). Kato HE, Kim YS, Paggi JM, Evans KE, Allen WE, Richardson C, Inoue K, Ito S, Ramakrishnan C, Fenno LE, Yamashita K, Hilger D, Lee SY, Berndt A, Shen K, Kandori H, Dror RO, Kobilka BK, & Deisseroth K (2018). Structural mechanisms of selectivity and gating in anion channelrhodopsins. Nature 561 7723:349-354. PubMed Id: 30158697. doi:10.1038/s41586-018-0504-5.
*Channelrhodopsin 2 (ChR2): Chlamydomonas reinhardtii* E Eukaryota (expressed in Leishmania tarentolae), 2.39 Å** C128T mutant, 2.7 Å: 6EIG	6EID	Data File Jmol Viewer 6EID 6EIG	Volkov et al. (2017). Volkov O, Kovalev K, Polovinkin V, Borshchevskiy V, Bamann C, Astashkin R, Marin E, Popov A, Balandin T, Willbold D, Büldt G, Bamberg E, Gordeliy V (2017). Structural insights into ion conduction by channelrhodopsin 2 Science 358 6366:eaan8862. PubMed Id: 29170206. doi:10.1126/science.aan8862.
*anion channelrhodopsin-1 (ACR1) light-gated anion channel: Guillardia theta* E Eukaryota (expressed in S. frugiperda), 2.9 Å**	6CSM	Data File Jmol Viewer 6CSM	Kim et al. (2018). Kim YS, Kato HE, Yamashita K, Ito S, Inoue K, Ramakrishnan C, Fenno LE, Evans KE, Paggi JM, Dror RO, Kandori H, Kobilka BK, & Deisseroth K (2018). Crystal structure of the natural anion-conducting channelrhodopsin GtACR1. Nature 561 7723:343-348. PubMed Id: 30158696. doi:10.1038/s41586-018-0511-6.
*anion channelrhodopsin-1 (ACR1) light-gated anion channel in dark (closed) state: Guillardia theta* E Eukaryota (expressed in S. frugiperda), 2.9 Å**	6EDQ	Data File Jmol Viewer 6EDQ	Li et al. (2019). Li H, Huang CY, Govorunova EG, Schafer CT, Sineshchekov OA, Wang M, Zheng L, & Spudich JL (2019). Crystal structure of a natural light-gated anion channelrhodopsin. Elife 8 :e41741. PubMed Id: 30614787. doi:10.7554/eLife.41741.
*anion channelrhodopsin-1 (ACR1) light-gated anion channel, bromide bound: Guillardia theta* E Eukaryota (expressed in Komagataella pastoris), 3.20 Å**	7L1E	Data File Jmol Viewer 7L1E	Li et al. (2021). Li H, Huang CY, Govorunova EG, Sineshchekov OA, Yi A, Rothschild KJ, Wang M, Zheng L, & Spudich JL (2021). The crystal structure of bromide-bound GtACR1 reveals a pre-activated state in the transmembrane anion tunnel. Elife 10 :e65903. PubMed Id: 33998458. doi:10.7554/eLife.65903.
*Channelrhodopsin Chrimson: Chlamydomonas noctigama* E Eukaryota (expressed in S. frugiperda), 2.6 Å**	5ZIH	Data File Jmol Viewer 5ZIH	Oda et al. (2018). Oda K, Vierock J, Oishi S, Rodriguez-Rozada S, Taniguchi R, Yamashita K, Wiegert JS, Nishizawa T, Hegemann P, & Nureki O (2018). Crystal structure of the red light-activated channelrhodopsin Chrimson. Nat Commun 9 1. PubMed Id: 30258177. doi:10.1038/s41467-018-06421-9.
*Proteorhodopsin (green-light absorbing): Uncultured marine gamma proteobacterium ebac31a08* B Bacteria (expressed in E. coli-based cell-free expression system), NMR Structure**	2L6X	Data File Jmol Viewer 2L6X	Reckel et al. (2011). Reckel S, Gottstein D, Stehle J, Löhr F, Verhoefen MK, Takeda M, Silvers R, Kainosho M, Glaubitz C, Wachtveitl J, Bernhard F, Schwalbe H, Güntert P, Dötsch V (2011). Solution NMR structure of proteorhodopsin. Angew Chem Int Ed Engl 50 :11942-11946. PubMed Id: 22034093. doi:10.1002/anie.201105648.
*Proteorhodopsin (green-light absorbing): uncultured Gammaproteobacteria bacterium* B Bacteria (expressed in E. coli), 2.93 Å** cryo-EM structure	7B03	Data File Jmol Viewer 7B03	Hirschi et al. (2021). Hirschi S, Kalbermatter D, Ucurum Z, Lemmin T, & Fotiadis D (2021). Cryo-EM structure and dynamics of the green-light absorbing proteorhodopsin. Nat Commun 12 1. PubMed Id: 34226545. doi:10.1038/s41467-021-24429-6.
*Proteorhodopsin: Exiguobacterium sibiricum* B Bacteria (expressed in E. coli), 2.30 Å** Lysine is the proton donor in this novel proteorhodopsin	4HYJ	Data File Jmol Viewer 4HYJ	Gushchin et al. (2013). Gushchin I, Chervakov P, Kuzmichev P, Popov AN, Round E, Borshchevskiy V, Ishchenko A, Petrovskaya L, Chupin V, Dolgikh DA, Arseniev AA, Kirpichnikov M, & Gordeliy V (2013). Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria. Proc Natl Acad Sci USA 110 :12631-12636. PubMed Id: 23872846. doi:10.1073/pnas.1221629110.
*Proteorhodopsin (blue-light absorbing), Med12BPR: uncultured bacterium* B Bacteria (expressed in E. coli), 2.31 Å** Isolated from the Mediterranean Sea at a depth of 12 m. Oligomerizes as a hexameric ring.	4JQ6	Data File Jmol Viewer 4JQ6	Ran et al. (2013). Ran T, Ozorowski G, Gao Y, Sineshchekov OA, Wang W, Spudich JL, & Luecke H (2013). Cross-protomer interaction with the photoactive site in oligomeric proteorhodopsin complexes. Acta Crystallogr D Biol Crystallogr 69 :1965-1980. PubMed Id: 24100316.
*Proteorhodopsin (blue-light absorbing); HOT75BPR, D97N mutant: gamma proteobacterium* B Bacteria (expressed in E. coli), 2.70 Å** Isolated from the Pacific Ocean near Hawaii at a depth of 75 m. Oligomerizes as a pentameric ring. D97N/Q105L mutant, 2.60 Å: 4KNF	4KLY	Data File Jmol Viewer 4KLY 4KNF	Ran et al. (2013). Ran T, Ozorowski G, Gao Y, Sineshchekov OA, Wang W, Spudich JL, & Luecke H (2013). Cross-protomer interaction with the photoactive site in oligomeric proteorhodopsin complexes. Acta Crystallogr D Biol Crystallogr 69 :1965-1980. PubMed Id: 24100316.
*Cruxrhodopsin-3 (cR3), pH 5: Haloarcula vallismortis* A Archaea (expressed in H. salinarum), 2.10 Å** at pH 6, 2.30 Å: 4JR8	4L35	Data File Jmol Viewer 4L35 4JR8	Chan et al. (2014). Chan SK, Kitajima-Ihara T, Fujii R, Gotoh T, Murakami M, Ihara K, & Kouyama T (2014). Crystal Structure of Cruxrhodopsin-3 from Haloarcula vallismortis. PLoS ONE 9 9:e108362. PubMed Id: 25268964. doi:10.1371/journal.pone.0108362.
*KR2 light-driven Na⁺ pump, acidic conditions: Krokinobacter eikastus* B Bacteria (expressed in E. coli), 2.30 Å** basic conditions, 2.30 Å: 3X3C Species name has changed to Dokdonia eikasta. See Int J Syst Evol Microbiol* (2012) doi: 10.1099/ijs.0.035253-0. But K. eikastus remains in common use in the literature.*	3X3B	Data File Jmol Viewer 3X3B 3X3C	Kato et al. (2015). Kato HE, Inoue K, Abe-Yoshizumi R, Kato Y, Ono H, Konno M, Hososhima S, Ishizuka T, Hoque MR, Kunitomo H, Ito J, Yoshizawa S, Yamashita K, Takemoto M, Nishizawa T, Taniguchi R, Kogure K, Maturana AD, Iino Y, Yawo H, Ishitani R, Kandori H, & Nureki O (2015). Structural basis for Na⁺ transport mechanism by a light-driven Na⁺ pump. Nature 521 :48-53. PubMed Id: 25849775. doi:10.1038/nature14322.
*KR2 light-driven Na⁺ pump, pentameric form at pH 6.0: Krokinobacter eikastus* B Bacteria (expressed in E. coli), 2.7 Å** pentameric form at pH 5.0, 2.6 Å: 6REZ pentameric form at pH 8.0, 2.2 Å: 6REW pentameric form S254A at pH 8.0, 2.4 Å: 6RF4 pentameric form G263F ar pH 8.0, 2.4 Å: 6RF3 pentameric "wet" form, 2.8 Å: 6RF1 pentameric "dry" form, 3 Å: 6RF0 monomeric pH 6.0, 2.3 Å: 6RF5 monomeric form H30K at pH 8.0, 2.2 Å: 6RFA monomeric form at pH 8.9, Å: 6RF7 monomeric form G263F at pH 4.3, 2.0 Å: 6RFC monomeric form S254A at pH 4.3, 2.1 Å: 6RFB monomeric form at pH 8.0, 1.8 Å: 6RF6	6REX	Data File Jmol Viewer 6REX 6REZ 6REW 6RF6 6RFA 6RF5 6RF1 6RF4 6RF3 6RF0 6RFC 6RF7 6RFB	Kovalev et al. (2019). Kovalev K, Polovinkin V, Gushchin I, Alekseev A, Shevchenko V, Borshchevskiy V, Astashkin R, Balandin T, Bratanov D, Vaganova S, Popov A, Chupin V, Büldt G, Bamberg E, & Gordeliy V (2019). Structure and mechanisms of sodium-pumping KR2 rhodopsin. Sci Adv 5 4:eaav2671. PubMed Id: 30989112. doi:10.1126/sciadv.aav2671.
*KR2 light-driven Na⁺ pump, pentameric form in O-state, pH 8: Krokinobacter eikastus* B Bacteria (expressed in E. coli), 2.10 Å** D116N mutant, monomeric form, pH 4.6, 1.80 Å: 6YBY D116N mutant, pentameric form, pH 8.0, 2.35 Å: 6YBZ steady-state-SMX activated state, pentameric form at room temperature, pH 8.0, 2.70 Å: 6YC0 H30A, pentameric form, pH 8.0, 2.20 Å: 6YC1 pentameric form at room temperature, pH 8.0, 2.50 Å: 6YC2 pentameric form, pH 8.0, 2.00 Å: 6YC3 steady-state activated state, pentameric form at room temperature, pH 8.0, 2.60 Å: 6YC4	6XYT	Data File Jmol Viewer 6XYT 6YC1 6YBY 6YC3 6YC2 6YC4 6YBZ 6YC0	Kovalev et al. (2020). Kovalev K, Astashkin R, Gushchin I, Orekhov P, Volkov D, Zinovev E, Marin E, Rulev M, Alekseev A, Royant A, Carpentier P, Vaganova S, Zabelskii D, Baeken C, Sergeev I, Balandin T, Bourenkov G, Carpena X, Boer R, Maliar N, Borshchevskiy V, Büldt G, Bamberg E, & Gordeliy V (2020). Molecular mechanism of light-driven sodium pumping. Nat Commun 11 1:2137. PubMed Id: 32358514. doi:10.1038/s41467-020-16032-y.
*KR2 light-driven Na⁺ pump, monomeric blue form at pH 4.3: Krokinobacter eikastus* B Bacteria (expressed in E. coli), 1.45 Å** Pentameric red form at pH 4.9, 2.20 Å: 4XTN Pentameric red form at pH 5.6, 1.45 Å: 4XTL	4XTL	Data File Jmol Viewer 4XTL 4XTN 4XTL	Gushchin et al. (2015). Gushchin I, Shevchenko V, Polovinkin V, Kovalev K, Alekseev A, Round E, Borshchevskiy V, Balandin T, Popov A, Gensch T, Fahlke C, Bamann C, Willbold D, Büldt G, Bamberg E, & Gordeliy V (2015). Crystal structure of a light-driven sodium pump. Nat Struct Mol Biol 22 :390-395. PubMed Id: 25849142. doi:10.1038/nsmb.3002.
*KR2 light-driven Na⁺ pump; fsec to msec structural changes. Dark state, acidic conditions: Krokinobacter eikastus* B Bacteria (expressed in E. coli), 1.60 Å** dark state, neutral conditions, 1.60 Å: 6TK6 800fs+2ps, 2.25 Å: 6TK5 1ns+16ns, 2.25 Å: 6TK4 30us+150us, 2.25 Å: 6TK3 1 msec, 2.50 Å: 6TK2 20 msec., 2.50 Å: 6TK1	6TK7	Data File Jmol Viewer 6TK7 6TK6 6TK4 6TK3 6TK5 6TK1 6TK2	Skopintsev et al. (2020). Skopintsev P, Ehrenberg D, Weinert T, James D, Kar RK, Johnson PJM, Ozerov D, Furrer A, Martiel I, Dworkowski F, Nass K, Knopp G, Cirelli C, Arrell C, Gashi D, Mous S, Wranik M, Gruhl T, Kekilli D, Brünle S, Deupi X, Schertler GFX, Benoit RM, Panneels V, Nogly P, Schapiro I, Milne C, Heberle J, & Standfuss J (2020). Femtosecond-to-millisecond structural changes in a light-driven sodium pump. Nature 583 7815:314-318. PubMed Id: 32499654. doi:10.1038/s41586-020-2307-8.
*Thermophilic rhodopsin: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.8 Å**	5AZD	Data File Jmol Viewer 5AZD	Tsukamoto et al. (2016). Tsukamoto T, Mizutani K, Hasegawa T, Takahashi M, Honda N, Hashimoto N, Shimono K, Yamashita K, Yamamoto M, Miyauchi S, Takagi S, Hayashi S, Murata T, & Sudo Y (2016). X-ray Crystallographic Structure of Thermophilic Rhodopsin. J Biol Chem 291 23:12223-12232. PubMed Id: 27129243. doi:10.1074/jbc.M116.719815.
*Heliorhodopsin (HeR): Thermoplasmatales archaeon SG8-52-1* A Archaea (expressed in E. coli), 2.4 Å**	6IS6	Data File Jmol Viewer 6IS6	Shihoya et al. (2019). Shihoya W, Inoue K, Singh M, Konno M, Hososhima S, Yamashita K, Ikeda K, Higuchi A, Izume T, Okazaki S, Hashimoto M, Mizutori R, Tomida S, Yamauchi Y, Abe-Yoshizumi R, Katayama K, Tsunoda SP, Shibata M, Furutani Y, Pushkarev A, Béjà O, Uchihashi T, Kandori H, & Nureki O (2019). Crystal structure of heliorhodopsin. Nature 574 7776:132-136. PubMed Id: 31554965. doi:10.1038/s41586-019-1604-6.
*Heliorhodopsin (HeR), low pH structure: Thermoplasmatales archaeon* A Archaea (expressed in E. coli), 1.97 Å**	7U55	Data File Jmol Viewer 7U55	Besaw et al. (2022). Besaw JE, Reichenwallner J, De Guzman P, Tucs A, Kuo A, Morizumi T, Tsuda K, Sljoka A, Miller RJD, & Ernst OP (2022). Low pH structure of heliorhodopsin reveals chloride binding site and intramolecular signaling pathway. Sci Rep 12 1:13955. PubMed Id: 35977989. doi:10.1038/s41598-022-17716-9.
*Heliorhodopsin (HeR) in the violet form, pH 8.8: Actinomycetia bacterium* B Bacteria (expressed in E. coli), 1.5 Å** blue form at pH 4.3, 1.5 Å: 6SU4	6SU3	Data File Jmol Viewer 6SU3 6SU4	Kovalev et al. (2020). Kovalev K, Volkov D, Astashkin R, Alekseev A, Gushchin I, Haro-Moreno JM, Chizhov I, Siletsky S, Mamedov M, Rogachev A, Balandin T, Borshchevskiy V, Popov A, Bourenkov G, Bamberg E, Rodriguez-Valera F, Büldt G, & Gordeliy V (2020). High-resolution structural insights into the heliorhodopsin family. Proc Natl Acad Sci USA 117 8:4131-4141. PubMed Id: 32034096. doi:10.1073/pnas.1915888117.
*Organic Lake Phycodnavirus rhodopsin II (OLPVRII): Organic Lake phycodnavirus* V Viruses (expressed in E. coli), 1.9 Å** This is the first reported structure of a viral rhodopsin.	6SQG	Data File Jmol Viewer 6SQG	Bratanov et al. (2019). Bratanov D, Kovalev K, Machtens JP, Astashkin R, Chizhov I, Soloviov D, Volkov D, Polovinkin V, Zabelskii D, Mager T, Gushchin I, Rokitskaya T, Antonenko Y, Alekseev A, Shevchenko V, Yutin N, Rosselli R, Baeken C, Borshchevskiy V, Bourenkov G, Popov A, Balandin T, Büldt G, Manstein DJ, Rodriguez-Valera F, Fahlke C, Bamberg E, Koonin E, & Gordeliy V (2019). Unique structure and function of viral rhodopsins. Nat Commun 10 1:4939. PubMed Id: 31666521. doi:10.1038/s41467-019-12718-0.
*NTQ chloride transport rhodopsin, type A crystal: Nonlabens marinus S1-08^T* B Bacteria (expressed in E. coli), 1.57 Å** type B crystal, 2.0 Å: 5G54 Br ion crystal, 2.17 Å: 5G2A T102N mutant, 1.80 Å: 5G2D T102D mutant, 2.31 Å: 5G2C	5G28	Data File Jmol Viewer 5G28 5G2D 5G54 5G2A 5G2C	Kim et al. (2016). Kim K, Kwon SK, Jun SH, Cha JS, Kim H, Lee W, Kim JF, & Cho HS (2016). Crystal structure and functional characterization of a light-driven chloride pump having an NTQ motif. Nat Commun 7 :12677. PubMed Id: 27554809. doi:10.1038/ncomms12677.
*NTQ chloride transport rhodopsin (ClR), dark state: Nonlabens marinus* B Bacteria (expressed in E. coli), 1.65 Å** Structures at different time points: 1 ps, 1.85 Å: 7CRI 2 ps, 1.85 Å: 7CRK 100 ps (0.90 mJ/mm²), 1.85 Å: 7CRS 100 ps (0.17 mJ/mm²), 1.85 Å: 7CRT 100 ps (2.63 mJ/mm²), 1.85 Å: 7CRX 100 ps (6.49 mJ/mm²), 1.85 Å: 7CRY	7CRJ	Data File Jmol Viewer 7CRJ 7CRI 7CRK 7CRY 7CRS 7CRT 7CRX	Yun et al. (2021). Yun JH, Li X, Yue J, Park JH, Jin Z, Li C, Hu H, Shi Y, Pandey S, Carbajo S, Boutet S, Hunter MS, Liang M, Sierra RG, Lane TJ, Zhou L, Weierstall U, Zatsepin NA, Ohki M, Tame JRH, Park SY, Spence JCH, Zhang W, Schmidt M, Lee W, & Liu H (2021). Early-stage dynamics of chloride ion-pumping rhodopsin revealed by a femtosecond X-ray laser. Proc Natl Acad Sci U S A 118 13:e2020486118. PubMed Id: 33753488. doi:10.1073/pnas.2020486118.
*NM-R3 bacterial chloride importer, dark-state, Pulse laser (ND-1%) at 140K: Nonlabens marinus* B Bacteria (expressed in E. coli), 1.9 Å** light-state, Pulse laser (ND-1%) at 140K, 2.00 Å: 6JYF dark-state, with Pulse laser (ND-1%) at 95K, 1.8 Å: 6JY6 light state, Pulse laser (ND-1%) at 95K, 1.8 Å: 6JY7 dark-state, CW laser (ND-3%) at 95K, 1.9 Å: 6JY8 light-state, CW laser (ND-3%) at 95K, 1.9 Å: 6JY9 dark-state, CW laser (ND-10%) at 95K, 1.80 Å: 6JYA light-state, CW laser (ND-10%) at 95K, 1.80 Å: 6JYB dark-state, CW laser (ND-30%) at 95K, 1.89 Å: 6JYC light-state, CW laser (ND-30%) at 95K, 2.01 Å: 6JYD	6JYE	Data File Jmol Viewer 6JYE 6JYB 6JYC 6JY9 6JYD 6JY6 6JY7 6JYF 6JY8 6JYA	Yun et al. (2020). Yun JH, Ohki M, Park JH, Ishimoto N, Sato-Tomita A, Lee W, Jin Z, Tame JRH, Shibayama N, Park SY, & Lee W (2020). Pumping mechanism of NM-R3, a light-driven bacterial chloride importer in the rhodopsin family. Sci Adv 6 6. PubMed Id: 32083178. doi:10.1126/sciadv.aay2042.
*NM-R3 bacterial chloride importer by femtosecond crystallography, resting state structure with bromide ion: Nonlabens marinus* B Bacteria (expressed in E. coli), 2.10 Å** structure at 1 msec after photoexcitation, 2.10 Å 7VGU anion-free structure determined at SACLA, 2.30 Å 7VGV	7VGT	Data File Jmol Viewer 7VGT 7VGV 7VGU	Hosaka et al. (2022). Hosaka T, Nomura T, Kubo M, Nakane T, Fangjia L, Sekine SI, Ito T, Murayama K, Ihara K, Ehara H, Kashiwagi K, Katsura K, Akasaka R, Hisano T, Tanaka T, Tanaka R, Arima T, Yamashita A, Sugahara M, Naitow H, Matsuura Y, Yoshizawa S, Tono K, Owada S, Nureki O, Kimura-Someya T, Iwata S, Nango E, & Shirouzu M (2022). Conformational alterations in unidirectional ion transport of a light-driven chloride pump revealed using X-ray free electron lasers. Proc Natl Acad Sci U S A 119 9:e2117433119. PubMed Id: 35197289. doi:10.1073/pnas.2117433119.
*NM-R3 bacterial chloride importer dark state by serial femtosecond crystallography: Nonlabens marinus* B Bacteria (expressed in E. coli), 1.45 Å** dark state structure determined by serial millisecond crystallography, 1.80 Å: 7O8L Anomalous bromide substructure under dark state conditions determined at 13.7 keV, 1.75 Å: 7O8Y light state structure at 10 ps after photoexcitation, 1.90 Å: 7O8G at 10 ns after photoexcitation, 1.80 Å: 7O8H at 1 μs after photoexcitation, 1.80 Å: 7O8I at 20 μs after photoexcitation, 1.80 Å: 7O8J at 300 μs after photoexcitation, 1.90 Å: 7O8K at 2.5 ms after photoexcitation, 2.20 Å: 7O8M at 7.5 ms after photoexcitation, 2.10 Å: 7O8N at 12.5 ms after photoexcitation, 2.20 Å: 7O8O at 17.5 ms after photoexcitation, 2.40 Å: 7O8P at 22.5 ms after photoexcitation, 2.60 Å: 7O8Q at 27.5 ms after photoexcitation, 2.70 Å: 7O8R at 32.5 ms after photoexcitation, 2.50 Å: 7O8S at 45 ms after photoexcitation, 2.50 Å: 7O8U at 55 ms after photoexcitation, 2.50 Å: 7O8V Anomalous bromide substructure under continuous illumination determined at 13.7 keV, 1.80 Å: 7O8Z	7O8F	Data File Jmol Viewer 7O8F 7O8R 7O8L 7O8P 7O8Y 7O8Z 7O8U 7O8K 7O8J 7O8O 7O8G 7O8H 7O8N 7O8Q 7O8M 7O8I 7O8V 7O8S	Mous et al. (2022). Mous S, Gotthard G, Ehrenberg D, Sen S, Weinert T, Johnson PJM, James D, Nass K, Furrer A, Kekilli D, Ma P, Brünle S, Casadei CM, Martiel I, Dworkowski F, Gashi D, Skopintsev P, Wranik M, Knopp G, Panepucci E, Panneels V, Cirelli C, Ozerov D, Schertler GFX, Wang M, Milne C, Standfuss J, Schapiro I, Heberle J, & Nogly P (2022). Dynamics and mechanism of a light-driven chloride pump. Science 375 6583:845-851. PubMed Id: 35113649. doi:10.1126/science.abj6663.
*Rhodopsin phosphodiesterase (Rh-PDE), transmembrane domain: Salpingoeca rosetta* E Eukaryota, 2.60 Å** transmembrane domain and linker region, 3.50 Å: 7D7Q phosphodiesterase domain, 2.10 Å: 7D7P	7CJ3	Data File Jmol Viewer 7CJ3 7D7Q 7D7P	Ikuta et al. (2020). Ikuta T, Shihoya W, Sugiura M, Yoshida K, Watari M, Tokano T, Yamashita K, Katayama K, Tsunoda SP, Uchihashi T, Kandori H, & Nureki O (2020). Structural insights into the mechanism of rhodopsin phosphodiesterase. Nat Commun 11 1:5605. PubMed Id: 33154353. doi:10.1038/s41467-020-19376-7.
*cyanorhodopsin (CyR) N2098R: Calothrix sp. NIES-2098* B Bacteria (expressed in E. coli), 2.65 Å**	6LM0	Data File Jmol Viewer 6LM0	Hasegawa et al. (2020). Hasegawa M, Hosaka T, Kojima K, Nishimura Y, Nakajima Y, Kimura-Someya T, Shirouzu M, Sudo Y, & Yoshizawa S (2020). A unique clade of light-driven proton-pumping rhodopsins evolved in the cyanobacterial lineage. Sci Rep 10 1:16752. PubMed Id: 33028840. doi:10.1038/s41598-020-73606-y.
*cyanorhodopsin (CyR) N4075R: Tolypothrix sp. NIES-4075* B Bacteria (expressed in E. coli), 1.90 Å**	6LM1	Data File Jmol Viewer 6LM1	Hasegawa et al. (2020). Hasegawa M, Hosaka T, Kojima K, Nishimura Y, Nakajima Y, Kimura-Someya T, Shirouzu M, Sudo Y, & Yoshizawa S (2020). A unique clade of light-driven proton-pumping rhodopsins evolved in the cyanobacterial lineage. Sci Rep 10 1:16752. PubMed Id: 33028840. doi:10.1038/s41598-020-73606-y.
*viral rhodopsin OLPVR1 in P1 space group: Organic Lake phycodnavirus* V Viruses (expressed in E. coli), 1.60 Å** viral rhodopsin OLPVR1 in P1212 space group, 1.40 Å: 7AKY viral rhodopsins chimera O1O2, 1.96 Å: 7AKW	7AKX	Data File Jmol Viewer 7AKX 7AKW 7AKY	Zabelskii et al. (2020). Zabelskii D, Alekseev A, Kovalev K, Rankovic V, Balandin T, Soloviov D, Bratanov D, Savelyeva E, Podolyak E, Volkov D, Vaganova S, Astashkin R, Chizhov I, Yutin N, Rulev M, Popov A, Eria-Oliveira AS, Rokitskaya T, Mager T, Antonenko Y, Rosselli R, Armeev G, Shaitan K, Vivaudou M, Büldt G, Rogachev A, Rodriguez-Valera F, Kirpichnikov M, Moser T, Offenhäusser A, Willbold D, Koonin E, Bamberg E, & Gordeliy V (2020). Viral rhodopsins 1 are an unique family of light-gated cation channels. Nat Commun 11 1:5707. PubMed Id: 33177509. doi:10.1038/s41467-020-19457-7.
*light-driven proton pump LR (Mac): Leptosphaeria maculans* E Eukaryota (expressed in Leishmania tarentolae), 2.20 Å**	7BMH	Data File Jmol Viewer 7BMH	Zabelskii et al. (2021). Zabelskii D, Dmitrieva N, Volkov O, Shevchenko V, Kovalev K, Balandin T, Soloviov D, Astashkin R, Zinovev E, Alekseev A, Round E, Polovinkin V, Chizhov I, Rogachev A, Okhrimenko I, Borshchevskiy V, Chupin V, Büldt G, Yutin N, Bamberg E, Koonin E, & Gordeliy V (2021). Structure-based insights into evolution of rhodopsins. Commun Biol 4 1:821. PubMed Id: 34193947. doi:10.1038/s42003-021-02326-4.
*Bestrhodopsin (rhodopsin-rhodopsin-bestrophin) complex: Phaeocystis* E Eukaryota (expressed in Spodoptera frugiperda), 3.21 Å** cryo-EM structure	7PL9	Data File Jmol Viewer 7PL9	Rozenberg et al. (2022). Rozenberg A, Kaczmarczyk I, Matzov D, Vierock J, Nagata T, Sugiura M, Katayama K, Kawasaki Y, Konno M, Nagasaka Y, Aoyama M, Das I, Pahima E, Church J, Adam S, Borin VA, Chazan A, Augustin S, Wietek J, Dine J, Peleg Y, Kawanabe A, Fujiwara Y, Yizhar O, Sheves M, Schapiro I, Furutani Y, Kandori H, Inoue K, Hegemann P, Béjà O, & Shalev-Benami M (2022). Rhodopsin-bestrophin fusion proteins from unicellular algae form gigantic pentameric ion channels. Nat Struct Mol Biol 29 6:592-603. PubMed Id: 35710843. doi:10.1038/s41594-022-00783-x.
*DTG rhodopsin: Pseudomonas putida* B Bacteria (expressed in E. coli), 2.84 Å**	7W74	Data File Jmol Viewer 7W74	Suzuki et al. (2022). Suzuki K, Del Carmen Marín M, Konno M, Bagherzadeh R, Murata T, & Inoue K (2022). Structural characterization of proton-pumping rhodopsin lacking a cytoplasmic proton donor residue by X-ray crystallography. J Biol Chem 298 3:101722. PubMed Id: 35151692. doi:10.1016/j.jbc.2022.101722.
*Schizorhodopsin 4 (SzR): Asgard group archaeon* A Archaea (expressed in E. coli), 2.10 Å**	7E4G	Data File Jmol Viewer 7E4G	Higuchi et al. (2021). Higuchi A, Shihoya W, Konno M, Ikuta T, Kandori H, Inoue K, & Nureki O (2021). Crystal structure of schizorhodopsin reveals mechanism of inward proton pumping. Proc Natl Acad Sci U S A 118 14:e2016328118. PubMed Id: 33790007. doi:10.1073/pnas.2016328118.
*Coccomyxa subellipsoidea rhodopsin (CsR) Light-driven proton pump,: Coccomyxa subellipsoidea* E Eukaryota (expressed in Spodoptera frugiperda), 2.00 Å**	6GYH	Data File Jmol Viewer 6GYH	Fudim et al. (2019). Fudim R, Szczepek M, Vierock J, Vogt A, Schmidt A, Kleinau G, Fischer P, Bartl F, Scheerer P, & Hegemann P (2019). Design of a light-gated proton channel based on the crystal structure of Coccomyxa rhodopsin. Sci Signal 12 573:eaav4203. PubMed Id: 30890657. doi:10.1126/scisignal.aav4203.
Gloeobacter rhodopsin: Gloeobacter violaceus B Bacteria (expressed in E. coli), 2.00 Å	6NWD	Data File Jmol Viewer 6NWD	Morizumi et al. (2019). Morizumi T, Ou WL, Van Eps N, Inoue K, Kandori H, Brown LS, & Ernst OP (2019). X-ray Crystallographic Structure and Oligomerization of Gloeobacter Rhodopsin. Sci Rep 9 1:11283. PubMed Id: 31375689. doi:10.1038/s41598-019-47445-5.
*Rhodopsin chloride pump: Mastigocladopsis repens* B Bacteria (expressed in E.coli), 2.33 Å** Proton-pumping mutant, 2.50 Å: 6WP8	6XL3	Data File Jmol Viewer 6XL3 6WP8	Besaw et al. (2020). Besaw JE, Ou WL, Morizumi T, Eger BT, Sanchez Vasquez JD, Chu JHY, Harris A, Brown LS, Miller RJD, & Ernst OP (2020). The crystal structures of a chloride-pumping microbial rhodopsin and its proton-pumping mutant illuminate proton transfer determinants. J Biol Chem 295 44:14793-14804. PubMed Id: 32703899. doi:10.1074/jbc.RA120.014118.
*ChRmine channel rhodopsin in small diameter lipid nanodisc: Rhodomonas lens* E Eukaryota (expressed in Spodoptera frugiperda), 2.74 Å** cryo-EM structure in large diameter nanodisc, 2.74 Å: 7SFJ Apo-ChRmine in MSP1E3D1 lipid nanodisc, 4.10 Å: 7SHS	7SFK	Data File Jmol Viewer 7SFK 7SHS 7SFJ	Tucker et al. (2022). Tucker K, Sridharan S, Adesnik H, & Brohawn SG (2022). Cryo-EM structures of the channelrhodopsin ChRmine in lipid nanodiscs. Nat Commun 13 1:4842. PubMed Id: 35977941. doi:10.1038/s41467-022-32441-7.
*ChRmine, pump-like channelrhodopsin: Rhodomonas lens* E Eukaryota (expressed in Spodoptera frugiperda), 2.02 Å** cryo-EM structure	7W9W	Data File Jmol Viewer 7W9W	Kishi et al. (2022). Kishi KE, Kim YS, Fukuda M, Inoue M, Kusakizako T, Wang PY, Ramakrishnan C, Byrne EFX, Thadhani E, Paggi JM, Matsui TE, Yamashita K, Nagata T, Konno M, Quirin S, Lo M, Benster T, Uemura T, Liu K, Shibata M, Nomura N, Iwata S, Nureki O, Dror RO, Inoue K, Deisseroth K, & Kato HE (2022). Structural basis for channel conduction in the pump-like channelrhodopsin ChRmine. Cell 185 4:672-689.e23. PubMed Id: 35114111. doi:10.1016/j.cell.2022.01.007.
Adenylyl Cyclases Membrane-integral adenylyl cyclases are important enzymes in G protein-dependent signal transduction
*Adenylyl cyclase AC9 bound to an activated stimulatory G protein: Bos taurus* E Eukaryota (expressed in Trichoplusia ni), 3.4 Å** cryo-EM structure bound to MANT-GTP, forskolin, and an activated stimulatory Gαs protein, 4.2 Å: 6R4O bound to an activated stimulatory G protein, 3.1 Å: 6R4P	6R3Q	Data File Jmol Viewer 6R3Q 6R4P 6R4O	Qi et al. (2019). Qi C, Sorrentino S, Medalia O, & Korkhov VM (2019). The structure of a membrane adenylyl cyclase bound to an activated stimulatory G protein. Science 364 6438:389-394. PubMed Id: 31023924. doi:10.1126/science.aav0778.
Histidine Kinase Receptors
*ArcB (1-115) Aerobic Respiration Control sensor membrane domain: Escherichia coli (cell-free expression)* B Bacteria, NMR Structure**	2KSD	Data File Jmol Viewer 2KSD	Maslennikov et al. (2010). Maslennikov I, Klammt C, Hwang E, Kefala G, Okamura M, Esquivies L, Mörs K, Glaubitz C, Kwiatkowski W, Jeon YH, & Choe S (2010). Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis. Proc Natl Acad Sci USA 107 :10902-10907. PubMed Id: 20498088.
*QseC (1-185) Sensor protein membrane domain: Escherichia coli (cell-free expression)* B Bacteria, NMR Structure**	2KSE	Data File Jmol Viewer 2KSE	Maslennikov et al. (2010). Maslennikov I, Klammt C, Hwang E, Kefala G, Okamura M, Esquivies L, Mörs K, Glaubitz C, Kwiatkowski W, Jeon YH, & Choe S (2010). Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis. Proc Natl Acad Sci USA 107 :10902-10907. PubMed Id: 20498088.
*QseE histidine kinase sensor domain: Escherichia coli* B Bacteria, 1.33 Å** X-ray structure	8JWD	Data File Jmol Viewer 8JWD	Matsumoto et al. (2023). Matsumoto K, Fukuda Y, & Inoue T (2023). Crystal structures of QseE and QseG: elements of a three-component system from Escherichia coli. Acta Crystallogr F Struct Biol Commun 79 11:285-293. PubMed Id: 37877621. doi:10.1107/S2053230X23009123.
*QseG outer membrane lipoprotein, crystallization condition I: Escherichia coli* B Bacteria, 2.30 Å** X-ray structure crystallization condition II, 2.35 Å: 7X6G crystallization condition III, 2.60 Å: 7X6H	7X6F	Data File Jmol Viewer 7X6F 7X6H 7X6G	Matsumoto et al. (2023). Matsumoto K, Fukuda Y, & Inoue T (2023). Crystal structures of QseE and QseG: elements of a three-component system from Escherichia coli. Acta Crystallogr F Struct Biol Commun 79 11:285-293. PubMed Id: 37877621. doi:10.1107/S2053230X23009123.
*KdpD (397-502) Sensor protein membrane domain: Escherichia coli (cell-free expression)* B Bacteria, NMR Structure**	2KSF	Data File Jmol Viewer 2KSF	Maslennikov et al. (2010). Maslennikov I, Klammt C, Hwang E, Kefala G, Okamura M, Esquivies L, Mörs K, Glaubitz C, Kwiatkowski W, Jeon YH, & Choe S (2010). Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis. Proc Natl Acad Sci USA 107 :10902-10907. PubMed Id: 20498088.
*NarQ nitrate/nitrite sensor histidine kinase in symmetric holo state: Escherichia coli* B Bacteria, 1.94 Å** Structure includes the sensor, TM, and HAMP domains in asymmetric holo state, 2.42 Å: 5JEF R50K mutant in symmetric apo state, 1.9 Å: 5JEQ	5IJI	Data File Jmol Viewer 5IJI 5JEF 5JEQ	Gushchin et al. (2017). Gushchin I, Melnikov I, Polovinkin V, Ishchenko A, Yuzhakova A, Buslaev P, Bourenkov G, Grudinin S, Round E, Balandin T, Borshchevskiy V, Willbold D, Leonard G, Büldt G, Popov A, & Gordeliy V (2017). Mechanism of transmembrane signaling by sensor histidine kinases. Science 356 :eaah6345. PubMed Id: 28522691. doi:10.1126/science.aah6345.
*NarQ histidine kinase proteolytic fragment: Escherichia coli* B Bacteria, 2.3 Å**	6XYN	Data File Jmol Viewer 6XYN	no PubMed entry (2020) Gushchin I, Melnikov I, Polovinkin V, Ishchenko A, & Gordeliy V (2020). Crystal structure of a proteolytic fragment of the sensor histidine kinase NarQ Crystals 10 :149. doi:103390/cryst10030149.
*histidine kinase NarQ (R50S variant) fragment: Escherichia coli* B Bacteria, 2.40 Å**	6YUE	Data File Jmol Viewer 6YUE	Gushchin et al. (2020). Gushchin I, Orekhov P, Melnikov I, Polovinkin V, Yuzhakova A, & Gordeliy V (2020). Sensor Histidine Kinase NarQ Activates via Helical Rotation, Diagonal Scissoring, and Eventually Piston-Like Shifts. Int J Mol Sci 21 9. PubMed Id: 32354084. doi:10.3390/ijms21093110.
Immune Receptors
*T cell receptor-CD3 complex: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.7 Å** cryo-EM structure	6JXR	Data File Jmol Viewer 6JXR	Dong et al. (2019). Dong , Zheng L, Lin J, Zhang B, Zhu Y, Li N, Xie S, Wang Y, Gao N, & Huang Z (2019). Structural basis of assembly of the human T cell receptor-CD3 complex. Nature 573 7775:546-552. PubMed Id: 31461748. doi:10.1038/s41586-019-1537-0.
*Transmembrane ζ-ζ dimer of the TCR-CD3 complex: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure**	2HAC	Data File Jmol Viewer 2HAC	Call et al. (2006). Call ME, Schnell JR, Xu C, Lutz RA, Chou JJ, & Wucherpfennig KW (2006). The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor. Cell 127 :355-368. PubMed Id: 17055436.
*T cell receptor (TCR)-CD3 complex: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure CS-bound TCR-CD3 complex, 3.10 Å 7FJF TCR_β L281A/L285A TCR-CD3 complex, 3.00 Å 7FJE	7FJD	Data File Jmol Viewer 7FJD 7FJF 7FJE	Chen et al. (2022). Chen Y, Zhu Y, Li X, Gao W, Zhen Z, Dong , Huang B, Ma Z, Zhang A, Song X, Ma Y, Guo C, Zhang F, & Huang Z (2022). Cholesterol inhibits TCR signaling by directly restricting TCR-CD3 core tunnel motility. Mol Cell 82 7:1278-1287.e5. PubMed Id: 35271814. doi:10.1016/j.molcel.2022.02.017.
*DAP12 dimeric signaling domain in complex with activating receptor NKG2C: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure** DAP12 dimer: 2L34	2L35	Data File Jmol Viewer 2L35 2L34	Call et al. (2010). Call ME, Wucherpfennig KW, & Chou JJ (2010). The structural basis for intramembrane assembly of an activating immunoreceptor complex. Nature Immunol 11 :1023-1029. PubMed Id: 20890284.
*DAP12 signaling domain trimer: Homo sapiens* E Eukaryota (expressed in E. coli), 1.77 Å** lipidic cubic phase crystallization DAP12 tetramer, 2.14Å: 4WO1	4WOL	Data File Jmol Viewer 4WOL 4WO1	Knoblich et al. (2015). Knoblich K, Park S, Lutfi M, van 't Hag L, Conn CE, Seabrook SA, Newman J, Czabotar PE, Im W, Call ME, & Call MJ (2015). Transmembrane Complexes of DAP12 Crystallized in Lipid Membranes Provide Insights into Control of Oligomerization in Immunoreceptor Assembly. Cell Rep 11 :1184-1192. PubMed Id: 25981043. doi:10.1016/j.celrep.2015.04.045.
*CD28 dimer transmembrane domain: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure**	7VU5	Data File Jmol Viewer 7VU5	Wu et al. (2022). Wu H, Cao R, Wen M, Xue H, & OuYang B (2022). Structural characterization of a dimerization interface in the CD28 transmembrane domain. Structure 30 6:803-812.e5. PubMed Id: 35397202. doi:10.1016/j.str.2022.03.004.
SNARE Protein Family
*Syntaxin 1A/SNAP-25/Synaptobrevin-2 Complex with transmembrane regions: Rattus norvegicus* E Eukaryota (expressed in E. coli), 3.4 Å** I2₁2₁2₁ space group, 4.80 Å: 3HD9.	3HD7	Data File Jmol Viewer 3HD7 3HD9	Stein et al. (2009). Stein A, Weber G, Wahl MC, & Jahn R (2009). Helical extension of the neuronal SNARE complex into the membrane. Nature 460 :525-528. PubMed Id: 19571812.
*Synaptobrevin, lipid-bound : Rattus norvegicus* E Eukaryota (expressed in E. coli), NMR Structure** Protein is in dodecylphosphocholine (DPC) micelles	2KOG	Data File Jmol Viewer 2KOG	Ellena et al. (2009). Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, & Tamm LK (2009). Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. Proc Natl Acad Sci USA 106 :20306-20311. PubMed Id: 19918058. doi:10.1073/pnas.0908317106.
*Syntaxin 1A in prefusion state: Rattus norvegicus* E Eukaryota (expressed in E. coli), NMR Structure** Structure in DPC micelles.	2M8R	Data File Jmol Viewer 2M8R	Liang et al. (2013). Liang B, Kiessling V, & Tamm LK (2013). Prefusion structure of syntaxin-1A suggests pathway for folding into neuronal trans-SNARE complex fusion intermediate. Proc Natl Acad Sci USA 110 :19384-19389. PubMed Id: 24218570. doi:10.1073/pnas.1314699110.
*Synaptotagmin-1 C2A, C2B domains and SNARE-pin proteins: Rattus norvegicus* E Eukaryota (expressed in E. coli), 10.4 Å** cryo-EM structure	6MTI	Data File Jmol Viewer 6MTI	Grushin et al. (2019). Grushin K, Wang J, Coleman J, Rothman JE, Sindelar CV, & Krishnakumar SS (2019). Structural basis for the clamping and Ca²⁺ activation of SNARE-mediated fusion by synaptotagmin. Nat Commun 10 1. PubMed Id: 31160571. doi:10.1038/s41467-019-10391-x.
*Sec1/Munc18-family (SM) Protein Vps45 in complex with Qa SNARE Tlg2: Chaetomium thermophilum* E Eukaryota (expressed in E. coli), 2.80 Å** in complex with Qa SNARE Tlg2 (1-310), 3.90 Å: 6XMD Structure of the SM protein Vps45, 2.00 Å: 6XJL	6XM1	Data File Jmol Viewer 6XM1 6XJL 6XMD	Eisemann et al. (2020). Eisemann TJ, Allen F, Lau K, Shimamura GR, Jeffrey PD, & Hughson FM (2020). The Sec1/Munc18 protein Vps45 holds the Qa-SNARE Tlg2 in an open conformation. Elife 9 . PubMed Id: 32804076. doi:10.7554/eLife.60724.
*STX17/SNAP29/VAMP8 SNARE complex: Homo sapiens* E Eukaryota (expressed in E. coli), 3.05 Å** STX17 LIR region in complex with GABARAP, 2.00 Å: 7BV4	7BV6	Data File Jmol Viewer 7BV6 7BV4	Li et al. (2020). Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, & Pan L (2020). Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. Proc Natl Acad Sci USA 117 35:21391-21402. PubMed Id: 32817423. doi:10.1073/pnas.2006997117.
*synaptobrevin-Munc18-1-syntaxin-1 complex class 2: Rattus norvegicus* E Eukaryota (expressed in E. coli), 3.50 Å** cryo-EM structure class 1, 3.70 Å: 7UDC	7UDB	Data File Jmol Viewer 7UDB 7UDC	Stepien et al. (2022). Stepien KP, Xu J, Zhang X, Bai XC, & Rizo J (2022). SNARE assembly enlightened by cryo-EM structures of a synaptobrevin-Munc18-1-syntaxin-1 complex. Sci Adv 8 25:eabo5272. PubMed Id: 35731863. doi:10.1126/sciadv.abo5272.
Claudins Claudins form the backbone of tight junctions
*Claudin-4 in complex with Clostridium perfringens* enterotoxin C-terminal domain: Homo sapiens E Eukaryota (expressed in Trichoplusia ni), 3.37 Å**	7KP4	Data File Jmol Viewer 7KP4	Vecchio et al. (2021). Vecchio AJ, Rathnayake SS, & Stroud RM (2021). Structural basis for Clostridium perfringens enterotoxin targeting of claudins at tight junctions in mammalian gut. Proc Natl Acad Sci U S A 118 15:e2024651118. PubMed Id: 33876770. doi:10.1073/pnas.2024651118.
*Claudin-4 in complex with Clostridium perfringens* enterotoxin C-terminal domain in complex with sFab COP-2: Homo sapiens E Eukaryota (expressed in Trichoplusia ni), 6.90 Å** cryo-EM structure in complex with sFab COP-3, 5.00 Å: 7TDN	7TDM	Data File Jmol Viewer 7TDM 7TDN	Orlando et al. (2022). Orlando BJ, Dominik PK, Roy S, Ogbu CP, Erramilli SK, Kossiakoff AA, & Vecchio AJ (2022). Development, structure, and mechanism of synthetic antibodies that target claudin and Clostridium perfringens enterotoxin complexes. J Biol Chem 298 9:102357. PubMed Id: 35952760. doi:10.1016/j.jbc.2022.102357.
*Claudin-9 in complex with Clostridium perfringens* enterotoxin C-terminal domain, closed form: Homo sapiens E Eukaryota (expressed in Spodoptera frugiperda), 3.2 Å** open form, 3.25 Å: 6OV3	6OV2	Data File Jmol Viewer 6OV2 6OV3	Vecchio & Stroud (2019). Vecchio AJ, & Stroud RM (2019). Claudin-9 structures reveal mechanism for toxin-induced gut barrier breakdown. Proc Natl Acad Sci USA 116 36:17817-17824. PubMed Id: 31434788. doi:10.1073/pnas.1908929116.
*Caludin-15: Mus musculus* E Eukaryota (expressed in S. frugiperda), 2.61 Å**	4P79	Data File Jmol Viewer 4P79	Suzuki et al. (2014). Suzuki H, Nishizawa T, Tani K, Yamazaki Y, Tamura A, Ishitani R, Dohmae N, Tsukita S, Nureki O, & Fujiyoshi Y (2014). Crystal structure of a claudin provides insight into the architecture of tight junctions. Science 344 :304-307. PubMed Id: 24744376. doi:10.1126/science.1248571.
*Claudin-19 in complex with Clostridium perfringens* enterotoxin: Mus musculus E Eukaryota (expressed in S. frugiperda), 3.70 Å**	3X29	Data File Jmol Viewer 3X29	Saitoh et al. (2015). Saitoh Y, Suzuki H, Tani K, Nishikawa K, Irie K, Ogura Y, Tamura A, Tsukita S, & Fujiyoshi Y (2015). Tight junctions. Structural insight into tight junction disassembly by Clostridium perfringens enterotoxin. Science 347 6223:775-778. PubMed Id: 25678664. doi:10.1126/science.1261833.
TMEM16 Family Proteins A functionally diverse family of proteins also known as Anoctamins
*TMEM16 Ca²⁺-activated lipid scramblase, crystal form 1: Nectria haematococca* E Eukaryota (expressed in S. cerevisiae), 3.30 Å** Crystal form 2, 3.40 Å: 4WIT	4WIS	Data File Jmol Viewer 4WIS 4WIT	Brunner et al. (2014). Brunner JD, Lim NK, Schenck S, Duerst A, & Dutzler R (2014). X-ray structure of a calcium-activated TMEM16 lipid scramblase. Nature 516 7530:207-212. PubMed Id: 25383531. doi:10.1038/nature13984.
*TMEM16 Ca²⁺-activated lipid scramblase in nanodiscs, Ca⁺²-bound open state: Nectria haematococca* E Eukaryota (expressed in S. cerevisiae), 3.6 Å** cryo-EM structure Ca⁺²-bound intermediate state, 3.7 Å: 6QMA Ca⁺²-bound closed state, 3.6 & Aring;:6QMB Ca⁺²-free state, 3.8 Å: 6QM4 in DDM, Ca⁺²-bound state, 3.6 Å: 6QM5 in DDM, Ca⁺²-free state, 3.7 Å: 6QM6	6QM9	Data File Jmol Viewer 6QM9 6QMA 6QM4 6QM5 6QM6 6QMB	Kalienkova et al. (2019). Kalienkova V, Clerico Mosina V, Bryner L, Oostergetel GT, Dutzler R, & Paulino C (2019). Stepwise activation mechanism of the scramblase nhTMEM16 revealed by cryo-EM. Elife 8 :e44364. PubMed Id: 30785398. doi:10.7554/eLife.44364.
*TMEM16 Ca²⁺-activated lipid scramblase in nanodiscs, Ca²⁺-bound, L302A mutant: Nectria haematococca* E Eukaryota (expressed in S. cerevisiae), 4 Å** cryo-EM structure	6OY3	Data File Jmol Viewer 6OY3	Khelashvili et al. (2019). Khelashvili G, Falzone ME, Cheng X, Lee BC, Accardi A, & Weinstein H (2019). Dynamic modulation of the lipid translocation groove generates a conductive ion channel in Ca²⁺-bound nhTMEM16. Nat Commun 10 1:4972. PubMed Id: 31672969. doi:10.1038/s41467-019-12865-4.
*TMEM16A calcium-activated chloride channel: Mus musculus* E Eukaryota (expressed in HEK293 cells), 6.6 Å** cryo-EM structure	5NL2	Data File Jmol Viewer 5NL2	Paulino et al. (2017). Paulino C, Neldner Y, Lam AK, Kalienkova V, Brunner JD, Schenck S, & Dutzler R (2017). Structural basis for anion conduction in the calcium-activated chloride channel TMEM16A. Elife 6 :e26232. PubMed Id: 28561733. doi:10.7554/eLife.26232.
*TMEM16A calcium-activated chloride channel w. bound Ca²⁺: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.75 Å** cryo-EM structure calcium-free structure, 4.06 Å: 5OYG	5OYB	Data File Jmol Viewer 5OYB 5OYG	Paulino et al. (2017). Paulino C, Kalienkova V, Lam AKM, Neldner Y, & Dutzler R (2017). Activation mechanism of the calcium-activated chloride channel TMEM16A revealed by cryo-EM. Nature 552 :421-425. PubMed Id: 29236691. doi:10.1038/nature24652.
*TMEM16A calcium-activated chloride channel embedded in nanodiscs: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.8 Å** solubilized in LMNG, 3.8 Å: 6BGJ	6BGI	Data File Jmol Viewer 6BGI 6BGJ	Dang et al. (2017). Dang S, Feng S, Tien J, Peters CJ, Bulkley D, Lolicato M, Zhao J, Zuberbühler K, Ye W, Qi L, Chen T, Craik CS, Nung Jan Y, Minor DL Jr, Cheng Y, & Yeh Jan L (2017). Cryo-EM structures of the TMEM16A calcium-activated chloride channel. Nature 552 7685:426-429. PubMed Id: 29236684. doi:10.1038/nature25024.
*TMEM16A calcium-activated chloride channel, calcium bound: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.70 Å** cryo-EM structure I551A mutant, calcium free, 3.30 Å: 7B5D I551A mutant, calcium bound, 4.10 Å: 7B5E	7B5C	Data File Jmol Viewer 7B5C 7B5E 7B5D	Lam et al. (2021). Lam AKM, Rheinberger J, Paulino C, & Dutzler R (2021). Gating the pore of the calcium-activated chloride channel TMEM16A. Nat Commun 12 1. PubMed Id: 33542223. doi:10.1038/s41467-020-20787-9.
*TMEM16A calcium-activated chloride channel with bound 1PBC and calcium: Mus musculus* E Eukaryota (expressed in HEK293 cells), 2.85 Å** cryo-EM structure	7ZK3	Data File Jmol Viewer 7ZK3	Lam et al. (2022). Lam AKM, Rutz S, & Dutzler R (2022). Inhibition mechanism of the chloride channel TMEM16A by the pore blocker 1PBC. Nat Commun 13 1:2798. PubMed Id: 35589730. doi:10.1038/s41467-022-30479-1.
*TMEM16 scramblase in nanodiscs in the presence of Ca²⁺: Neosartorya fumigata* E Eukaryota (expressed in S. cerevisiae), 4.05 Å** cryo-EM structure in the absence of calcium, 3.89 Å: 6DZ7 in the presence of calcium and ceramide 24:0, 3.59 Å: 6E1O	6E0H	Data File Jmol Viewer 6E0H 6DZ7 6E1O	Falzone et al. (2019). Falzone ME, Rheinberger J, Lee BC, Peyear T, Sasset L, Raczkowski AM, Eng ET, Di Lorenzo A, Andersen OS, Nimigean CM, & Accardi A (2019). Structural basis of Ca²⁺-dependent activation and lipid transport by a TMEM16 scramblase. Elife 8 :e43229. PubMed Id: 30648972. doi:10.7554/eLife.43229.
*TMEM16F scramblase & ion channel in lipid nanodiscs, Ca⁺²-bound state: Mus musculus* E Eukaryota (expressed in GnTI^- cells), 3.5 Å** cryo-EM structure Ca⁺²-free state, 3.3 Å: 6QPI in digitonin, Ca⁺²-bound state, 3.2 Å: 6QP6 in digitonin, Ca⁺²-free state, 3.8 Å: 6QPB	6QPC	Data File Jmol Viewer 6QPC 6QP6 6QPI 6QPB	Alvadia et al. (2019). Alvadia C, Lim NK, Clerico Mosina V, Oostergetel GT, Dutzler R, & Paulino C (2019). Cryo-EM structures and functional characterization of the murine lipid scramblase TMEM16F. Elife 8 :e44365. PubMed Id: 30785399. doi:10.7554/eLife.44365.
*TMEM16F scramblase & ion channel in digitonin with bound Ca²⁺: Mus musculus* E Eukaryota (expressed in HEK293), 3.47 Å** cryo-EM structure digitonin without bound Ca²⁺, 3.98 Å: 6P47 in nanodiscs with supplement of PIP2 in Cl1, 3.15 Å: 6P48 in nanodiscs with supplement of PIP2 in Cl2, 3.27 Å: 6P49	6P46	Data File Jmol Viewer 6P46 6P47 6P48 6P49	Feng et al. (2019). Feng S, Dang S, Han TW, Ye W, Jin P, Cheng T, Li J, Jan YN, Jan LY, & Cheng Y (2019). Cryo-EM Studies of TMEM16F Calcium-Activated Ion Channel Suggest Features Important for Lipid Scrambling. Cell Rep 28 2:567-579.e4. PubMed Id: 31291589. doi:10.1016/j.celrep.2019.06.023.
*TMEM16F scramblase & ion channel in digitonin, F518H mutant, Ca⁺²-free state: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.39 Å** cryo-EM structure Ca⁺²-bound state, 2.96 Å: 8B8J in lipid nanodiscs, Ca⁺²-bound state, 2.94 Å: 8B8Q in digitonin, N562A mutant, Ca⁺²-bound state, open/closed form, 3.49 Å: 8B8M in digitonin, N562A mutant, Ca⁺²-bound state, closed/closed form, 3.01 Å: 8B8K in digitonin, F518A and Q623A mutant, Ca⁺²-bound state, open/closed form, 3.09 Å: 8BC0 in digitonin, F518A and Q623A mutant, Ca⁺²-bound state, closed/closed form, 2.93 Å: 8BC1	8B8G	Data File Jmol Viewer 8B8G 8B8J 8B8K 8BC1 8BC0 8B8Q 8B8M	Arndt et al. (2022). Arndt M, Alvadia C, Straub MS, Clerico Mosina V, Paulino C, & Dutzler R (2022). Structural basis for the activation of the lipid scramblase TMEM16F. Nat Commun 13 1:6692. PubMed Id: 36335104. doi:10.1038/s41467-022-34497-x.
*TMEM16F scramblase & ion channel in complex with Ca²⁺ and PIP₂, no inhibitor: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure with bound inhibitor 1PBC, 3.12 Å: 8SUN with bound inhibitor niclosamide, 3.10 Å: 8SUR class 1, no inhibitor, 3.20 Å: 8TAL class 2, no inhibitor, 3.10 Å: 8TAI	8TAG	Data File Jmol Viewer 8TAG 8SUN 8TAI 8SUR 8TAL	Feng et al. (2023). Feng S, Puchades C, Ko J, Wu H, Chen Y, Figueroa EE, Gu S, Han TW, Ho B, Cheng T, Li J, Shoichet B, Jan YN, Cheng Y, & Jan LY (2023). Identification of a drug binding pocket in TMEM16F calcium-activated ion channel and lipid scramblase. Nat Commun 14 1:4874. PubMed Id: 37573365. doi:10.1038/s41467-023-40410-x.
*TMEM16K scramblase & ion channel in detergent, 2 mM Ca²⁺ closed form: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.47 Å** cryo-EM structure low Ca²⁺, closed form 4.2 Å: 6R7Y Ca²⁺-free, closed form 5.14 Å: 6R7Z crystal structure, 3.2 Å: 5OC9 crystal structure form 2, 3.5 Å: 6R65	6R7X	Data File Jmol Viewer 6R7X 6R65 5OC9 6R7Z 6R7Y	Bushell et al. (2019). Bushell SR, Pike ACW, Falzone ME, Rorsman NJG, Ta CM, Corey RA, Newport TD, Christianson JC, Scofano LF, Shintre CA, Tessitore A, Chu A, Wang Q, Shrestha L, Mukhopadhyay SMM, Love JD, Burgess-Brown NA, Sitsapesan R, Stansfeld PJ, Huiskonen JT, Tammaro P, Accardi A, & Carpenter EP (2019). The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K. Nat Commun 10 1. PubMed Id: 31477691. doi:10.1038/s41467-019-11753-1.
XKR Family of Proteins Kell blood group precursor proteins, often involved apoptotic lipid scrambling
*XKR9 lipid scramblase, full length with synthetic nanobody: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.66 Å** cryo-EM structure caspase-3 cleaved, 4.3 Å: 7P16	7P14	Data File Jmol Viewer 7P14 7P16	Straub et al. (2021). Straub MS, Alvadia C, Sawicka M, & Dutzler R (2021). Cryo-EM structures of the caspase-activated protein XKR9 involved in apoptotic lipid scrambling. Elife 10 :e69800. PubMed Id: 34263724. doi:10.7554/eLife.69800.
*Xkr8 scramblase in complex with basigin: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.80 Å** cryo-EM structure	7DCE	Data File Jmol Viewer 7DCE	Sakuragi et al. (2021). Sakuragi T, Kanai R, Tsutsumi A, Narita H, Onishi E, Nishino K, Miyazaki T, Baba T, Kosako H, Nakagawa A, Kikkawa M, Toyoshima C, & Nagata S (2021). The tertiary structure of the human Xkr8-Basigin complex that scrambles phospholipids at plasma membranes. Nat Struct Mol Biol 28 10:825-834. PubMed Id: 34625749. doi:10.1038/s41594-021-00665-8.
Sec, Translocase, and Insertase Proteins Membrane Proteins Involved with Protein Secretion and Insertion formerly listed as "Channels: Protein-Conducting"
*SecYEβ translocon: Methanococcus jannaschii* A Archaea, 3.5 Å** Coördinates of native complex: 1RHZ. Coördinates of double-mutant complex (K422R,V423T) 1RH5 (3.2 Å resolution).	1RHZ	Data File Jmol Viewer 1RHZ 1RH5 SecY complex, alpha subunit SecY complex, beta subunit SecY complex, gamma subunit	van den Berg et al. (2004). van den Berg B, Clemons WM, Collinson I, Hartmann E, Harrison SC, & Rapoport TA (2004). X-ray structure of a protein-conducting channel. Nature 427 :36-44. PubMed Id: 14661030.
*SecYEβ translocon with full-plug (TM2a) deletion: Methanococcus jannaschii* A Archaea, 3.6 Å** Coördinates of mutant with half-plug deletion 2YXQ (3.5 Å resolution).	2YXR	Data File Jmol Viewer 2YXR 2YXQ	Li et al. (2007). Li W, Schulman S, Boyd D, Erlandson K, Beckwith J & Rapoport TA (2007). The plug domain of the SecY protein stabilizes the closed state of the translocon channel and maintains a membrane seal. Mol Cell 26 :1409-38. PubMed Id: 17531810.
*SecYEβ "primed" translocon: Pyrococcus furiosus* A Archaea (expressed in E. coli), 3.1 Å**	3MP7	Data File Jmol Viewer 3MP7	Egea and Stroud (2010). Egea PF & Stroud RM (2010). Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes. Proc Natl Acad Sci USA 107 :17182-17187. PubMed Id: 20855604.
*SecYEG translocon in complex with SecA: Thermotoga maritima* B Bacteria (expressed in E. coli), 4.5 Å**	3DIN	Data File Jmol Viewer 3DIN	Zimmer et al. (2008). Zimmer J, Nam Y, & Rapoport TA (2008). Structure of a complex of the ATPase SecA and the protein-translocation channel. Nature 455 :936-943. PubMed Id: 18923516.
*SecYE translocon in complex with B. subtilis* SecA: Geobacillus thermodenitrificans B Bacteria (expressed in E. coli), 3.7 Å** An OmpA signal sequence is covalently inserted into SecA residue after residue 741. The insert carries a Cys residue that cross-links with a Cys residue in the so-called plug domain of SecY.	5EUL	Data File Jmol Viewer 5EUL	Li et al. (2016). Li L, Park E, Ling J, Ingram J, Ploegh H, & Rapoport TA (2016). Crystal structure of a substrate-engaged SecY protein-translocation channel. Nature 531 :395-399. PubMed Id: 26950603. doi:10.1038/nature17163.
*SecA-SecYE complex in nanodiscs, substrate-engaged: Geobacillus thermodenitrificans (SecYE) and Bacillus subtilis (SecA)* B Bacteria, 3.45 Å** cryo-EM structure	6ITC	Data File Jmol Viewer 6ITC	Ma et al. (2019). Ma C, Wu X, Sun D, Park E, Catipovic MA, Rapoport TA, Gao N, & Li L (2019). Structure of the substrate-engaged SecA-SecY protein translocation machine. Nat Commun 10 1. PubMed Id: 31253804. doi:10.1038/s41467-019-10918-2.
*SecA/SecYE/proOMPA(4Y)-sfGFP complex with bound ADP.BeF₃^-: Bacillus subtillis/Geobaccilus thermodentrificans* B Bacteria, 3.35 Å** cryo-EM structure with bound ADP, 3.33 Å: 7XHB	7XHA	Data File Jmol Viewer 7XHA 7XHB	Dong et al. (2023). Dong L, Yang S, Chen J, Wu X, Sun D, Song C, & Li L (2023). Structural basis of SecA-mediated protein translocation. Proc Natl Acad Sci U S A 120 2:e2208070120. PubMed Id: 36598944. doi:10.1073/pnas.2208070120.
*SecYEG translocon in lipid nanodiscs bound to a ribosome: Escherichia coli* B Bacteria, 6 Å** cryo-EM structure	6R7L	Data File Jmol Viewer 6R7L	Kater et al. (2019). Kater L, Frieg B, Berninghausen O, Gohlke H, Beckmann R, & Kedrov A (2019). Partially inserted nascent chain unzips the lateral gate of the Sec translocon. EMBO Rep. 20 10. PubMed Id: 31379073. doi:10.15252/embr.201948191.
*SecYE translocon in complex with a Fab fragment: Thermus thermophilus* B Bacteria (expressed in E. coli), 3.20 Å** SecYE alone 2ZQP (6.0 Å resolution).	2ZJS	Data File Jmol Viewer 2ZJS 2ZQP	Tsukazaki et al. (2008). Tsukazaki T, Mori H, Fukai S, Ishitani R, Mori T, Dohmae N, Perederina A, Sugita Y, Vassylyev DG, Ito K, & Nureki O (2008). Conformational transition of Sec machinery inferred from bacterial SecYE structures. Nature 455 :988-991. PubMed Id: 18923527.
*SecYEG translocon, I222 space group: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.72 Å** C222₁ space group, 3.64 Å: 5CH4	5AWW	Data File Jmol Viewer 5AWW 5CH4	Tanaka et al. (2015). Tanaka Y, Sugano Y, Takemoto M, Mori T, Furukawa A, Kusakizako T, Kumazaki K, Kashima A, Ishitani R, Sugita Y, Nureki O, & Tsukazaki T (2015). Crystal Structures of SecYEG in Lipidic Cubic Phase Elucidate a Precise Resting and a Peptide-Bound State. Cell Rep 13 :1561-1568. PubMed Id: 26586438. doi:10.1016/j.celrep.2015.10.025.
*Sec61 translocase opened by a signal sequence: Canis lupus familiaris* E Eukaryota, 3.6 Å** cryo-EM structure	3JC2	Data File Jmol Viewer 3JC2	Voorhees & Hegde (2016). Voorhees RM, & Hegde RS (2016). Structure of the Sec61 channel opened by a signal sequence. Science 351 :88-91. PubMed Id: 26721998. doi:10.1126/science.aad4992.
*Sec61 translocase in inhibited state: Canis lupus familiaris* E Eukaryota, 2.69 Å** cryo-EM structure	6Z3T	Data File Jmol Viewer 6Z3T	Gérard et al. (2020). Gérard SF, Hall BS, Zaki AM, Corfield KA, Mayerhofer PU, Costa C, Whelligan DK, Biggin PC, Simmonds RE, & Higgins MK (2020). Structure of the Inhibited State of the Sec Translocon. Mol Cell 79 3:406-415.e7. PubMed Id: 32692975. doi:10.1016/j.molcel.2020.06.013.
*Sec61 ribosome-associated translocon complex with 5 accessory factors: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.84 Å** cryo-EM structure	6W6L	Data File Jmol Viewer 6W6L	McGilvray et al. (2020). McGilvray PT, Anghel SA, Sundaram A, Zhong F, Trnka MJ, Fuller JR, Hu H, Burlingame AL, & Keenan RJ (2020). An ER translocon for multi-pass membrane protein biogenesis. Elife 9 :e56889. PubMed Id: 32820719. doi:10.7554/eLife.56889.
*Sec61 translocase, partially-open apo state (class 1): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.03 Å** cryo-EM structure partially open state (class 2), 3.40 Å: 8DNW in complex with inhibitor cotransin, 2.98 Å: 8DNX in complex with inhibitor decantransin, 2.85 Å: 8DNY in complex with inhibitor apratoxin F, 2.57 Å: 8DNZ in complex with inhibitor mycolatone, 2.86 Å: 8DO0 in complex with inhibitor ipomoeassin F, 3.01 Å: 8DO1 in complex with inhibitor cyclotriazadisulfonamide, 2.95 Å: 8DO2 in complex with inhibitor eeyarestatin I, 3.22 Å: 8DO3	8DNV	Data File Jmol Viewer 8DNV 8DO3 8DNX 8DNY 8DNZ 8DO0 8DNW 8DO1 8DO2	Itskanov et al. (2023). Itskanov S, Wang L, Junne T, Sherriff R, Xiao L, Blanchard N, Shi WQ, Forsyth C, Hoepfner D, Spiess M, & Park E (2023). A common mechanism of Sec61 translocon inhibition by small molecules. Nat Chem Biol 19 9:1063-1071. PubMed Id: 37169959. doi:10.1038/s41589-023-01337-y.
*80S ribosome stalled on a 2-TMD Rhodopsin intermediate in complex with the Sec61 translocon: Oryctolagus cuniculus* E Eukaryota (expressed in HEK293 cells), 3.25 Å** cryo-EM structure stalled on a 4-TMD Rhodopsin intermediate, 3.88 Å: 7TUT These important structures show that for multipass membrane proteins, the TM segments are inserted on the backside of Sec61 without passing through the Sec61 lateral gate.	7TM3	Data File Jmol Viewer 7TM3 7TUT	Smalinskaitė et al. (2022). Smalinskaitė L, Kim MK, Lewis AJO, Keenan RJ, & Hegde RS (2022). Mechanism of an intramembrane chaperone for multipass membrane proteins. Nature 611 7934:161-166. PubMed Id: 36261528. doi:10.1038/s41586-022-05336-2.
*Sec protein-translocation channel complex (Sec61-Sec63-Sec71-Sec72): Saccharomyces cerevisiae* E Eukaryota, 3.68 Å** cryo-EM structure	6N3Q	Data File Jmol Viewer 6N3Q	Itskanov & Park (2019). Itskanov S, & Park E (2019). Structure of the posttranslational Sec protein-translocation channel complex from yeast. Science 363 6422:84-87. PubMed Id: 30545845. doi:10.1126/science.aav6740.
*Sec protein-translocation channel complex (Sec61-Sec63-Sec71-Sec72): Saccharomyces cerevisiae* E Eukaryota, 4.1 Å** cryo-EM structure	6ND1	Data File Jmol Viewer 6ND1	Wu et al. (2019). Wu X, Cabanos C, & Rapoport TA (2019). Structure of the post-translational protein translocation machinery of the ER membrane. Nature 566 7742:136-139. PubMed Id: 30644436. doi:10.1038/s41586-018-0856-x.
*Sec protein-translocation channel complex (Sec61-Sec63-Sec71-Sec72) post-translational complex: Saccharomyces cerevisiae* E Eukaryota, 4.40 Å** cryo-EM structure x-ray: Sec62 cytoplasmic domain, 2.54 Å: 6ZZZ	7AFT	Data File Jmol Viewer 7AFT 6ZZZ	Weng et al. (2021). Weng TH, Steinchen W, Beatrix B, Berninghausen O, Becker T, Bange G, Cheng J, & Beckmann R (2021). Architecture of the active post-translational Sec translocon. EMBO J 40 3:e105643. PubMed Id: 33305433. doi:10.15252/embj.2020105643.
*Sec protein-translocation channel complexes. Wild-type Sec61 without Sec62: Saccharomyces cerevisiae* E Eukaryota, 3.10 Å** cryo-EM structure with Sec62, conformation 1 (C1), 3.20 Å: 7KAI with Sec62, conformation 2, 3.10 Å: 7KAJ Sec61 pore mutant without Sec62, 4.00 Å: 7KAO Sec61 pore mutant w. Sec62, conformation 1, 4.10 Å: 7KAP Sec61 pore mutant w. Sec62, conformation 2, 4.00 Å: 7KAQ Sec63 FN3 mutant, without Sec62, 4.00 Å: 7KAR Sec61 pore ring and Sec63 FN3 double mutant without Sec62, 4.40 Å: 7KAT Sec61 pore ring and Sec63 FN3 double mutant with Sec62, 4.00 Å: 7KAU Sec63 FN3 and residues 210-216 mutated, 3.80 Å: 7KB5	7KAH	Data File Jmol Viewer 7KAH 7KB5 7KAP 7KAU 7KAJ 7KAI 7KAR 7KAQ 7KAO 7KAT	Itskanov et al. (2021). Itskanov S, Kuo KM, Gumbart JC, & Park E (2021). Stepwise gating of the Sec61 protein-conducting channel by Sec63 and Sec62. Nat Struct Mol Biol 28 2:162-172. PubMed Id: 33398175. doi:10.1038/s41594-020-00541-x.
*Sec protein-translocation channel complexes. Sec61 wild-type without Sec62: Thermomyces lanuginosus* E Eukaryota (expressed in S. cerevisiae), 3.90 Å** cryo-EM structure wild-type Sec61 with Sec62, plug-open conformation, 4.00 Å: 7KAL wild-type Sec61 with Sec62, plug-closed conformation, 3.80 Å: 7KAM wild-type Sec61, Sec62-lacking mutant (Delta Sec62), 3.70 Å: 7KAN	7KAK	Data File Jmol Viewer 7KAK 7KAL 7KAM 7KAN	Itskanov et al. (2021). Itskanov S, Kuo KM, Gumbart JC, & Park E (2021). Stepwise gating of the Sec61 protein-conducting channel by Sec63 and Sec62. Nat Struct Mol Biol 28 2:162-172. PubMed Id: 33398175. doi:10.1038/s41594-020-00541-x.
*YidC_27-266 insertase: Bacillus halodurans* B Bacteria (expressed in E. coli), 2.40 Å** YidC_27-267, 3.20 Å: 3WO7	3WO6	Data File Jmol Viewer 3WO6 3WO7	Kumazaki et al. (2014). Kumazaki K, Chiba S, Takemoto M, Furukawa A, Nishiyama K, Sugano Y, Mori T, Dohmae N, Hirata K, Nakada-Nakura Y, Maturana AD, Tanaka Y, Mori H, Sugita Y, Arisaka F, Ito K, Ishitani R, Tsukazaki T, & Nureki O (2014). Structural basis of Sec-independent membrane protein insertion by YidC. Nature 509 :516-520. PubMed Id: 24739968. doi:10.1038/nature13167.
*YidC insertase, full length: Escherichia coli* B Bacteria, 3.20 Å**	3WVF	Data File Jmol Viewer 3WVF	Kumazaki et al. (2014). Kumazaki K, Kishimoto T, Furukawa A, Mori H, Tanaka Y, Dohmae N, Ishitani R, Tsukazaki T, & Nureki O (2014). Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase. Sci Rep 4 :7299. PubMed Id: 25466392. doi:10.1038/srep07299.
*YidC insertase, full length: Escherichia coli* B Bacteria, 2.8 Å**	6AL2	Data File Jmol Viewer 6AL2	Tanaka et al. (2018). Tanaka Y, Izumioka A, Abdul Hamid A, Fujii A, Haruyama T, Furukawa A, & Tsukazaki T (2018). 2.8-Å crystal structure of Escherichia coli YidC revealing all core regions, including flexible C2 loop. Biochem Biophys Res Commun 505 1:141-145. PubMed Id: 30241934. doi:10.1016/j.bbrc.2018.09.043.
*YidC insertase: Thermotoga maritima* B Bacteria (expressed in E. coli), 3.84 Å** Periplasmic domain alone, 2.52 Å: 5Y82	5Y83	Data File Jmol Viewer 5Y83 5Y82	Xin et al. (2018). Xin Y, Zhao Y, Zheng J, Zhou H, Zhang XC, Tian C, & Huang Y (2018). Structure of YidC from Thermotoga maritima and its implications for YidC-mediated membrane protein insertion. FASEB J 32 5:2411-2421. PubMed Id: 29295859. doi:10.1096/fj.201700893RR.
*YidC insertase with N-terminal amphipathic helix resolved: Thermotoga maritima* B Bacteria (expressed in E. coli), 3.40 Å**	6Y86	Data File Jmol Viewer 6Y86	Nass et al. (2022). Nass KJ, Ilie IM, Saller MJ, Driessen AJM, Caflisch A, Kammerer RA, & Li X (2022). The role of the N-terminal amphipathic helix in bacterial YidC: Insights from functional studies, the crystal structure and molecular dynamics simulations. Biochim Biophys Acta Biomembr 1864 3:18325. PubMed Id: 34871574. doi:10.1016/j.bbamem.2021.183825.
*WRB/CAML/TRC40 insertase: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 4.20 Å** cryo-EM structure	6SO5	Data File Jmol Viewer 6SO5	McDowell et al. (2020). McDowell MA, Heimes M, Fiorentino F, Mehmood S, Farkas Á, Coy-Vergara J, Wu D, Bolla JR, Schmid V, Heinze R, Wild K, Flemming D, Pfeffer S, Schwappach B, Robinson CV, & Sinning I (2020). Structural Basis of Tail-Anchored Membrane Protein Biogenesis by the GET Insertase Complex. Mol Cell 80 1:72-86.e7. PubMed Id: 32910895. doi:10.1016/j.molcel.2020.08.012.
*WRB/CAML/TRC40 (Get1/Get2/Get3) insertase: Homo sapiens* E Eukaryota (expressed in E. coli), 3.20 Å** cryo-EM structure with helix α3’ deletion of Get2, 4.20 Å: 8CR2	8CR1	Data File Jmol Viewer 8CR1 8CR2	McDowell et al. (2023). McDowell MA, Heimes M, Enkavi G, Farkas Á, Saar D, Wild K, Schwappach B, Vattulainen I, & Sinning I (2023). The GET insertase exhibits conformational plasticity and induces membrane thinning. Nat Commun 14 1:7355. PubMed Id: 37963916. doi:10.1038/s41467-023-42867-2.
*WRB/TRP40 (Get1-cytoplasmic domain/Get3) complex: Homo sapiens* E Eukaryota (expressed in E. coli), 2.80 Å** X-ray structure	8CQZ	Data File Jmol Viewer 8CQZ	McDowell et al. (2023). McDowell MA, Heimes M, Enkavi G, Farkas Á, Saar D, Wild K, Schwappach B, Vattulainen I, & Sinning I (2023). The GET insertase exhibits conformational plasticity and induces membrane thinning. Nat Commun 14 1:7355. PubMed Id: 37963916. doi:10.1038/s41467-023-42867-2.
*WRB/CAML/TRC40 (Get1/Get2/Get3) insertase in amphipol:: Chaetomium thermophilum* E Eukaryota (expressed in E. coli), 5.00 Å** cryo-EM structure in nanodisc, 4.70 Å: 8ODV	8ODU	Data File Jmol Viewer 8ODU 8ODV	McDowell et al. (2023). McDowell MA, Heimes M, Enkavi G, Farkas Á, Saar D, Wild K, Schwappach B, Vattulainen I, & Sinning I (2023). The GET insertase exhibits conformational plasticity and induces membrane thinning. Nat Commun 14 1:7355. PubMed Id: 37963916. doi:10.1038/s41467-023-42867-2.
*DUF106 YidC-like protein: Methanocaldococcus jannaschi* A Archaea (expressed in E. coli), 3.50 Å** This structure establishes the universality of the YidC/Oxa1/Alb3 family in the three domains of life	5C8J	Data File Jmol Viewer 5C8J	Borowska et al. (2015). Borowska MT, Dominik PK, Anghel SA, Kossiakoff AA, & Keenan RJ (2015). A YidC-like Protein in the Archaeal Plasma Membrane. Structure 23 :1715-1724. PubMed Id: 26256539. doi:10.1016/j.str.2015.06.025.
*SecDF protein-export enhancer: Thermus thermophilus* B Bacteria (expressed in E. coli), 3.30 Å** SecDF associates with SecYEG to enhance protein export using the transmembrane proton motive force (PMF). It is a member of the resistance nodulation and cell division (RND) superfamily. A related member of the RND superfamily is the AcrB multi-drug efflux transporter. P1 periplasmic domain, 2.6 Å: 3AQO P4 periplasmic domain, NMR structure: 2RRN	3AQP	Data File Jmol Viewer 3AQP 3AQO 2RRN	Tsukazaki et al. (2011). Tsukazaki T, Mori H, Echizen Y, Ishitani R, Fukai S, Tanaka T, Perederina A, Vassylyev DG, Kohno T, Maturana AD, Ito K, & Nureki O (2011). Structure and function of a membrane component SecDF that enhances protein export. Nature 474 :235-238. PubMed Id: 21562494. doi:10.1038/nature09980.
*SecDF protein-export enhancer in super-membrane-facing (Super F) form: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.8 Å**	5YHF	Data File Jmol Viewer 5YHF	Furukawa et al. (2018). Furukawa A, Nakayama S, Yoshikaie K, Tanaka Y, & Tsukazaki T (2018). Remote Coupled Drastic β-Barrel to β-Sheet Transition of the Protein Translocation Motor. Structure 26 :485-489.e2. PubMed Id: 29398525. doi:10.1016/j.str.2018.01.002.
*SecDF protein-export enhancer in I form, wild-type: Deinococcus radiodurans* B Bacteria (expressed in E. coli), 4.0 Å** S-S mutant (MolA, MolB), 2.75 Å: 5XAN S-S mutant (MolC), 2.61 Å: 5AXP	5XAM	Data File Jmol Viewer 5XAM 5XAN 5AXP	Furukawa et al. (2017). Furukawa A, Yoshikaie K, Mori T, Mori H, Morimoto YV, Sugano Y, Iwaki S, Minamino T, Sugita Y, Tanaka Y, & Tsukazaki T (2017). Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven Protein Secretion Motor SecDF. Cell Rep 19 5:895-901. PubMed Id: 28467902. doi:10.1016/j.celrep.2017.04.030.
*TatA twin-arginine translocase monomer: Bacillus subtilis* B Bacteria (expressed in E. coli), NMR structure** structure determined in DPC micelles	2L16	Data File Jmol Viewer 2L16	Hu et al. (2010). Hu Y, Zhao E, Li H, Xia B, & Jin C (2010). Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis. J Am Chem Soc 132 :15942-15944. PubMed Id: 20726548. doi:10.1021/ja1053785.
*TatA twin-arginine translocase, model of oligomeric complex: Escherichia coli* B Bacteria, NMR/Molecular Dynamics Model** TatA monomer, NMR Structure: 2LZR	2LZS	Data File Jmol Viewer 2LZS 2LZR	Rodriguez et al. (2013). Rodriguez F, Rouse SL, Tait CE, Harmer J, De Riso A, Timmel CR, Sansom MS, Berks BC, & Schnell JR (2013). Structural model for the protein-translocating element of the twin-arginine transport system. Proc Natl Acad Sci USA 110 :E1092-E1101. PubMed Id: 23471988. doi:10.1073/pnas.1219486110.
*TatC twin-arginine translocase receptor: Aquifex aeolicus* B Bacteria (expressed in E. coli), 3.50 Å** Crystallized using lauryl maltose neopentyl glycol (LMNG)	4B4A	Data File Jmol Viewer 4B4A	Rollauer et al. (2012). Rollauer SE, Tarry MJ, Graham JE, Jääskeläinen M, Jäger F, Johnson S, Krehenbrink M, Liu SM, Lukey MJ, Marcoux J, McDowell MA, Rodriguez F, Roversi P, Stansfeld PJ, Robinson CV, Sansom MS, Palmer T, Högbom M, Berks BC, & Lea SM (2012). Structure of the TatC core of the twin-arginine protein transport system. Nature 492 :210-214. PubMed Id: 23201679. doi:10.1038/nature11683.
*TatC twin-arginine translocase receptor: Aquifex aeolicus* B Bacteria (expressed in E. coli), 4.00 Å** Crystallized using DHCP Structure using DDM for crystallization, 6.80 Å: 4HTT	4HTS	Data File Jmol Viewer 4HTS 4HTT	Ramasamy et al. (2013). Ramasamy S, Abrol R, Suloway CJ, & Clemons WM Jr (2013). The Glove-like Structure of the Conserved Membrane Protein TatC Provides Insight into Signal Sequence Recognition in Twin-Arginine Translocation. Structure 21 :777-788. PubMed Id: 23583035. doi:10.1016/j.str.2013.03.004.
*ER-associated protein degradation (ERAD) protein. Hrd1 channel in complex with Hrd3: Saccharomyces cerevisiae* E Eukaryota, 4.1 Å** cryo-EM structure E3 ubiquitin-protein ligase component HRD3, 3.9 Å: 5V7V	5V6P	Data File Jmol Viewer 5V6P 5V7V	Schoebel et al. (2017). Schoebel S, Mi W, Stein A, Ovchinnikov S, Pavlovicz R, DiMaio F, Baker D, Chambers MG, Su H, Li D, Rapoport TA, & Liao M (2017). Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3. Nature 548 :352-355. PubMed Id: 28682307. doi:10.1038/nature23314.
*ER-associated protein degradation (ERAD) protein Hrd1 ubiquitin ligase complex: Saccharomyces cerevisiae* E Eukaryota, 4.30 Å** cryo-EM structure Hrd1-Usa1/Der1/Hrd3 complex of the expected topology, 4.30 Å: 6VJZ Hrd1-Usa1/Der1/Hrd3 of the flipped topology, 4.10 Å: 6VK0 Hrd1/Hrd3 part from Hrd1-Usa1/Der1/Hrd3 complex, 3.90 Å: 6VK1 Hrd3/Yos9 complex, 3.70 Å: 6VK3	6VJY	Data File Jmol Viewer 6VJY 6VJZ 6VK3 6VK1 6VK0	Wu et al. (2020). Wu X, Siggel M, Ovchinnikov S, Mi W, Svetlov V, Nudler E, Liao M, Hummer G, & Rapoport TA (2020). Structural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex. Science 368 6489. PubMed Id: 32327568. doi:10.1126/science.aaz2449.
*Derlin-1 ERAD retrotranslocation channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.80 Å** cryo-EM structure	7CZB	Data File Jmol Viewer 7CZB	Rao et al. (2021). Rao B, Li S, Yao D, Wang Q, Xia Y, Jia Y, Shen Y, & Cao Y (2021). The cryo-EM structure of an ERAD protein channel formed by tetrameric human Derlin-1. Sci Adv 7 10:eabe8591. PubMed Id: 33658201. doi:10.1126/sciadv.abe8591.
Plasmodium translocon of exported protein (PTEX) Core Complex in the Engaged (Extended) State: Plasmodium falciparum E Eukaryota, 4.16 Å cryo-EM structure in resetting (compact) state, 4.23 Å: 6E11	6E10	Data File Jmol Viewer 6E10 6E11	Ho et al. (2018). Ho CM, Beck JR, Lai M, Cui Y, Goldberg DE, Egea PF, & Zhou ZH (2018). Malaria parasite translocon structure and mechanism of effector export. Nature 561 7721:70-75. PubMed Id: 30150771. doi:10.1038/s41586-018-0469-4.
*ATG9A transmembrane protein of the core autophagy machinery, State A: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.80 Å** cryo-EM structure State B, 2.90 Å: 6WR4	6WQZ	Data File Jmol Viewer 6WQZ 6WR4	Guardia et al. (2020). Guardia CM, Tan XF, Lian T, Rana MS, Zhou W, Christenson ET, Lowry AJ, Faraldo-Gómez JD, Bonifacino JS, Jiang J, & Banerjee A (2020). Structure of Human ATG9A, the Only Transmembrane Protein of the Core Autophagy Machinery. Cell Rep 31 13:107837. PubMed Id: 32610138. doi:10.1016/j.celrep.2020.107837.
*ATG9A transmembrane protein of the core autophagy machinery in amphipols: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.40 Å** cryo-EM structure in nanodiscs, 3.40 Å: 7JLP in LMNG micelles, 4.00 Å: 7JLQ	7JLO	Data File Jmol Viewer 7JLO 7JLQ 7JLP	Maeda et al. (2020). Maeda S, Yamamoto H, Kinch LN, Garza CM, Takahashi S, Otomo C, Grishin NV, Forli S, Mizushima N, & Otomo T (2020). Structure, lipid scrambling activity and role in autophagosome formation of ATG9A. Nat Struct Mol Biol 27 12:1194-1201. PubMed Id: 33106659. doi:10.1038/s41594-020-00520-2.
*ATG9A transmembrane protein of the core autophagy machinery: Schizosaccharomyces pombe* E Eukaryota (expressed in Saccharomyces cerevisiae), 3.00 Å** cryo-EM structure	7D0I	Data File Jmol Viewer 7D0I	Matoba et al. (2020). Matoba K, Kotani T, Tsutsumi A, Tsuji T, Mori T, Noshiro D, Sugita Y, Nomura N, Iwata S, Ohsumi Y, Fujimoto T, Nakatogawa H, Kikkawa M, & Noda NN (2020). Atg9 is a lipid scramblase that mediates autophagosomal membrane expansion. Nat Struct Mol Biol 27 12:1185-1193. PubMed Id: 33106658. doi:10.1038/s41594-020-00518-w.
*ER membrane protein complex (EMC): Homo sapiens* E Eukaryota, 6.4 Å** cryo-EM structure x-ray structure of EMC2/EMC9 complex, 2.20 Å:	6Z3W	Data File Jmol Viewer 6Z3W	O'Donnell et al. (2020). O'Donnell JP, Phillips BP, Yagita Y, Juszkiewicz S, Wagner A, Malinverni D, Keenan RJ, Miller EA, & Hegde RS (2020). The architecture of EMC reveals a path for membrane protein insertion. Elife 9 :e57887. PubMed Id: 32459176. doi:10.7554/eLife.57887.
*ER membrane protein complex (EMC) in nanodiscs: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure	6WW7	Data File Jmol Viewer 6WW7	Pleiner et al. (2020). Pleiner T, Tomaleri GP, Januszyk K, Inglis AJ, Hazu M, & Voorhees RM (2020). Structural basis for membrane insertion by the human ER membrane protein complex. Science 369 6502:433-436. PubMed Id: 32439656. doi:10.1126/science.abb5008.
*ER membrane protein complex (EMC) in GDN detergent: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure in lipid nanodiscs, 3.39 Å: 7ADO	7ADP	Data File Jmol Viewer 7ADP 7ADO	Miller-Vedam et al. (2020). Miller-Vedam LE, Bräuning B, Popova KD, Schirle Oakdale NT, Bonnar JL, Prabu JR, Boydston EA, Sevillano N, Shurtleff MJ, Stroud RM, Craik CS, Schulman BA, Frost A, & Weissman JS (2020). Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients. Elife 9 :e62611. PubMed Id: 33236988. doi:10.7554/eLife.62611.
*ER membrane protein complex (EMC) in complex with Ca_V1.2 and Ca_Vβ₃: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure	8EOI	Data File Jmol Viewer 8EOI	Chen et al. (2023). Chen Z, Mondal A, Abderemane-Ali F, Jang S, Niranjan S, Montaño JL, Zaro BW, & Minor DL Jr (2023). EMC chaperone-Ca_V structure reveals an ion channel assembly intermediate. Nature 619 7969:410-419. PubMed Id: 37196677. doi:10.1038/s41586-023-06175-5.
*ER membrane protein complex (EMC): Saccharomyces cerevisiae* E Eukaryota, 3.00 Å** cryo-EM structure	6WB9	Data File Jmol Viewer 6WB9	Bai et al. (2020). Bai L, You Q, Feng X, Kovach A, & Li H (2020). Structure of the ER membrane complex, a transmembrane-domain insertase. Nature 584 7821:475-478. PubMed Id: 32494008. doi:10.1038/s41586-020-2389-3.
*ER membrane protein complex (EMC) in DDM detergent: Saccharomyces cerevisiae* E Eukaryota, 4.30 Å** cryo-EM structure complex in lipid nanodiscs, 3.20 Å: 7KRA	7KTX	Data File Jmol Viewer 7KTX 7KRA	Miller-Vedam et al. (2020). Miller-Vedam LE, Bräuning B, Popova KD, Schirle Oakdale NT, Bonnar JL, Prabu JR, Boydston EA, Sevillano N, Shurtleff MJ, Stroud RM, Craik CS, Schulman BA, Frost A, & Weissman JS (2020). Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients. Elife 9 :e62611. PubMed Id: 33236988. doi:10.7554/eLife.62611.
*TIM22 complex from mitochondrial inner membrane: Saccharomyces cerevisiae* E Eukaryota, 3.83 Å** cryo-EM structure	6LO8	Data File Jmol Viewer 6LO8	Zhang et al. (2020). Zhang Y, Ou X, Wang X, Sun D, Zhou X, Wu X, Li Q, & Li L (2020). Structure of the mitochondrial TIM22 complex from yeast. Cell Res . PubMed Id: 32918038. doi:10.1038/s41422-020-00399-0.
*TIM22 complex from mitochondrial inner membrane: Homo sapiens* E Eukaryota, 3.70 Å** cryo-EM structure	7CGP	Data File Jmol Viewer 7CGP	Qi et al. (2020). Qi L, Wang Q, Guan Z, Wu Y, Shen C, Hong S, Cao J, Zhang X, Yan C, & Yin P (2020). Cryo-EM structure of the human mitochondrial translocase TIM22 complex. Cell Res . PubMed Id: 32901109. doi:10.1038/s41422-020-00400-w.
Channels: Mechanosensitive
*MscL Mechanosensitive channel: Mycobacterium tuberculosis* B Bacteria, 3.5 Å** This structure supersedes 1MSL.	2OAR	Data File Jmol Viewer 2OAR MscL mechanosensor channel monomer	Chang et al. (1998). Chang G, Spencer RH, Lee AT, Barclay MT, & Rees DC (1998). Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel. Science 282 :2220-2226. PubMed Id: 9856938.
*MscL Mechanosensitive channel, Δ95-120: Staphylococcus aureus* B Bacteria, 3.8 Å** Shows MscL in an expanded intermediate state.	3HZQ	Data File Jmol Viewer 3HZQ	Liu et al. (2009). Liu Z, Gandhi CS, & Rees DC (2009). Structure of a tetrameric MscL in an expanded intermediate state. Nature 461 :120-124. PubMed Id: 19701184.
*MscL mechanosensitive channel in closed state: Methanosarcina acetivorans* A Archaea (expressed in E. coli), 3.5 Å** expanded intermediate state, 4.1 Å: 4Y7J	4Y7K	Data File Jmol Viewer 4Y7K 4Y7J	Li et al. (2015). Li J, Guo J, Ou X, Zhang M, Li Y, & Liu Z (2015). Mechanical coupling of the multiple structural elements of the large-conductance mechanosensitive channel during expansion. Proc Natl Acad Sci USA 112 :10726-10731. PubMed Id: 26261325. doi:10.1073/pnas.1503202112.
*MscS voltage-modulated mechanosensitive channel: Escherichia coli* B Bacteria, 3.70 Å** This structure supersedes 1MXM.	2OAU	Data File Jmol Viewer 2OAU MscS mechanosensor channel monomer	Bass et al. (2002). Bass RB, Strop P, Barclay M, & Rees DC (2002). Crystal Structure of Escherichia coli MscS, a Voltage-modulated and mechanosensitive channel. Science 298 :1582-1587. PubMed Id: 12446901.
*MscS mechanosensitive channel in the open form: Escherichia coli* B Bacteria, 3.45 Å**	2VV5	Data File Jmol Viewer 2VV5	Wang et al. (2008). Wang W, Black SS, Edwards MD, Miller S, Morrison EL, Bartlett W, Dong C, Naismith JH, & Booth IR (2008). The structure of an open form of an E. coli mechanosensitive channel at 3.45 Å resolution. Science 321 :1179-1183. PubMed Id: 18755969.
*MscS voltage-modulated mechanosensitive channel, D67R1 mutant: Escherichia coli* B Bacteria, 2.99 Å**	5AJI	Data File Jmol Viewer 5AJI	Pliotas et al. (2015). Pliotas C, Dahl AC, Rasmussen T, Mahendran KR, Smith TK, Marius P, Gault J, Banda T, Rasmussen A, Miller S, Robinson CV, Bayley H, Sansom MS, Booth IR, & Naismith JH (2015). The role of lipids in mechanosensation. Nat Struct Mol Biol 22 :991-998. PubMed Id: 26551077. doi:10.1038/nsmb.3120.
*MscS mechanosensitive channel embedded in nanodiscs: Escherichia coli* B Bacteria, 2.9 Å** cryo-EM structure	6RLD	Data File Jmol Viewer 6RLD	Rasmussen et al. (2019). Rasmussen T, Flegler VJ, Rasmussen A, & Böttcher B (2019). Structure of the Mechanosensitive Channel MscS Embedded in the Membrane Bilayer. J Mol Biol 431 17:3081-3090. PubMed Id: 31291591. doi:10.1016/j.jmb.2019.07.006.
*MscS mechanosensitive channel with His-tag embedded in nanodiscs: Escherichia coli* B Bacteria, 3.1 Å** cryo-EM structure in nanodiscs without His-tag, 4.1 Å: 6PWP in dodecylmaltoside, 3.4Å: 6PWO	6PWN	Data File Jmol Viewer 6PWN 6PWO 6PWP	Reddy et al. (2019). Reddy B, Bavi N, Lu A, Park Y, & Perozo E (2019). Molecular basis of force-from-lipids gating in the mechanosensitive channel MscS. Elife 8 . PubMed Id: 31880537. doi:10.7554/eLife.50486.
*MscS voltage-modulated mechanosensitive channel in peptidiscs: Escherichia coli* B Bacteria, 3.3 Å** cryo-EM structure	6UZH	Data File Jmol Viewer 6UZH	Angiulli et al. (2020). Angiulli G, Dhupar HS, Suzuki H, Wason IS, Duong Van Hoa F, & Walz T (2020). New approach for membrane protein reconstitution into peptidiscs and basis for their adaptability to different proteins. Elife 9 :e53530. PubMed Id: 32125274. doi:10.7554/eLife.53530.
*MscS voltage-modulated mechanosensitive channel in PC-18:1 nanodiscs: Escherichia coli* B Bacteria, 3.20 Å** cryo-EM structure in PC-10 nanodiscs, 3.40 Å: 6VYL in PC-18:1 nanodiscs treated with beta-cyclodextran, 3.70 Å: 6VYM	6VYK	Data File Jmol Viewer 6VYK 6VYM 6VYL	Zhang et al. (2021). Zhang Y, Daday C, Gu RX, Cox CD, Martinac B, de Groot BL, & Walz T (2021). Visualization of the mechanosensitive ion channel MscS under membrane tension. Nature 590 7846:509-514. PubMed Id: 33568813. doi:10.1038/s41586-021-03196-w.
*MscS voltage-modulated mechanosensitive channel, DDM-solubilized, closed conformation: Escherichia coli* B Bacteria, 3.90 Å** cryo-EM structure DDM-solubilized, open conformation, 3.10 Å: 7OO0 DDM-solubilized, closed conformation with added lipid, 3.10 Å: 7OO6 LMNG-solubilized, open conformation, 2.30 Å: 7ONJ LMNG-solubilized, open conformation with added lipid, 2.70 Å: 7OOA LMNG-solubilized, closed conformation with added lipid, 3.70 Å: 7OO8	7ONL	Data File Jmol Viewer 7ONL 7OOA 7OO0 7ONJ 7OO6 7OO8	Flegler et al. (2021). Flegler VJ, Rasmussen A, Borbil K, Boten L, Chen HA, Deinlein H, Halang J, Hellmanzik K, Löffler J, Schmidt V, Makbul C, Kraft C, Hedrich R, Rasmussen T, & Böttcher B (2021). Mechanosensitive channel gating by delipidation. Proc Natl Acad Sci U S A 118 33:e2107095118. PubMed Id: 34376558. doi:10.1073/pnas.2107095118.
*MSL1 MscS voltage-modulated mechanosensitive channel homolog in nanodiscs: Arabidopsis thaliana* E Eukaryota (expressed in P. pastoris), 3.39 Å** cryo-EM structure in detergents, 3.06 Å: 6VXM A320V mutant in detergents, 2.96 Å: 6VXN	6VXP	Data File Jmol Viewer 6VXP 6VXN 6VXM	Deng et al. (2020). Deng Z, Maksaev G, Schlegel AM, Zhang J, Rau M, Fitzpatrick JAJ, Haswell ES, & Yuan P (2020). Structural mechanism for gating of a eukaryotic mechanosensitive channel of small conductance. Nat Commun 11 1. PubMed Id: 32704140. doi:10.1038/s41467-020-17538-1.
*MSL1 MscS voltage-modulated mechanosensitive channel homolog: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	6LYP	Data File Jmol Viewer 6LYP	Li et al. (2020). Li Y, Hu Y, Wang J, Liu X, Zhang W, & Sun L (2020). Structural Insights into a Plant Mechanosensitive Ion Channel MSL1. Cell Rep 30 13:4518-4527.e3. PubMed Id: 32234484. doi:10.1016/j.celrep.2020.03.026.
*Piezo1 mechanosensitive channel by cryo-EM: Mus musculus* E Eukaryota (expressed in HEK293 cells), 4.8 Å** C-terminal extracellular domain by x-ray, 1.45 Å: 4RAX	3JAC	Data File Jmol Viewer 3JAC 4RAX	Ge et al. (2015). Ge J, Li W, Zhao Q, Li N, Chen M, Zhi P, Li R, Gao N, Xiao B, & Yang M (2015). Architecture of the mammalian mechanosensitive Piezo1 channel. Nature 527 7576:64-69. PubMed Id: 26390154. doi:10.1038/nature15247.
*Piezo1 mechanosensitive channel, closed state: Mus musculus* E Eukaryota (expressed in expressed in HEK293 cells), 3.8 Å** cryo-EM structure	6B3R	Data File Jmol Viewer 6B3R	Guo & MacKinnon (2017). Guo YR, & MacKinnon R (2017). Structure-based membrane dome mechanism for Piezo mechanosensitivity. Elife 6 :e33660. PubMed Id: 29231809. doi:10.7554/eLife.33660.
*Piezo1 mechanosensitive channel, closed state: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.8 Å** cryo-EM structure	6BPZ	Data File Jmol Viewer 6BPZ	Saotome et al. (2018). Saotome K, Murthy SE, Kefauver JM, Whitwam T, Patapoutian A, & Ward AB (2018). Structure of the mechanically activated ion channel Piezo1. Nature 554 :481-486. PubMed Id: 29261642. doi:10.1038/nature25453.
*Piezo1 mechanosensitive channel, closed state: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.97 Å** cryo-EM structure	5Z10	Data File Jmol Viewer 5Z10	Zhao et al. (2018). Zhao Q, Zhou H, Chi S, Wang Y, Wang J, Geng J, Wu K, Liu W, Zhang T, Dong MQ, Wang J, Li X, & Xiao B (2018). Structure and mechanogating mechanism of the Piezo1 channel. Nature 554 :487-492. PubMed Id: 29469092. doi:10.1038/nature25743.
*Piezo1 mechanosensitive channel: Piezo 1.1 isoform: Mus musculus* E Eukaryota (expressed in HEK293 cells), 4.50 Å** cryo-EM structure	6LQI	Data File Jmol Viewer 6LQI	Geng et al. (2020). Geng J, Liu W, Zhou H, Zhang T, Wang L, Zhang M, Li Y, Shen B, Li X, & Xiao B (2020). A Plug-and-Latch Mechanism for Gating the Mechanosensitive Piezo Channel. Neuron 106 3:438-451.e6. PubMed Id: 32142647. doi:10.1016/j.neuron.2020.02.010.
*Piezo1 mechanosensitive channel in a lipid bilayer, curved structure: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.46 Å** cryo-EM structure Flattened Structure, 6.81 Å 7WLU	7WLT	Data File Jmol Viewer 7WLT 7WLU	Yang et al. (2022). Yang X, Lin C, Chen X, Li S, Li X, & Xiao B (2022). Structure deformation and curvature sensing of PIEZO1 in lipid membranes. Nature 604 7905:377-383. PubMed Id: 35388220. doi:10.1038/s41586-022-04574-8.
*Piezo1 mechanosensitive channel in complex with MyoD family inhibitor MDFIC, composite map: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.66 Å** cryo-EM structure	8IMZ	Data File Jmol Viewer 8IMZ	Zhou et al. (2023). Zhou Z, Ma X, Lin Y, Cheng D, Bavi N, Secker GA, Li JV, Janbandhu V, Sutton DL, Scott HS, Yao M, Harvey RP, Harvey NL, Corry B, Zhang Y, & Cox CD (2023). MyoD-family inhibitor proteins act as auxiliary subunits of Piezo channels. Science 381 6659:799-804. PubMed Id: 37590348. doi:10.1126/science.adh8190.
*Piezo2 mechanosensitive channel, closed state: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.8 Å** cryo-EM structure	6KG7	Data File Jmol Viewer 6KG7	Wang et al. (2019). Wang L, Zhou H, Zhang M, Liu W, Deng T, Zhao Q, Li Y, Lei J, Li X, & Xiao B (2019). Structure and mechanogating of the mammalian tactile channel PIEZO2. Nature 573 7773:225-229. PubMed Id: 31435011. doi:10.1038/s41586-019-1505-8.
*Hyperosmolality-gated calcium-permeable channel (OSCA) 1.1: Arabidopsis thaliana* E Eukaryota (expressed in sf9 cells), 3.5 Å** (The original PDB code for this structure, 5YD1, is obsolete.) cryo-EM structure The original PDB code for this structure, 5YD1, is obsolete. OSCA 3.1, 4.8 Å: 5Z1F	6JPF	Data File Jmol Viewer 6JPF 5Z1F	Zhang et al. (2018). Zhang M, Wang D, Kang Y, Wu JX, Yao F, Pan C, Yan Z, Song C, & Chen L (2018). Structure of the mechanosensitive OSCA channels. Nat Struct Mol Biol 25 9:850-858. PubMed Id: 30190597. doi:10.1038/s41594-018-0117-6.
*Hyperosmolality-gated calcium-permeable channel (OSCA) 1.1, extended state: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 2.50 Å** cryo-EM structure	8GRN	Data File Jmol Viewer 8GRN	Zhang et al. (2023). Zhang M, Shan Y, Cox CD, & Pei D (2023). A mechanical-coupling mechanism in OSCA/TMEM63 channel mechanosensitivity. Nat Commun 14 1:3943. PubMed Id: 37402734. doi:10.1038/s41467-023-39688-8.
*Mechanically-activated ion channel OSCA 1.2 in nanodiscs: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 3.1 Å** cryo-EM structure in LMNG detergent micelles, 3.5 Å: 6MGW	6MGV	Data File Jmol Viewer 6MGV 6MGW	Jojoa-Cruz et al. (2018). Jojoa-Cruz S, Saotome K, Murthy SE, Tsui CCA, Sansom MS, Patapoutian A, & Ward AB (2018). Cryo-EM structure of the mechanically activated ion channel OSCA1.2. Elife 7 :e41845. PubMed Id: 30382939. doi:10.7554/eLife.41845.
*Mechanically-activated ion channel OSCA 1.2 in peptidiscs: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 2.80 Å** cryo-EM structure	8T56	Data File Jmol Viewer 8T56	Jojoa-Cruz et al. (2024). Jojoa-Cruz S, Burendei B, Lee WH, & Ward AB (2024). Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain. Structure 32 2:157-167.e5. PubMed Id: 38103547. doi:10.1016/j.str.2023.11.009.
*Mechanically-activated ion channel OSCA 1.2 in liposome, inside-in open state: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 3.29 Å** cryo-EM structure inside-out closed state, 3.56 Å: 8XNG in DOPC detergent (1:20), contracted state 1, 3.23 Å: 8XS4 in DOPC detergent (1:20), contracted state 2, 3.33 Å: 8XS5 in DOPC detergent (1:20), expanded state, 3.32 Å: 8XVX in DOPC detergent (1:50), contracted state, 3.59 Å: 8XW2 in DOPC detergent (1:50), expanded state, 3.63 Å: 8XW3 V335W mutant in DDM detergent, 4.49 Å: 8XW1	8XAJ	Data File Jmol Viewer 8XAJ 8XS4 8XW2 8XW1 8XW3 8XVX 8XS5 8XNG	Han et al. (2024). Han Y, Zhou Z, Jin R, Dai F, Ge Y, Ju X, Ma X, He S, Yuan L, Wang Y, Yang W, Yue X, Chen Z, Sun Y, Corry B, Cox CD, & Zhang Y (2024). Mechanical activation opens a lipid-lined pore in OSCA ion channels. Nature . PubMed Id: 38570680. doi:10.1038/s41586-024-07256-9.
*Mechanically-activated ion channel OSCA 1.2: Oryza sativa* E Eukaryota (expressed in P. pastoris), 4.9 Å** cryo-EM structure	6OCE	Data File Jmol Viewer 6OCE	Maity et al. (2019). Maity K, Heumann JM, McGrath AP, Kopcho NJ, Hsu PK, Lee CW, Mapes JH, Garza D, Krishnan S, Morgan GP, Hendargo KJ, Klose T, Rees SD, Medrano-Soto A, Saier MH Jr, Piñeros M, Komives EA, Schroeder JI, Chang G, & Stowell MHB (2019). Cryo-EM structure of OSCA1.2 from Oryza sativa elucidates the mechanical basis of potential membrane hyperosmolality gating. Proc Natl Acad Sci USA 116 28:14309-14318. PubMed Id: 31227607. doi:10.1073/pnas.1900774116.
*Mechanically-activated ion channel OSCA 2.3 in peptidiscs: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 2.70 Å** cryo-EM structure	8T57	Data File Jmol Viewer 8T57	Jojoa-Cruz et al. (2024). Jojoa-Cruz S, Burendei B, Lee WH, & Ward AB (2024). Structure of mechanically activated ion channel OSCA2.3 reveals mobile elements in the transmembrane domain. Structure 32 2:157-167.e5. PubMed Id: 38103547. doi:10.1016/j.str.2023.11.009.
*Hyperosmolality-gated calcium-permeable channel (OSCA) 3.1, contracted state: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure extended state, 3.30 Å: 8GSO	8GRO	Data File Jmol Viewer 8GRO 8GSO	Zhang et al. (2023). Zhang M, Shan Y, & Pei D (2023). Mechanism underlying delayed rectifying in human voltage-mediated activation Eag2 channel. Nat Commun 14 1:1470. PubMed Id: 36928654. doi:10.1038/s41467-023-37204-6.
*Mechanically-activated ion channel OSCA 3.1, Y367N/G454S/Y458I mutant, open/open state: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 3.84 Å** cryo-EM structure open/desensitized state, 3.89 Å: 8XS0 R611E/R619E mutant, closed/open state, 3.71 Å: 8XVY R611E/R619E mutant, closed/desensitized state, 3.78 Å: 8XVZ WT, in GDN detergent, 3.11 Å: 8XW0	8XRY	Data File Jmol Viewer 8XRY 8XS0 8XW0 8XVY 8XVZ	Han et al. (2024). Han Y, Zhou Z, Jin R, Dai F, Ge Y, Ju X, Ma X, He S, Yuan L, Wang Y, Yang W, Yue X, Chen Z, Sun Y, Corry B, Cox CD, & Zhang Y (2024). Mechanical activation opens a lipid-lined pore in OSCA ion channels. Nature . PubMed Id: 38570680. doi:10.1038/s41586-024-07256-9.
*Hypo-osmolality-gated calcium-permeable channel TMEM63A: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	8GRS	Data File Jmol Viewer 8GRS	Zhang et al. (2023). Zhang M, Shan Y, Cox CD, & Pei D (2023). A mechanical-coupling mechanism in OSCA/TMEM63 channel mechanosensitivity. Nat Commun 14 1:3943. PubMed Id: 37402734. doi:10.1038/s41467-023-39688-8.
*Hypo-osmolality-gated calcium-permeable channel TMEM63B in digitonin detergent: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.84 Å** cryo-EM structure	8XW4	Data File Jmol Viewer 8XW4	Han et al. (2024). Han Y, Zhou Z, Jin R, Dai F, Ge Y, Ju X, Ma X, He S, Yuan L, Wang Y, Yang W, Yue X, Chen Z, Sun Y, Corry B, Cox CD, & Zhang Y (2024). Mechanical activation opens a lipid-lined pore in OSCA ion channels. Nature . PubMed Id: 38570680. doi:10.1038/s41586-024-07256-9.
*Hypo-osmolality-gated calcium-permeable channel TMEM63C: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.56 Å**	8K0B	Data File Jmol Viewer 8K0B	Qin et al. (2023). Qin Y, Yu D, Wu D, Dong J, Li WT, Ye C, Cheung KC, Zhang Y, Xu Y, Wang Y, Shi YS, & Dang S (2023). Cryo-EM structure of TMEM63C suggests it functions as a monomer. Nat Commun 14 1:7265. PubMed Id: 37945568. doi:10.1038/s41467-023-42956-2.
*Mechanosensitive Ion Channel Flycatcher1 in GDN, composite model: Dionaea muscipula* E Eukaryota (expressed in HEK293 cells), 2.80 Å** cryo-EM structure Flycatcher1 in GDN, 2.80 Å 7N5E Protomer in 'Down' conformation in GDN, 2.70 Å 7N5F Protomer in 'Up' conformation in GDN, 2.40 Å 7N5G	7N5D	Data File Jmol Viewer 7N5D 7N5E 7N5F 7N5G	Jojoa-Cruz et al. (2022). Jojoa-Cruz S, Saotome K, Tsui CCA, Lee WH, Sansom MSP, Murthy SE, Patapoutian A, & Ward AB (2022). Structural insights into the Venus flytrap mechanosensitive ion channel Flycatcher1. Nat Commun 13 1:850. PubMed Id: 35165281. doi:10.1038/s41467-022-28511-5.
*Ynal Mechanosensitive channel in amphipols: Escherichia coli* B Bacteria, 3.80 Å** cryo-EM structure	5Y4O	Data File Jmol Viewer 5Y4O	Yu et al. (2018). Yu J, Zhang B, Zhang Y, Xu CQ, Zhuo W, Ge J, Li J, Gao N, Li Y, & Yang M (2018). A binding-block ion selective mechanism revealed by a Na/K selective channel. Protein Cell 9 7:629-639. PubMed Id: 28921397. doi:10.1007/s13238-017-0465-8.
*Ynal Mechanosensitive channel using SMA2000: Escherichia coli* B Bacteria, 2.40 Å** cryo-EM structure	7N4T	Data File Jmol Viewer 7N4T	Catalano et al. (2021). Catalano C, Ben-Hail D, Qiu W, Blount P, des Georges A, & Guo Y (2021). Cryo-EM Structure of Mechanosensitive Channel YnaI Using SMA2000: Challenges and Opportunities. Membranes (Basel) 11 11:849. PubMed Id: 34832078. doi:10.3390/membranes11110849.
*Transmembrane channel-like protein 1 (TMC-1) complex. Expanded conformation: Caenorhabditis elegans* E Eukaryota, 3.10 Å** cryo-EM structure contracted conformation, 3.09 Å: 7USX complex with ARRD-6, 3.54 Å: 7USY	7USW	Data File Jmol Viewer 7USW 7USX 7USY	Jeong et al. (2022). Jeong H, Clark S, Goehring A, Dehghani-Ghahnaviyeh S, Rasouli A, Tajkhorshid E, & Gouaux E (2022). Structures of the TMC-1 complex illuminate mechanosensory transduction. Nature 610 7933:796-803. PubMed Id: 36224384. doi:10.1038/s41586-022-05314-8.
*MscK mechanosenstive ion channel, G924S mutant in a closed conformation: Escherichia coli* B Bacteria (expressed in Komagataella pastoris), 3.84 Å** cryo-EM structure Open Conformation, 3.48 Å: 7UX1	7UW5	Data File Jmol Viewer 7UW5 7UX1	Mount et al. (2022). Mount J, Maksaev G, Summers BT, Fitzpatrick JAJ, & Yuan P (2022). Structural basis for mechanotransduction in a potassium-dependent mechanosensitive ion channel. Nat Commun 13 1:6904. PubMed Id: 36371466. doi:10.1038/s41467-022-34737-0.
Channels: Potassium, Sodium, & Proton Ion-Selective
*KcsA Potassium channel, H⁺ gated: Streptomyces lividans* B Bacteria (expressed in E. coli), 3.2 Å**	1BL8	Data File Jmol Viewer 1BL8 KcsA potassium channel	Doyle et al. (1998). Doyle DA, Cabral JM, Pfuetzner RA, Kuo AL, Gulbis JM, Cohen SL, Chait BT, & MacKinnon R (1998). The structure of the potassium channel: Molecular basis of K⁺conduction and selectivity. Science 280 :69-77. PubMed Id: 9525859.
*KcsA Potassium channel, H⁺ gated. Complexed with Fab.: Streptomyces lividans* B Bacteria (expressed in E. coli), 2.0 Å** R-free = 0.233. 1K4D, 2.3 Å, R-free = 0.235	1K4C	Data File Jmol Viewer 1K4C 1K4D	Zhou et al. (2001). Zhou Y, Morais-Cabral JH, Kaufman A, & MacKinnon R (2001). Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 Å. Nature 414 :43-48. PubMed Id: 11689936.
*Full-length KcsA Potassium channel, H⁺ gated: Streptomyces lividans* B Bacteria (expressed in E. coli), NMR structure**	1F6G	Data File Jmol Viewer 1F6G	Cortes et al. (2001). Cortes DM, Cuello LG, & Perozo E (2001). Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating. J Gen Physiol 117 2:165-180. PubMed Id: 11158168. doi:10.1085/jgp.117.2.165.
*KcsA Potassium channel, H⁺ gated. Complexed with Fab, Tl, & Tetrabutylammonium (TBA): Streptomyces lividans* B Bacteria (expressed in E. coli), 2.76 Å** In complex with tetraethylarsonium (TEAS) rather than TBA, 3.01 Å: 2BOC	2BOB	Data File Jmol Viewer 2BOB 2BOC	Lenaeus et al. (2005). Lenaeus MJ, Vamvouka M, Focia PJ, & Gross A (2005). Structural basis of TEA blockade in a model potassium channel. Nat Struc Mol Biol 12 :454-459. PubMed Id: 15852022.
*KcsA-Fab complex in NaCl: Streptomyces lividans* B Bacteria (expressed in E. coli), 3.20 Å** In BaCl₂, 2.70 Å: 2ITD KcsA, M96V mutant in KCl, 2.52 Å: 2NLJ	2ITC	Data File Jmol Viewer 2ITC 2ITD 2NLJ	Lockless et al. (2007). Lockless SW, Zhou M, & MacKinnon R (2007). Structural and thermodynamic properties of selective ion binding in a K⁺ channel. PLoS Biol 5 :e121. PubMed Id: 17472437. doi:10.1371/journal.pbio.0050121.
*Full-length KcsA Potassium channel, H⁺ gated: Streptomyces lividans* B Bacteria (expressed in E. coli), 3.80 Å** Crystallized with synthetic Fab2 antibodies. C-terminal domain alone (residues 129-158) crystallized with synthetic Fab4 antibodies 3EFD, 2.60 Å	3EFF	Data File Jmol Viewer 3EFF 3EFD	Uysal et al. (2009). Uysal S, Vásquez V, Tereshko V, Esaki K, Fellouse FA, Sidhu SS, Koide S, Perozo E, & Kossiakoff A (2009). Crystal structure of full-length KcsA in its closed conformation. Proc Natl Acad Sci USA 106 :6644-6649. PubMed Id: 19346472.
*Full-length KcsA Potassium channel, H⁺ gated: Streptomyces lividans* B Bacteria (expressed in E. coli), 3.80 Å** Open conformation of the full-length channel. Reveals that the activation gate expands about 20 Å	3PJS	Data File Jmol Viewer 3PJS	Uysal et al. (2011). Uysal S, Cuello LG, Cortes DM, Koide S, Kossiakoff AA, & Perozo E (2011). Mechanism of activation gating in the full-length KcsA K⁺ channel. Proc Natl Acad Sci USA 108 :11896-11899. PubMed Id: 21730186. doi:10.1073/pnas.1105112108.
*KcsA Potassium channel in the presence of 150 mM Li⁺ and 3 mM K⁺: Streptomyces lividans* B Bacteria (expressed in E. coli), 2.75 Å** KcsA in the presence of 150 mM Li⁺ and 0 mM K⁺, 2.85 Å: 3GB7	3IGA	Data File Jmol Viewer 3IGA 3GB7	Thompson et al. (2009). Thompson AN, Kim I, Panosian TD, Iverson TM, Allen TW, & Nimigean CM (2009). Mechanism of potassium-channel selectivity revealed by Na⁺and L⁺binding sites within the KcsA pore. Nat Struct Mol Biol 16 :1321-1324. PubMed Id: 19946269.
*KcsA Potassium channel in the open inactivated state. Open 32 Å conformer: Streptomyces lividans* B Bacteria (expressed in E. coli), 3.30 Å** Open 23 Å conformer, 3.20 Å: 3F7V Open 17 Å conformer, 3.40 Å: 3F7Y Open 16 Å conformer, 3.00 Å: 3FB6 Open 14.5 Å conformer, 2.80 Å: 3FB5	3F5W	Data File Jmol Viewer 3F5W 3FB5 3F7V 3FB6 3F7Y	Cuello et al. (2010). Cuello LG, Jogini V, Cortes DM, & Perozo E (2010). Structural mechanism of C-type inactivation in K⁺channels. Nature 466 :203-208. PubMed Id: 20613835.
*KcsA Potassium channel E71H-F103A inactivated-state mutant (closed state): Streptomyces lividans* B Bacteria (expressed in E. coli), 3.20 Å** KcsA open-state in the presence of Rb⁺, 3.30 Å: 3FB7	3HPL	Data File Jmol Viewer 3HPL 3FB7	Cuello et al. (2010). Cuello LG, Jogini V, Cortes DM, Pan AC, Gagnon DG, Dalmas O, Cordero-Morales JF, Chakrapani S, Roux B, & Perozo E (2010). Structural basis for the coupling between activation and inactivation gates in K⁺channels. Nature 466 :272-275. PubMed Id: 20613845.
*KcsA Potassium channel E71I modal-gating mutant: Streptomyces lividans* B Bacteria (expressed in E. coli), 2.30 Å** E71Q mutant, 2.70 Å: 3OR6	3OR7	Data File Jmol Viewer 3OR7 3OR6	Chakrapani et al. (2011). Chakrapani S, Cordero-Morales JF, Jogini V, Pan AC, Cortes DM, Roux B, & Perozo E (2011). On the structural basis of modal gating behavior in K⁺channels. Nat Struct Mol Biol 18 :67-74. PubMed Id: 21186363.
*KcsA Y82C with bound Cadmium : Streptomyces lividans* B Bacteria (expressed in E. coli), 2.40 Å** with nitroxide spin label, 2.50 Å: 3STZ	3STL	Data File Jmol Viewer 3STL 3STZ	Raghuraman et al. (2012). Raghuraman H, Cordero-Morales JF, Jogini V, Pan AC, Kollewe A, Roux B, & Perozo E (2012). Mechanism of Cd²⁺ Coordination during Slow Inactivation in Potassium Channels. Structure 20 :1332-1342. PubMed Id: 22771214. doi:10.1016/j.str.2012.03.027.
*KcsA Potassium channel Y78 ester mutant in high K⁺: Streptomyces lividans* B Bacteria (expressed in E. coli + semi-synthesis), 2.06 Å**	4MSW	Data File Jmol Viewer 4MSW	Matulef et al. (2013). Matulef K, Komarov AG, Costantino CA, & Valiyaveetil FI (2013). Using protein backbone mutagenesis to dissect the link between ion occupancy and C-type inactivation in K⁺ channels. Proc Natl Acad Sci USA 110 44:17886-17891. PubMed Id: 24128761. doi:10.1073/pnas.1314356110.
*KcsA Potassium channel, H⁺ gated in KCl. Complexed with Fab & Tetrabutylammonium (TBA): Streptomyces lividans* B Bacteria (expressed in E. coli), 2.40 Å** In complex with tetrahexylammonium, 2.40 Å: 4UUJ In complex with tetraoctylammonium, 2.40 Å: 2W0F	2JK5	Data File Jmol Viewer 2JK5 4UUJ 2W0F	Lenaeus et al. (2014). Lenaeus MJ, Burdette D, Wagner T, Focia PJ, & Gross A (2014). Structures of KcsA in Complex with Symmetrical Quaternary Ammonium Compounds Reveal a Hydrophobic Binding Site. Biochemistry 53 :5365-5373. PubMed Id: 25093676. doi:10.1021/bi500525s.
*KcsA Potassium channel, V76ester mutation: Streptomyces lividans* B Bacteria (expressed in E. coli + semi-synthesis), 2.75 Å** V76ester + G77dA, 2.3 Å: 5EC2 G77ester mutation, 2.3 Å: 5EBW T75G (conductive state), 2.3 Å: 5EBL T75G (non-conductive state), 2.5 Å: 5EBM	5EC1	Data File Jmol Viewer 5EC1 5EBL 5EC2 5EBW 5EBM	Matulef et al. (2016). Matulef K, Annen AW, Nix JC, & Valiyaveetil FI (2016). Individual Ion Binding Sites in the K⁺ Channel Play Distinct Roles in C-type Inactivation and in Recovery from Inactivation. Structure 24 :750-761. PubMed Id: 27150040. doi:10.1016/j.str.2016.02.021.
*KcsA Potassium channel, open-conformation, E71A mutant: Streptomyces lividans* B Bacteria (expressed in E. coli), 2.25 Å** deep-inactivated open conformation (Y82A mutant), 2.37 Å: 5VKE closed conformation (Y82A-F103A mutant), 2.25 Å: 5VKH	5VK6	Data File Jmol Viewer 5VK6 5VKE 5VKH	Cuello et al. (2017). Cuello LG, Cortes DM, & Perozo E (2017). The gating cycle of a K⁺ channel at atomic resolution. Elife 6 :e28032. PubMed Id: 29165243. doi:10.7554/eLife.28032.
*KcsA Potassium channel, H⁺ gated. G77A mutant; 2,4-ion bound configuration: Streptomyces lividans* B Bacteria (expressed in E. coli), 2.09 Å** G77C mutant; the 2,4-ion bound configuration, 2.13 Å: 6NFV G77A mutant in NaCl, 2.05 Å: 6PA0	6NFU	Data File Jmol Viewer 6NFU 6NFV 6PA0	Tilegenova et al. (2019). Tilegenova C, Cortes DM, Jahovic N, Hardy E, Hariharan P, Guan L, & Cuello LG (2019). Structure, function, and ion-binding properties of a K⁺ channel stabilized in the 2,4-ion-bound configuration. Proc Natl Acad Sci USA 116 34:16829-16834. PubMed Id: 31387976. doi:10.1073/pnas.1901888116.
*KcsA Potassium channel, open state. Barium blocked. 1 mM BaCl₂: Streptomyces lividans* (expressed in E. coli), 3.24 Å** open state, 2 mM BaCl₂, 3.60 Å: 6W0B open state, 4 mM BaCl₂, 3.60 Å: 6W0C open state, 5 mM BaCl₂, 3.64 Å: 6W0D open state, 10 BaCl₂, 3.51 Å: 6W0E closed state, 5mM BaCl₂, 2.40 Å: 6W0F closed state, 1 mM KCl, 5mM BaCl₂, 2.60 Å: 6W0G closed state, 5mM KCl, 5mM BaCl₂, 2.40 Å: 6W0H closed state, 10mM KCl, 5mM BaCl₂, 2.33 Å: 6W0I closed state incubated in BaCl₂ & NaCl, 2.50 Å: 6W0J	6W0A	Data File Jmol Viewer 6W0A 6W0G 6W0D 6W0F 6W0J 6W0I 6W0C 6W0H 6W0B 6W0E	Rohaim et al. (2020). Rohaim A, Gong L, Li J, Rui H, Blachowicz L, & Roux B (2020). Open and Closed Structures of a Barium-Blocked Potassium Channel. J Mol Biol 432 17:4783-4798. PubMed Id: 32615129. doi:10.1016/j.jmb.2020.06.012.
*KcsA Potassium channel, W67F mutant+TBA+Fab, pre-open: Streptomyces lividans* B Bacteria (expressed in E. coli), 2.64 Å** W67F+Fab, open, 2.69 Å 7M2I Wild-Type + Fab, 3.20 Å 7M2J	7M2H	Data File Jmol Viewer 7M2H 7M2I 7M2J	Reddi et al. (2021). Reddi R, Matulef K, Riederer E, Moenne-Loccoz P, & Valiyaveetil FI (2021). Structures of Gating Intermediates in a K⁺ channel. J Mol Biol 433 23:167296. PubMed Id: 34627789. doi:10.1016/j.jmb.2021.167296.
*KcsA E71V mutant, closed gate with K⁺: Streptomyces lividans* B Bacteria (expressed in E. coli), 2.77 Å** closed gate with Ba²⁺, 2.85 Å 7MHX with Barium, 7MJT with sodium, 3.10 Å 7MK6 in Potassium, 3.00 Å 7MUB	7MHR	Data File Jmol Viewer 7MHR 7MHX 7MUB 7MK6 7MJT	Rohaim et al. (2022). Rohaim A, Vermeulen BJA, Li J, Kümmerer F, Napoli F, Blachowicz L, Medeiros-Silva J, Roux B, & Weingarth M (2022). A distinct mechanism of C-type inactivation in the Kv-like KcsA mutant E71V. Nat Commun 13 1:1574. PubMed Id: 35322021. doi:10.1038/s41467-022-28866-9.
*KcsA Potassium channel, H⁺ gated. T75A mutant, closed and deep-inactivated conformation.: Streptomyces coelicolor* B Bacteria (expressed in E. coli), 2.35 Å** Open and conductive conformation, 2.37 Å: 6BY3	6BY2	Data File Jmol Viewer 6BY2 6BY3	Labro et al. (2018). Labro AJ, Cortes DM, Tilegenova C, & Cuello LG (2018). Inverted allosteric coupling between activation and inactivation gates in K⁺ channels. Proc Natl Acad Sci USA 115 21:5426-5431. PubMed Id: 29735651. doi:10.1073/pnas.1800559115.
*Two-Pore Domain Potassium Channel K_2P1.1 (TWIK-1): Homo sapiens* E Eukaryota (expressed in Pichia pastoris), 3.40 Å** The protein is a homodimer. It is sensitive to temperature, pH, and membrane stretch. The channel becomes permeable to Na⁺ during hypokalemia.	3UKM	Data File Jmol Viewer 3UKM	Miller & Long (2012). Miller AN & Long SB (2012). Crystal structure of the human two-pore domain potassium channel K2P1. Science 335 :432-436. PubMed Id: 22282804. doi:10.1126/science.121327.
*Two-Pore Domain Potassium Channel K_2P1.1 (TWIK-1) in MSP1D1 lipid nanodisc, pH 7.4: Rattus norvegicus* E Eukaryota (expressed in Komagataella pastoris), 3.33 Å** cryo-EM structure in MSP1E3D1 Lipid Nanodisc at pH 5.5, 3.43 Å: 7SK1	7SK0	Data File Jmol Viewer 7SK0 7SK1	Turney et al. (2022). Turney TS, Li V, & Brohawn SG (2022). Structural Basis for pH-gating of the K+ channel TWIK1 at the selectivity filter. Nat Commun 13 1:3232. PubMed Id: 35680900. doi:10.1038/s41467-022-30853-z.
*Two-Pore Domain Potassium Channel K_2P3.1 (TASK-1), closed conformation: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å** closed conformation with a bound inhibitor BAY 1000493, 2.90 Å: 6RV3 closed conformation with a bound inhibitor BAY 2341237, 3.10 Å: 6RV4	6RV2	Data File Jmol Viewer 6RV2 6RV3 6RV4	Rödström et al. (2020). Rödström KEJ, Kiper AK, Zhang W, Rinné S, Pike ACW, Goldstein M, Conrad LJ, Delbeck M, Hahn MG, Meier H, Platzk M, Quigley A, Speedman D, Shrestha L, Mukhopadhyay SMM, Burgess-Brown NA, Tucker SJ, M¨ller T, Decher N, & Carpenter EP (2020). A lower X-gate in TASK channels traps inhibitors within the vestibule. Nature :443-447. PubMed Id: 32499642. doi:10.1038/s41586-020-2250-8.
*Two-Pore Domain Potassium Channel K_2P5 (TASK2) in nanodisc at pH 6.5: Mus musculus* E Eukaryota (expressed in Komagataella pastoris), 3.45 Å** cryo-EM structure pH 8.5, 3.52 Å: 6WM0	6WLV	Data File Jmol Viewer 6WLV 6WM0	Li et al. (2020). Li B, Rietmeijer RA, & Brohawn SG (2020). Structural basis for pH gating of the two-pore domain K⁺ channel TASK2. Nature 586 7829:457-462. PubMed Id: 32999458. doi:10.1038/s41586-020-2770-2.
*Two-Pore Domain Potassium Channel K_2P4.1 (TRAAK): Homo sapiens* E Eukaryota (expressed in Pichia pastoris), 3.80 Å** The protein is a homodimer. This channel is sensitive to temperature, pH, voltage, lipid interactions, and membrane stretch.	3UM7	Data File Jmol Viewer 3UM7	Brohawn et al. (2012). Brohawn SG, del Mármol J, & MacKinnon R (2012). Crystal structure of the human K2P TRAAK, a lipid- and mechano-sensitive K⁺ ion channel. Science 335 :436-441. PubMed Id: 22282805. doi:10.1126/science.1213808.
*Two-Pore Domain Potassium Channel K_2P4.1 (TRAAK): Homo sapiens* E Eukaryota (expressed in Pichia pastoris), 2.75 Å** This structure reveals a domain-swapped chain connectivity enabled by the helical cap that exchanges two opposing outer helices 180° around the channel.	4I9W	Data File Jmol Viewer 4I9W	Brohawn et al. (2013). Brohawn SG, Campbell EB, & Mackinnon R (2013). Domain-swapped chain connectivity and gated membrane access in a Fab-mediated crystal of the human TRAAK K⁺ channel. Proc Natl Acad Sci USA 110 :2129-2134. PubMed Id: 23341632. doi:10.1073/pnas.1218950110.
*Two-Pore Domain Potassium Channel K_2P4.1 (TRAAK) in non-conductive state in the presence of K⁺: Homo sapiens* E Eukaryota (expressed in Pichia pastoris), 2.50 Å** Non-conductive state in the presence of Tl⁺, 3.01 Å: 4WFH Conductive state in the presence of K⁺, 2.50 Å: 4WFE Conductive state in the presence of Tl⁺, 3.00 Å: 4WFG	4WFF	Data File Jmol Viewer 4WFF 4WFG 4WFH 4WFE	Brohawn et al. (2014). Brohawn SG, Campbell EB, & MacKinnon R (2014). Physical mechanism for gating and mechanosensitivity of the human TRAAK K⁺ channel. Nature 516 7529:126-130. PubMed Id: 25471887. doi:10.1038/nature14013.
*Two-Pore Domain Potassium Channel K_2P4.1 (TRAAK), G124I mutant: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 3.30 Å** W262S mutant, 3.40 Å: 4RUF	4RUE	Data File Jmol Viewer 4RUE 4RUF	Lolicato et al. (2014). Lolicato M, Riegelhaupt PM, Arrigoni C, Clark KA, & Minor DL Jr (2014). Transmembrane helix straightening and buckling underlies activation of mechanosensitive and thermosensitive K_2P channels. Neuron 84 6:1198-1212. PubMed Id: 25500157. doi:10.1016/j.neuron.2014.11.017.
*Two-Pore Domain Potassium Channel K_2P4.1 (TRAAK); FHIEG mutant A198E, conductive K⁺ bound state: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 2.26 Å** Tl⁺ bound conductive conformation, 2.77 Å 7LJA FHEIG mutant A270P in a K⁺ bound conductive conformation, 2.78 Å 7LJ4 G158D imutant in a K⁺ bound conductive conformation, 2.97 Å 7LJB	7LJ5	Data File Jmol Viewer 7LJ5 7LJB 7LJA 7LJ4	Rietmeijer et al. (2021). Rietmeijer RA, Sorum B, Li B, & Brohawn SG (2021). Physical basis for distinct basal and mechanically gated activity of the human K⁺ channel TRAAK. Neuron 109 18:2902-2913.e4. PubMed Id: 34390650. doi:10.1016/j.neuron.2021.07.009.
*Two-Pore Domain Potassium Channel K_2P4.1 (TRAAK) in complex with 1B10 Fab: Mus musculus* E Eukaryota (expressed in Komagataella pastoris), 2.77 Å**	6PIS	Data File Jmol Viewer 6PIS	Brohawn et al. (2019). Brohawn SG, Wang W, Handler A, Campbell EB, Schwarz JR, & MacKinnon R (2019). The mechanosensitive ion channel TRAAK is localized to the mammalian node of Ranvier. Elife 8 . PubMed Id: 31674909. doi:10.7554/eLife.50403.
*Two-Pore Domain Potassium Channel K_2P2.1 (TREK-1), apo structure: Mus musculus* E Eukaryota (expressed in Komagataella pastoris), 3.1 Å** ML335 complex, 3.0 Å: 6CQ8 ML402 complex, 2.8 Å: 6CQ9 Former PDB codes: 5VK5, 5VKN, & 5VKP replaced by 6CQ6, 6CQ8, & 6CQ9, repectively.	6CQ6	Data File Jmol Viewer 6CQ6 6CQ8 6CQ9	Lolicato et al. (2017). Lolicato M, Arrigoni C, Mori T, Sekioka Y, Bryant C, Clark KA, & Minor DL Jr (2017). K2P2.1 (TREK-1)-activator complexes reveal a cryptic selectivity filter binding site. Nature 7663:364-368. PubMed Id: 28693035. doi:10.1038/nature22988.
*K_2P 2.1(TREK-1), I110D mutant, apo channel structure: Mus musculus* E Eukaryota (expressed in Komagataella pastoris), 3.40 Å** RuR bound channel structure, 3.40 Å: 6V3I RuR:ML335 bound channel structure, 2.80 Å: 6V37 Ru360 bound channel structure, 3.51 Å: 6V3C	6V36	Data File Jmol Viewer 6V36 6V3C 6V3I 6V37	Pope et al. (2020). Pope L, Lolicato M, & Minor DL Jr (2020). Polynuclear Ruthenium Amines Inhibit K_2P Channels via a "Finger in the Dam" Mechanism. Cell Chem Biol 27 5:511-524.e4. PubMed Id: 32059793. doi:10.1016/j.chembiol.2020.01.011.
*Two-Pore Domain Potassium Channel K_2P2.1 (TREK-1), 0 mM K⁺: Mus musculus* E Eukaryota (expressed in Komagataella pastoris), 3.88 Å** 1 mM K⁺, 3.40 Å: 6W7C 10 mM K⁺, 3.50 Å: 6W7D 30 mM K⁺, 3.29 Å: 6W7E 50 mM K⁺, 3.60 Å: 6W82 100 mM K⁺, 3.90 Å: 6W83 200 mM K⁺, 3.70 Å: 6W84 In complex with ML335: 0 mM K⁺, 3.40 Å: 6W8F 1 mM K⁺, 2.60 Å: 6W8C 10 mM K⁺, 3.00 Å: 6W8A 30 mM K⁺, 3.20 Å: 6W88 50 mM K⁺, 3.20 Å: 6W87 100 mM K⁺, 3.30 Å: 6W86 200 mM K⁺, 3.80 Å: 6W85	6W7B	Data File Jmol Viewer 6W7B 6W85 6W7E 6W84 6W88 6W8A 6W87 6W7D 6W8C 6W8F 6W82 6W83 6W7C 6W86	Lolicato et al. (2020). Lolicato M, Natale AM, Abderemane-Ali F, Crottès D, Capponi S, Duman R, Wagner A, Rosenberg JM, Grabe M, & Minor DL Jr (2020). K_2P channel C-type gating involves asymmetric selectivity filter order-disorder transitions. Sci Adv 6 44. PubMed Id: 33127683. doi:10.1126/sciadv.abc9174.
*Two-Pore Domain Potassium Channel K_2P10.1 (TREK-2), up state: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.20 Å** down state, 3.80 Å: 4XDJ in complex with Br-fluoxetine, 3.50 Å: 4XDL in complex with norfluoxetine, 3.60 Å: 4XDK	4BW5	Data File Jmol Viewer 4BW5 4XDK 4XDJ 4XDL	Dong et al. (2015). Dong YY, Pike AC, Mackenzie A, McClenaghan C, Aryal P, Dong L, Quigley A, Grieben M, Goubin S, Mukhopadhyay S, Ruda GF, Clausen MV, Cao L, Brennan PE, Burgess-Brown NA, Sansom MS, Tucker SJ, & Carpenter EP (2015). K2P channel gating mechanisms revealed by structures of TREK-2 and a complex with Prozac. Science 347 6227:1256-1259. PubMed Id: 25766236. doi:10.1126/science.1261512.
*Two-pore channel TPC1: Arabidopsis thaliana* E Eukaryota (expressed in S. cerevisiae), 2.87 Å**	5DQQ	Data File Jmol Viewer 5DQQ	Kintzer & Stroud (2016). Kintzer AF, & Stroud RM (2016). Structure, inhibition and regulation of two-pore channel TPC1 from Arabidopsis thaliana. Nature 531 :258-262. PubMed Id: 26961658. doi:10.1038/nature17194.
*Two-pore channel TPC1: Arabidopsis thaliana* E Eukaryota (expressed in Komagataella pastoris), 3.31 Å**	5E1J	Data File Jmol Viewer 5E1J	Guo et al. (2016). Guo J, Zeng W, Chen Q, Lee C, Chen L, Yang Y, Cang C, Ren D, & Jiang Y (2016). Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana. Nature 531 :196-201. PubMed Id: 26689363. doi:10.1038/nature16446.
*Two-pore channel TPC1 mutant, Na⁺ selective: Arabidopsis thaliana* E Eukaryota (expressed in Komagataella pastoris), 3.3 Å**	5TUA	Data File Jmol Viewer 5TUA	Guo et al. (2017). Guo J, Zeng W, & Jiang Y (2017). Tuning the ion selectivity of two-pore channels. Proc Natl Acad Sci USA 114 :1009-1014. PubMed Id: 28096396. doi:10.1073/pnas.1616191114.
*Two-pore channel TPC1 without Ca²⁺-chelating amino acids reconstituted in saposin A: Arabidopsis thaliana* E Eukaryota (expressed in S. cerevisiae), 3.3 Å** cryo-EM structure removal of chelating amino acids: D240N, D545N, & E528Q (termed TPC1_DDE) with cat06 Fab, 3.3 Å: 6E1K in state 1, 3.7 Å: 6E1N in state 2, 3.7 Å: 6E1P	6E1M	Data File Jmol Viewer 6E1M 6E1K 6E1P 6E1N	Kintzer et al. (2018). Kintzer AF, Green EM, Dominik PK, Bridges M, Armache JP, Deneka D, Kim SS, Hubbell W, Kossiakoff AA, Cheng Y, & Stroud RM (2018). Structural basis for activation of voltage sensor domains in an ion channel TPC1. Proc Natl Acad Sci USA 115 39:E9095-E9104. PubMed Id: 30190435. doi:10.1073/pnas.1805651115.
*Two-pore channel TPC1 D454N mutant with 1 mM EDTA state I: Arabidopsis thaliana* E Eukaryota (expressed in Saccharomyces cerevisiae), 2.70 Å** cryo-EM structure with 1mM Ca²⁺, 2.50 Å 7TBG EDTA state II, 3.50 Å: 7TDD DDE mutant, 3.20 Å: 7TDE	7TDF	Data File Jmol Viewer 7TDF 7TDE 7TBG 7TDD	Dickinson et al. (2022). Dickinson MS, Lu J, Gupta M, Marten I, Hedrich R, & Stroud RM (2022). Molecular basis of multistep voltage activation in plant two-pore channel 1. Proc Natl Acad Sci U S A 119 9:e2110936119. PubMed Id: 35210362. doi:10.1073/pnas.2110936119.
*Two-pore channel TPC1 with 1mM Ca²⁺: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure with 50mM Ca²⁺, 3.10 Å 7FHL D240A/D454A/E528A mutant with 1mM Ca²⁺, 3.30 Å 7FHN D240A/D454A/E528A mutant with 50mM Ca²⁺, 2.80 Å 7FHO	7FHK	Data File Jmol Viewer 7FHK 7FHN 7FHO 7FHL	Ye et al. (2021). Ye F, Xu L, Li X, Zeng W, Gan N, Zhao C, Yang W, Jiang Y, & Guo J (2021). Voltage-gating and cytosolic Ca²⁺ activation mechanisms of Arabidopsis two-pore channel AtTPC1. Proc Natl Acad Sci U S A 118 49:e2113946118. PubMed Id: 34845029. doi:10.1073/pnas.2113946118.
*Two-pore channel TPC1 with bound PtdIns(3,5)P₂: Mus musculus* E Eukaryota (expressed in HEK293F cells), 3.2 Å** cryo-EM structure apo protein, 3.4 Å: 6C96	6C9A	Data File Jmol Viewer 6C9A 6C96	She et al. (2018). She J, Guo J, Chen Q, Zeng W, Jiang Y, & Bai XC (2018). Structural insights into the voltage and phospholipid activation of the mammalian TPC1 channel. Nature 556 7699:130-134. PubMed Id: 29562233. doi:10.1038/nature26139.
*Two-pore channel TPC2, apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.5 Å** cryo-EM structure ligand-bound closed state, 3.4 Å: 6NQ2 ligand-bound open state, 3.7 Å: 6NQ0	6NQ1	Data File Jmol Viewer 6NQ1 6NQ2 6NQ0	She et al. (2019). She J, Zeng W, Guo J, Chen Q, Bai XC, & Jiang Y (2019). Structural mechanisms of phospholipid activation of the human TPC2 channel. Elife 8 . PubMed Id: 30860481. doi:10.7554/eLife.45222.
*Two-pore channel TPC3 in resting state: Danio rerio* E Eukaryota (expressed in HEK293 cells), 3.11 Å** cryo-EM structure	6V1Q	Data File Jmol Viewer 6V1Q	Dickinson et al. (2020). Dickinson MS, Myasnikov A, Eriksen J, Poweleit N, & Stroud RM (2020). Resting state structure of the hyperdepolarization activated two-pore channel 3. Proc Natl Acad Sci USA 117 4:1988-1993. PubMed Id: 31924746. doi:10.1073/pnas.1915144117.
*KvAP Voltage-gated potassium Channel in complex with Fab: Aeropyrum pernix* A Archaea (expressed in E. coli), 3.2 Å** Voltage sensor domain, 1.9 Å: 1ORS	1ORQ	Data File Jmol Viewer 1ORQ 1ORS KvAP potassium channel	Jiang et al. (2003). Jiang Y, Lee A, Chen J, Ruta V, Cadene M, Chait BT, & MacKinnon R (2003). X-ray structure of a voltage-dependent K⁺channel. Nature 423 :33-41. PubMed Id: 12721618. Crystal structures. See also: Jiang et al. (2003). Jiang Y, Ruta V, Chen J, Lee A, & MacKinnon R (2003). The principle of gating charge movement in a voltage-dependent K+ channel. Nature 423 :42-48. PubMed Id: 12721619. Voltage sensor mechanism.
*KvAP Voltage-gated potassium Channel in complex with Fv fragments: Aeropyrum pernix* A Archaea (expressed in E. coli), 3.9 Å**	2A0L	Data File Jmol Viewer 2A0L	Lee et al. (2005). Lee SY, Lee A, Chen J, & MacKinnon R (2005). Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane. Proc Natl Acad Sci USA 102 :15441-15446. PubMed Id: 16223877.
*KvAP Voltage-Sensing Domain in phospholipid micelles: Aeropyrum pernix* A Archaea (expressed in E. coli), NMR Structure**	2KYH	Data File Jmol Viewer 2KYH	Butterwick & MacKinnon (2010). Butterwick JA & MacKinnon R (2010). Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP. J Mol Biol 403 :591-606. PubMed Id: 20851706.
*KvAP Voltage-gated potassium Channel: Aeropyrum pernix* B Bacteria (expressed in E. coli), 5.9 Å** cryo-EM structure	6UWM	Data File Jmol Viewer 6UWM	Tao & MacKinnon (2019). Tao X, & MacKinnon R (2019). Cryo-EM structure of the KvAP channel reveals a non-domain-swapped voltage sensor topology. Elife 8 :e52164. PubMed Id: 31755864. doi:10.7554/eLife.52164.
*Shaker Kv channel: Drosophila melanogaster* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure W434F mutant, 2.90 Å 7SJ1	7SIP	Data File Jmol Viewer 7SIP 7SJ1	Tan et al. (2022). Tan XF, Bae C, Stix R, Fernández-Mariño AI, Huffer K, Chang TH, Jiang J, Faraldo-Gómez JD, & Swartz KJ (2022). Structure of the Shaker Kv channel and mechanism of slow C-type inactivation. Sci Adv 8 11. PubMed Id: 35302848. doi:10.1126/sciadv.abm7814.
*Shaker Kv channel in low K⁺: Drosophila melanogaster* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure	8TEO	Data File Jmol Viewer 8TEO	Stix et al. (2023). Stix R, Tan XF, Bae C, Fernández-Mariño AI, Swartz KJ, & Faraldo-Gómez JD (2023). Eukaryotic Kv channel Shaker inactivates through selectivity filter dilation rather than collapse. Sci Adv 9 49:eadj5539. PubMed Id: 38064553. doi:10.1126/sciadv.adj5539.
*Kv1.2 Voltage-gated potassium Channel: Rattus norvegicus* E Eukaryota (expressed in Pichia pastoris), 2.9 Å**	2A79	Data File Jmol Viewer 2A79	Long et al. (2005). Long SB, Campbell EB, & Mackinnon R (2005). Crystal Structure of a Mammalian Voltage-Dependent Shaker Family K+ Channel. Science 309 :897-903. PubMed Id: 16002581. See also: Long et al. (2005). Long SB, Campbell EB, & Mackinnon R (2005). Voltage Sensor of Kv1.2: Structural Basis of Electromechanical Coupling. Science 309 :903-908. PubMed Id: 16002579.
*Kv1.2 Voltage-gated potassium Channel (full length): Rattus norvegicus* E Eukaryota (expressed in Pichia pastoris), 2.9 Å** Re-refinement of 2A79 above using normal-mode x-ray crystallographic refinement	3LUT	Data File Jmol Viewer 3LUT	Chen et al. (2010). Chen X, Wang Q, Ni F, & Ma J (2010). Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement. Proc Natl Acad Sci USA 107 :11352-11357. PubMed Id: 20534430.
*Kv1.2 Voltage-gated potassium Channel, C-type inactivation: Rattus norvegicus* E Eukaryota (expressed in Komagataella pastoris), 3.10 Å** Kv 1.2 chimera-3m, 3.32 Å 7SIT	7SIZ	Data File Jmol Viewer 7SIZ 7SIT	Reddi et al. (2022). Reddi R, Matulef K, Riederer EA, Whorton MR, & Valiyaveetil FI (2022). Structural basis for C-type inactivation in a Shaker family voltage-gated K⁺ channel. Sci Adv 8 16:eabm8804. PubMed Id: 35452285. doi:10.1126/sciadv.abm8804.
*Kv1.2/Kv2.1 Voltage-gated potassium channel chimera: Rattus norvegicus* E Eukaryota (expressed in Pichia pastoris), 2.4 Å** First Kv channel with resolved lipids.	2R9R	Data File Jmol Viewer 2R9R	Long et al. (2007). Long SB, Tao X, Campbell EB, & Mackinnon R (2007). Atomic structure of a voltage-dependent K⁺channel in a lipid membrane-like environment. Nature 450 :376-382. PubMed Id: 18004376.
*Kv1.2/Kv2.1 Voltage-gated potassium channel chimera: Rattus norvegicus* E Eukaryota (expressed in Pichia pastoris), 2.9 Å** F233W Mutant.	3LNM	Data File Jmol Viewer 3LNM	Tao et al. (2010). Tao X, Lee A, Limapichat W, Dougherty DA, & MacKinnon R (2010). A gating charge transfer center in voltage sensors. Science 328 :67-73. PubMed Id: 20360102.
*Kv1.2/Kv2.1 Voltage-gated potassium channel chimera, V406W mutant: Rattus norvegicus* E Eukaryota (expressed in Pichia pastoris), 3.3 Å**	5WIE	Data File Jmol Viewer 5WIE	Pau et al. (2017). Pau V, Zhou Y, Ramu Y, Xu Y, & Lu Z (2017). Crystal structure of an inactivated mutant mammalian voltage-gated K⁺ channel. Nat Struct Mol Biol 24 :857-865. PubMed Id: 28846092. doi:10.1038/nsmb.3457.
*Kv1.2/Kv2.1 voltage-gated potassium channel chimera in lipid nanodiscs: Rattus norvegicus* E Eukaryota (expressed in Komagataella pastoris), 3.3 Å** cryo-EM structure cytosolic domain, 3 Å: 6EBL TM domain of α subunit, 4 Å: 6EBM	6EBK	Data File Jmol Viewer 6EBK 6EBL 6EBM	Matthies et al. (2018). Matthies D, Bae C, Toombes GE, Fox T, Bartesaghi A, Subramaniam S, & Swartz KJ (2018). Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs. Elife 7 :e37558. PubMed Id: 30109985. doi:10.7554/eLife.37558.
*K_v1.3 lymphocyte Voltage-gated potassium Channel: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** cryo-EM structure H451N mutant, 3.30 Å: 7EJ2	7EJ1	Data File Jmol Viewer 7EJ1 7EJ2	Liu et al. (2021). Liu S, Zhao Y, Dong H, Xiao L, Zhang Y, Yang Y, Ong ST, Chandy KG, Zhang L, & Tian C (2021). Structures of wild-type and H451N mutant human lymphocyte potassium channel KV1.3. Cell Discov 7 1:39. PubMed Id: 34059645. doi:10.1038/s41421-021-00269-y.
*K_v1.3 lymphocyte Voltage-gated potassium Channel with beta subunits, apo state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.40 Å** cryo-EM structure dalazatide-bound state, 3.40 Å 7WF4	7WF3	Data File Jmol Viewer 7WF3 7WF4	Tyagi et al. (2022). Tyagi A, Ahmed T, Jian S, Bajaj S, Ong ST, Goay SSM, Zhao Y, Vorobyov I, Tian C, Chandy KG, & Bhushan S (2022). Rearrangement of a unique Kv1.3 selectivity filter conformation upon binding of a drug. Proc Natl Acad Sci U S A 119 5:e2113536119. PubMed Id: 35091471. doi:10.1073/pnas.2113536119.
*K_v3.1 voltage-gated potassium channel, apo condition: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure with Zn, 3.10 Å: 7PHI dimeric state, with Zn, 3.10 Å: 7PHK with EDTA, 3.20 Å: 7PHL	7PHH	Data File Jmol Viewer 7PHH 7PHK 7PHI 7PHL	Chi et al. (2022). Chi G, Liang Q, Sridhar A, Cowgill JB, Sader K, Radjainia M, Qian P, Castro-Hartmann P, Venkaya S, Singh NK, McKinley G, Fernandez-Cid A, Mukhopadhyay SMM, Burgess-Brown NA, Delemotte L, Covarrubias M, & Dürr KL (2022). Cryo-EM structure of the human Kv3.1 channel reveals gating control by the cytoplasmic T1 domain. Nat Commun 13 1:4087. PubMed Id: 35840580. doi:10.1038/s41467-022-29594-w.
*K_v3.1 voltage-gated potassium channel, apo channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.65 Å** cryo-EM structure with bound modulator Lu AG00563, 3.03 Å: 7PQU	7PQT	Data File Jmol Viewer 7PQT 7PQU	Botte et al. (2022). Botte M, Huber S, Bucher D, Klint JK, Rodríguez D, Tagmose L, Chami M, Cheng R, Hennig M, & Abdul Rahman W (2022). Apo and ligand-bound high resolution Cryo-EM structures of the human Kv3.1 channel reveal a novel binding site for positive modulators. PNAS Nexus 1 3:pgac083. PubMed Id: 36741467. doi:10.1093/pnasnexus/pgac083.
*K_v3.1 voltage-gated potassium channel with bound modulator AUT1: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure with bound modulator AUT5, 2.50 Å: 8QUD	8QUC	Data File Jmol Viewer 8QUC 8QUD	Liang et al. (2024). Liang Q, Chi G, Cirqueira L, Zhi L, Marasco A, Pilati N, Gunthorpe MJ, Alvaro G, Large CH, Sauer DB, Treptow W, & Covarrubias M (2024). The binding and mechanism of a positive allosteric modulator of Kv3 channels. Nat Commun 15 1:2533. PubMed Id: 38514618. doi:10.1038/s41467-024-46813-8.
*Kv4.2 Voltage-gated potassium Channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure Kv4.2-KChIP1 complex, 3.10 Å 7F3F Kv4.2-KChIP1 complex (Octodon degus), 3.10 Å 7E84 Kv4.2-KChIP1 complex, intracellular region, 3.10 Å 7E83 Kv4.2-KChIP1 complex, transmembrane region, 3.20 Å 7E7Z Kv4.2-DPP6S complex, 4.20 Å 7E8B Kv4.2-DPP6S complex, transmembrane and intracellular region, 3.40 Å 7E87 Kv4.2-DPP6S complex, extracellular region, 4.00 Å 7E89 Kv4.2-DPP6S-KChIP1 complex, 4.50 Å 7E8H Kv4.2-DPP6S-KChIP1 complex, transmembrane and intracellular region, 3.90 Å 7E8E Kv4.2-DPP6S-KChIP1 complex, extracellular region, 4.50 Å 7E8G	7F0J	Data File Jmol Viewer 7F0J 7E8H 7F3F 7E8G 7E89 7E8E 7E83 7E84 7E8B 7E7Z 7E87	Kise et al. (2021). Kise Y, Kasuya G, Okamoto HH, Yamanouchi D, Kobayashi K, Kusakizako T, Nishizawa T, Nakajo K, & Nureki O (2021). Structural basis of gating modulation of Kv4 channel complexes. Nature 599 7883:158-164. PubMed Id: 34552243. doi:10.1038/s41586-021-03935-z.
*K_v4.2 Voltage-gated potassium Channel, in complex with KChIP2, TM region, open state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.76 Å** cryo-EM structure inactivated state, class 1, 3.00 Å: 7UKC inactivated state, class 2, 2.88 Å: 7UKD in an intermediate state, 3.01 Å: 7UKE putative resting state, 3.02 Å:7UKF in an open state, 2.24 Å: 7UKG in an open state, intracellular region, 2.33 Å:7UKH	7UK5	Data File Jmol Viewer 7UK5 7UKE 7UKG 7UKF 7UKC 7UKD 7UKH	Ye et al. (2022). Ye W, Zhao H, Dai Y, Wang Y, Lo YH, Jan LY, & Lee CH (2022). Activation and closed-state inactivation mechanisms of the human voltage-gated KV4 channel complexes. Mol Cell 82 13:2427-2442.e4. PubMed Id: 35597238. doi:10.1016/j.molcel.2022.04.032.
*K_v4.3 Voltage-gated potassium Channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure complex with KChIP1, 3.40 Å: 7W6N complex with KChIP2, 2.80 Å: 7W6S complex with KChIP1 & DPP6, 3.85 Å: 7W6T	7W3Y	Data File Jmol Viewer 7W3Y 7W6N 7W6S 7W6T	Ma et al. (2022). Ma D, Zhao C, Wang X, Li X, Zha Y, Zhang Y, Fu G, Liang P, Guo J, & Lai D (2022). Structural basis for the gating modulation of Kv4.3 by auxiliary subunits. Cell Res 32 4:411-414. PubMed Id: 34997220. doi:10.1038/s41422-021-00608-4.
*Eag1 (KCNH1, K_v10.1) voltage-gated K⁺ channel with bound calmodulin (CaM): Rattus norvegicus* E Eukaryota (expressed in SF9 cells), 3.78 Å** Cryo-EM structure	5K7L	Data File Jmol Viewer 5K7L	Whicher & MacKinnon (2016). Whicher JR, & MacKinnon R (2016). Structure of the voltage-gated K⁺ channel Eag1 reveals an alternative voltage sensing mechanism. Science 353 :664-669. PubMed Id: 27516594. doi:10.1126/science.aaf8070.
*Eag2 (KCNH5) K_v voltage-gated K⁺ channel, closed state 1: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure closed state 2, 3.40 Å: 7YIE pre-open state 1, 3.50 Å: 7YIF pre-open state 2, 3.60 Å: 7YIG open state, 3.50 Å: 7YIH pore dilation but the non-conducting state, 3.80 Å: 7YIJ	7YID	Data File Jmol Viewer 7YID 7YIJ 7YIG 7YIH 7YIF 7YIE	Zhang et al. (2023). Zhang M, Shan Y, & Pei D (2023). Mechanism underlying delayed rectifying in human voltage-mediated activation Eag2 channel. Nat Commun 14 1:1470. PubMed Id: 36928654. doi:10.1038/s41467-023-37204-6.
*Eag K_v channel with voltage sensor in the up conformation: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.90 Å** cryo-EM structure voltage sensor in the intermediate conformation, 4.90 Å: 8EP0 voltage sensor in the down conformation, 5.40 Å:8EP1	8EOW	Data File Jmol Viewer 8EOW 8EP0 8EP1	Mandala & MacKinnon (2022). Mandala VS, & MacKinnon R (2022). Voltage-sensor movements in the Eag Kv channel under an applied electric field. Proc Natl Acad Sci U S A 119 46:e2214151119. PubMed Id: 36331999. doi:10.1073/pnas.2214151119.
*hERG voltage-dependent K⁺ channel hERG_T: Homo sapiens* E Eukaryota (expressed in HEK293S cells), 3.8 Å** cryo-EM structure. Engineered protein. Residues 141-350 and 871-1005 were removed. hERG_Ts, 3.7 Å: 5VA1 hERG_Ts S631A mutant, 4.0 Å: 5VA3	5VA2	Data File Jmol Viewer 5VA2 5VA1 5VA3	Wang & MacKinnon (2017). Wang W, & MacKinnon R (2017). Cryo-EM Structure of the Open Human Ether-à-go-go-Related K⁺ Channel hERG. Cell 169 3:422-430.e10. PubMed Id: 28431243. doi:10.1016/j.cell.2017.03.048.
*hERG voltage-dependent K⁺ channel, K⁺ bound: homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.90 Å** cryo-EM structure in the presence of astemizole, 3.70 Å: 7CN1	7CN0	Data File Jmol Viewer 7CN0 7CN1	Asai et al. (2021). Asai T, Adachi N, Moriya T, Oki H, Maru T, Kawasaki M, Suzuki K, Chen S, Ishii R, Yonemori K, Igaki S, Yasuda S, Ogasawara S, Senda T, & Murata T (2021). Cryo-EM Structure of K⁺-Bound hERG Channel Complexed with the Blocker Astemizole. Structure 29 3:203-212.e4. PubMed Id: 33450182. doi:10.1016/j.str.2020.12.007.
*KvLm voltaged-gated potassium channel: C-terminal pore module: Listeria monocytogenes* B Bacteria (expressed in E. coli), 3.10 Å** Shows pore in transient conformation between closed and open. Crystallized under sodium condition, 3.35 Å: 4H37	4H33	Data File Jmol Viewer 4H33 4H37	Santos et al. (2012). Santos JS, Asmar-Rovira GA, Han GW, Liu W, Syeda R, Cherezov V, Baker KA, Stevens RC, & Montal M (2012). Crystal Structure of a Voltage-gated K⁺ Channel Pore Module in a Closed State in Lipid Membranes. J Biol Chem 287 :43063-43070. PubMed Id: 23095758. doi:10.1074/jbc.M112.415091.
*MthK Potassium channel, Ca⁺⁺ gated: Methanothermobacter thermautotrophicus* A Archaea (expressed in E. coli), 3.3 Å**	1LNQ	Data File Jmol Viewer 1LNQ MthK K+ channel	Jiang et al. (2002). Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R (2002). Crystal structure and mechanism of a calcium-gated potassium channel. Nature 417 :515-22. PubMed Id: 12037559. Crystal structure and mechanism. See also: Jiang et al. (2002). Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R (2002). The open pore conformation of potassium channels. Nature 417 :523-6. PubMed Id: 12037560. Open pore conformation.
*K⁺ pore of the MthK Potassium channel (residues 28-99): Methanothermobacter thermautotrophicus* A Archaea (expressed in E. coli), 1.45 Å** 3LDC crystallized in 100 mM KCl. S68H/V77C mutant. 99 mM NaCl + 1 mM KCl; S68R, V77C mutant; 1.45 Å: 3LDD 100 mM NaCl; S68H, V77C mutant; 2.21 Å: 3LDE	3LDC	Data File Jmol Viewer 3LDC 3LDD 3LDE	Ye et al. (2010). Ye S, Li Y, & Jiang Y (2010). Novel insights into K⁺selectivity from high-resolution structures of an open K⁺channel pore. Nature Struct Molec Biol 17 :1019-1023. PubMed Id: 20676101.
*MthK Potassium channel, Ca⁺⁺ gated: Methanothermobacter thermautotrophicus* A Archaea (expressed in E. coli), 3.40 Å** RCK domain D184N mutant, Ca²⁺-bound, 2.80 Å: 3RBX	3RBZ	Data File Jmol Viewer 3RBZ 3RBX	Pau et al. (2011). Pau VP, Smith FJ, Taylor AB, Parfenova LV, Samakai E, Callaghan MM, Abarca-Heidemann K, Hart PJ, & Rothberg BS (2011). Structure and function of multiple Ca²⁺-binding sites in a K⁺ channel regulator of K⁺ conductance (RCK) domain. Proc Natl Acad Sci USA 108 :17684-17689. PubMed Id: 21997217. doi:10.1073/pnas.1107229108.
*MthK Potassium channel gating ring with bound Ba²⁺: Methanothermobacter thermautotrophicus* A Archaea (expressed in E. coli), 3.10 Å**	4EI2	Data File Jmol Viewer 4EI2	Smith et al. (2012). Smith FJ, Pau VP, Cingolani G, Rothberg BS (2012). Crystal Structure of a Ba²⁺-Bound Gating Ring Reveals Elementary Steps in RCK Domain Activation. Structure 20 :2038-2047. PubMed Id: 23085076. doi:10.1016/j.str.2012.09.014.
*MthK Potassium channel pore (S68H,V77C mutant): Methanothermobacter thermautotrophicus* A Archaea (expressed in E. coli), 1.65 Å** In the presence of TBSb, 1.65 Å 4HZ3	4HYO	Data File Jmol Viewer 4HYO 4HZ3	Posson et al. (2013). Posson DJ, McCoy JG, & Nimigean CM (2013). The voltage-dependent gate in MthK potassium channels is located at the selectivity filter. Nature Struc Mol Biol 20 :159-166. PubMed Id: 23262489. doi:10.1038/nsmb.2473.
*MthK Potassium channel gating ring with bound Ca²⁺: Methanothermobacter thermautotrophicus* A Archaea (expressed in E. coli), 2.50 Å** with single ligand, 1.84 Å: 4L74 D184N mutant, 2.39 Å: 4L75 E212Q mutant, 2.99 Å: 4L76	4L73	Data File Jmol Viewer 4L73 4L76 4L74 4L75	Smith et al. (2013). Smith FJ, Pau VP, Cingolani G, & Rothberg BS (2013). Structural basis of allosteric interactions among Ca²⁺-binding sites in a K⁺ channel RCK domain. Nat Commun 4 :2621. PubMed Id: 24126388. doi:10.1038/ncomms3621.
*MthK Potassium channel, full length: Methanothermobacter thermautotrophicus* B Bacteria (expressed in E. coli), 3.11 Å**	6OLY	Data File Jmol Viewer 6OLY	Kopec et al. (2019). Kopec W, Rothberg BS, & de Groot BL (2019). Molecular mechanism of a potassium channel gating through activation gate-selectivity filter coupling. Nat Commun 10 1:5366. PubMed Id: 31772184. doi:10.1038/s41467-019-13227-w.
*MthK Potassium channel, Ca⁺⁺ gated, closed state with EDTA: Methanothermobacter thermautotrophicus* B Bacteria (expressed in E.coli), 3.60 Å** cryo-EM structure calcium bound, open inactivated state, 4.50 Å: 6U68 Calcium bound, open-inactivated state 2, 6.30 Å: 6U6E Calcium-bound, closed state, 3.60 Å: 6U5R Calcium-bound, gating ring state 1, 3.30 Å: 6U5P Calcium-bound, gating ring state 2, 3.20 Å: 6U5N Calcium-bound, closed state, 3.60 Å: 6U5R N-terminal truncation state 1, 6.70 Å: 6UX7 N-terminal truncation state 2 bound with calcium, 4.50 Å: 6UXA N-terminal truncation state 3 bound with calcium, 4.90 Å: 6UXB N-terminal truncation RCK domain state 1 bound with calcium, 3.50 Å: 6UWN N-terminal truncation RCK domain state 2 bound with calcium, 3.50 Å: 6UX4	6U6D	Data File Jmol Viewer 6U6D 6UX7 6UX4 6UXA 6UWN 6U5R 6U6E 6UXB 6U5P 6U68 6U5N	Fan et al. (2020). Fan C, Sukomon N, Flood E, Rheinberger J, Allen TW, & Nimigean CM (2020). Ball-and-chain inactivation in a calcium-gated potassium channel. Nature 580 7802:288-293. PubMed Id: 32269335. doi:10.1038/s41586-020-2116-0.
*MthK Potassium channel pore, 150 mM K⁺: Methanothermobacter thermautotrophicus* B Bacteria (expressed in E. coli), 1.65 Å** 50 mM K⁺, 1.55 Å: 6U9T 11 mM K⁺, 1.80 Å: 6U9Y 6 mM K⁺, 1.95 Å: 6U9Z	6U9P	Data File Jmol Viewer 6U9P 6U9Y 6U9T 6U9Z	Boiteux et al. (2020). Boiteux C, Posson DJ, Allen TW, & Nimigean CM (2020). Selectivity filter ion binding affinity determines inactivation in a potassium channel. Proc Natl Acad Sci U S A 117 47:29968-29978. PubMed Id: 33154158. doi:10.1073/pnas.2009624117.
*Slo1 (BK) calcium-activated K⁺ channel: Aplysia californica* E Eukaryota (expressed in Trichoplusia ni), 3.5 Å** cryo-EM structure	5TJ6	Data File Jmol Viewer 5TJ6	Tao et al. (2017). Tao X, Hite RK, & MacKinnon R (2017). Cryo-EM structure of the open high-conductance Ca⁺²-activated K⁺ channel. Nature 541 :46-51. PubMed Id: 27974795. doi:10.1038/nature20608.
*Slo1 (BK) calcium-activated K⁺ channel with bound Ca²⁺: Aplysia californica* E Eukaryota (expressed in Trichoplusia ni), 3.8 Å** cryo-EM structure	5TJI	Data File Jmol Viewer 5TJI	Hite et al. (2017). Hite RK, Tao X, & MacKinnon R (2017). Structural basis for gating the high-conductance Ca²⁺-activated K⁺ channel. Nature 541 :52-57. PubMed Id: 27974801. doi:10.1038/nature20775.
*Human BK (SLO1) Channel Ca²⁺-activation apparatus: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.0 Å** Consists of four BK subunits organized as a ring of 8 RCK (Regulator of K⁺ conductance) domains. Although not a transmembrane protein, it is an important accessory structure for regulating voltage-gated potassium channels.	3MT5	Data File Jmol Viewer 3MT5	Yuan et al. (2010). Yuan P, Leonetti MD, Pico AR, Hsiung Y, & MacKinnon R (2010). Structure of the human BK channel Ca²⁺-activation apparatus at 3.0 A resolution. Science 329 :182-186. PubMed Id: 20508092.
*Human BK (SLO1) Channel Ca²⁺-activation apparatus: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.1 Å** Consists of four BK subunits organized as a ring of 8 RCK (Regulator of K⁺ conductance) domains. Although not a transmembrane protein, it is an important accessory structure for regulating voltage-gated potassium channels.	3NAF	Data File Jmol Viewer 3NAF	Wu et al. (2010). Wu Y, Yang Y, Ye S, & Jiang Y (2010). Structure of the gating ring from the human large-conductance Ca²⁺-gated K(+) channel. Nature 466 :393-397. PubMed Id: 20574420.
*Human BK (SLO1) K⁺ channel in complex with β4, Ca²⁺ bound: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.2 Å** cryo-EM structure Ca²⁺-free, 3.5 Å: 6V35 Ca²⁺-bound hsSlo1 channel, 3.8 Å: 6V38 Ca²⁺-free hsSlo1 channel, 4 Å: 6V3G	6V22	Data File Jmol Viewer 6V22 6V38 6V3G 6V35	Tao & MacKinnon (2019). Tao X, & MacKinnon R (2019). Molecular structures of the human Slo1 K⁺ channel in complex with β4. Elife 8 :e51409. PubMed Id: 31815672. doi:10.7554/eLife.51409.
*Human BK (SLO1) K⁺ channel, L390P mutant: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 2.00 Å**	6V5A	Data File Jmol Viewer 6V5A	Geng et al. (2020). Geng Y, Deng Z, Zhang G, Budelli G, Butler A, Yuan P, Cui J, Salkoff L, & Magleby KL (2020). Coupling of Ca²⁺ and voltage activation in BK channels through the ?B helix/voltage sensor interface. Proc Natl Acad Sci USA 117 25:14512-14521. PubMed Id: 32513714. doi:10.1073/pnas.1908183117.
*Human BK (SLO1) K⁺ channel in total membrane vesicles, Ca²⁺-free and EDTA-free: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.80 Å** cryo-EM structure in plasma membrane vesicles, 2.70 Å: 8GHF in digitonin, Ca²⁺-free and EDTA-free, 3.30 Å: 8GHG	8GH9	Data File Jmol Viewer 8GH9 8GHF 8GHG	Tao et al. (2023). Tao X, Zhao C, & MacKinnon R (2023). Membrane protein isolation and structure determination in cell-derived membrane vesicles. Proc Natl Acad Sci U S A 120 18:e2302325120. PubMed Id: 37098056. doi:10.1073/pnas.2302325120.
*BK (SLO1) Channel Ca²⁺ gating ring from zebra fish in the open state: Danio rerio* E Eukaryota (expressed in S. frugiperda), 3.61 Å**	3U6N	Data File Jmol Viewer 3U6N	Yuan et al. (2012). Yuan P, Leonetti MD, Hsiung Y, & Mackinnon R (2012). Open structure of the Ca²⁺ gating ring in the high-conductance Ca²⁺-activated K⁺ channel. Nature 481 :94-97. PubMed Id: 22139424. doi:10.1038/nature10670.
*Slo1 channel, calcium bound: Drosophila melanogaster* E Eukaryota (expressed in Trichoplusia ni), 2.38 Å** cryo-EM structure Ca²⁺ free, 2.78 Å 7PXF Emodepside-bound, 2.59 Å 7PXH	7PXE	Data File Jmol Viewer 7PXE 7PXH 7PXF	Raisch et al. (2021). Raisch T, Brockmann A, Ebbinghaus-Kintscher U, Freigang J, Gutbrod O, Kubicek J, Maertens B, Hofnagel O, & Raunser S (2021). Small molecule modulation of the Drosophila Slo channel elucidated by cryo-EM. Nat Commun 12 1:7164. PubMed Id: 34887422. doi:10.1038/s41467-021-27435-w.
*Slo2.2 Na⁺-activated K⁺ channel, complete: Gallus gallus* E Eukaryota (expressed in S. frugiperda), 4.5 Å** Cryo-EM structure Gating ring only, 5A6F TM domain only, 5A6G	5A6E	Data File Jmol Viewer 5A6E 5A6F 5A6G	Hite et al. (2015). Hite RK, Yuan P, Li Z, Hsuing Y, Walz T, & MacKinnon R (2015). Cryo-electron microscopy structure of the Slo2.2 Na(+)-activated K(+) channel. Nature 527 :198-203. PubMed Id: 26436452. doi:10.1038/nature14958.
*Slo2.2 Na⁺-activated K⁺ channel (complete), open conformation: Gallus gallus* E Eukaryota (expressed in S. frugiperda), 3.8 Å** cryo-EM structure closed conformation, 4.3 Å: 5U76	5U70	Data File Jmol Viewer 5U70 5U76	Hite & MacKinnon (2017). Hite RK, & MacKinnon R (2017). Structural Titration of Slo2.2, a Na⁺-Dependent K⁺ Channel. Cell 168 :390-399. PubMed Id: 28111072. doi:10.1016/j.cell.2016.12.030.
*Slo2.2 Na⁺-activated K⁺ channel, open conformation: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.18 Å** cryo-EM structure closed confirmation, 2.95 Å: 8HKM closed confirmation, state 1, 2.64 Å: 8HK6 closed confirmation, state 2, 2.66 Å: 8HKF closed confirmation, state 3, 2.84 Å: 8HKK with bound inhibitor Compound 23, 2.90 Å: 8HKQ	8HIR	Data File Jmol Viewer 8HIR 8HKF 8HKK 8HK6 8HKQ 8HKM	Zhang et al. (2023). Zhang J, Liu S, Fan J, Yan R, Huang B, Zhou F, Yuan T, Gong J, Huang Z, & Jiang D (2023). Structural basis of human Slo2.2 channel gating and modulation. Cell Rep 42 8:112858. PubMed Id: 37494189. doi:10.1016/j.celrep.2023.112858.
*SLO3 K⁺ Channel pH-sensitive Gating Ring: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.40 Å** Although not a transmembrane protein, it is an important accessory structure for regulating voltage-gated potassium channels.	4HPF	Data File Jmol Viewer 4HPF	Leonetti et al. (2012). Leonetti MD, Yuan P, Hsiung Y, & Mackinnon R (2012). Functional and structural analysis of the human SLO3 pH- and voltage-gated K⁺ channel. Proc Natl Acad Sci USA 109 :19274-19279. PubMed Id: 23129643. doi:10.1073/pnas.1215078109.
*small-conductance Ca²⁺-activated K⁺ (SK) channel calmodulin complex, Ca- bound state I: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure calmodulin channel complex, 3.40 Å: 6CNM calmodulin channel complex in the Ca²⁺ bound state II, 4.70 Å: 6CNO	6CNN	Data File Jmol Viewer 6CNN 6CNO 6CNM	Lee & MacKinnon (2018). Lee CH, & MacKinnon R (2018). Activation mechanism of a human SK-calmodulin channel complex elucidated by cryo-EM structures. Science 360 6388:508-513. PubMed Id: 29724949. doi:10.1126/science.aas9466.
*GsuK multi-ligand gated K⁺ channel, L97D mutant: Geobacter sulfurreducens* B Bacteria (expressed in E. coli), 2.60 Å** This a multi-ligand gated channel. Both ADP and NAD⁺ activate the channel, whereas Ca²⁺ serves as an allosteric inhibitor. L97D mutant with bound ADP, 2.80 Å: 4GX1 L97D mutant with bound NAD⁺, 3.20 Å: 4GX2 Wild-type channel, 3.70 Å: 4GX5 RCK domain, 3.00 Å: 4GVL	4GX0	Data File Jmol Viewer 4GX0 4GX1 4GX5 4GX2 4GVL	Kong et al. (2012). Kong C, Zeng W, Ye S, Chen L, Sauer DB, Lam Y, Derebe MG, & Jiang Y (2012). Distinct gating mechanisms revealed by the structures of a multi-ligand gated K⁺ channel. eLife 1 :e00184. PubMed Id: 23240087. doi:10.7554/eLife.00184.
*Kir2.1 Inward-Rectifier Potassium 2.1 Channel: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 4.30 Å** cryo-EM structure	7ZDZ	Data File Jmol Viewer 7ZDZ	Fernandes et al. (2022). Fernandes CAH, Zuniga D, Fagnen C, Kugler V, Scala R, Péhau-Arnaudet G, Wagner R, Perahia D, Bendahhou S, & Vénien-Bryan C (2022). Cryo-electron microscopy unveils unique structural features of the human Kir2.1 channel. Sci Adv 8 38:eabq8489. PubMed Id: 36149965. doi:10.1126/sciadv.abq8489.
*Kir2.2 Inward-Rectifier Potassium Channel (Complete): Gallus gallus* E Eukaryota (expressed in Pichia pastoris), 3.1 Å**	3JYC	Data File Jmol Viewer 3JYC	Tao et al (2009). Tao X, Avalos JL, Chen J, & MacKinnon R (2009). Crystal structure of the eukaryotic strong inward-rectifier K⁺channel Kir2.2 at 3.1 Å resolution. Science 326 :1668-1674. PubMed Id: 20019282.
*Kir2.2 Inward-Rectifier Potassium Channel in complex with PIP₂: Gallus gallus* E Eukaryota (expressed in Pichia pastoris), 3.31 Å** In complex with dioctanoylglycerol pyrophosphate (DGPP), 2.45 Å: 3SPC I223L mutant in complex with PIP₂, 3.00 Å: 3SPH I223L mutant, apo form, 3.31 Å: 3SPJ R186A mutant in complex with PIP₂, 2.61 Å: 3SPG	3SPI	Data File Jmol Viewer 3SPI 3SPG 3SPC 3SPH 3SPJ	Hansen et al. (2011). Hansen SB, Tao X, & Mackinnon R (2011). Structural basis of PIP₂ activation of the classical inward rectifier K⁺ channel Kir2.2. Nature 477 :495-498. PubMed Id: 21874019. doi:10.1038/nature10370.
*Kir2.2 Inward-Rectifier Potassium Channel, K62W mutant (apo form): Gallus gallus* E Eukaryota (expressed in Komagataella pastoris), 2.0 Å** in complex with PIP₂, 2.8 Å: 5KUM	5KUK	Data File Jmol Viewer 5KUK 5KUM	Lee et al. (2016). Lee SJ, Ren F, Zangerl-Plessl EM, Heyman S, Stary-Weinzinger A, Yuan P, & Nichols CG (2016). Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipids. J Gen Physiol 148 :227-237. PubMed Id: 27527100. doi:10.1085/jgp.201611616.
*Kir2.2 Inward-Rectifier Potassium Channel, forced open G178D mutant: Gallus gallus* E Eukaryota (expressed in Komagataella pastoris), 3.6 Å** with bound PIP₂, 2.81 Å: 6M84	6M86	Data File Jmol Viewer 6M86 6M84	Zangerl-Plessl et al. (2020). Zangerl-Plessl EM, Lee SJ, Maksaev G, Bernsteiner H, Ren F, Yuan P, Stary-Weinzinger A, & Nichols CG (2020). Atomistic basis of opening and conduction in mammalian inward rectifier potassium (Kir2.2) channels. J Gen Physiol 152 1. PubMed Id: 31744859. doi:10.1085/jgp.201912422.
*GIRK1 (Kir3.1) cytoplasmic domain: Mus musculus* E Eukaryota (expressed in E. coli), 1.8 Å** GIRK = G-Protein-Gated Inward Rectifying Potassium Channel	1N9P	Data File Jmol Viewer 1N9P	Nishida & MacKinnon (2002). Nishida M & MacKinnon R (2002). Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 Å resolution. Cell 111 :957-65. PubMed Id: 12507423.
*Kir3.1-Prokaryotic Kir Chimera: Mus musculus & Burkholderia xenovornas* E Eukaryota (expressed in Escherichia coli), 2.2 Å**	2QKS	Data File Jmol Viewer 2QKS	Nishida et al (2007). Nishida M, Cadene M, Chait, BT & MacKinnon R (2007). Crystal structure of a Kir3.1-prokaryotic Kir channel chimera. EMBO J 26 :4005-4015. PubMed Id: 17703190.
*Kir3.1 cytoplasmic domain: Mus musculus* E Eukaryota (expressed in E. coli), 2.0 Å**	3K6N	Data File Jmol Viewer 3K6N	Xu et al (2009). Xu Y, Shin HG, Szép S, & Lu Z (2009). Physical determinants of strong voltage sensitivity of K⁺channel block. Nat Struct Mol Biol 16 :1252-1258. PubMed Id: 19915587.
*GIRK2 (Kir3.2) G-protein-gated K⁺ channel: Mus musculus* E Eukaryota (expressed in Pichia pastoris), 3.60 Å** First complete structure of a G-protein-gated potassium-selective channel. Wild-type protein + PIP₂, 3.00 Å: 3SYA D228N mutant, 3.4 Å: 3SYC R201A mutant, 3.1 Å: 3SYP R201A mutant + PIP₂, 3.45 Å: 3SYQ	3SYO	Data File Jmol Viewer 3SYO 3SYP 3SYA 3SYC 3SYQ	Whorton & Mackinnon (2011). Whorton MR & Mackinnon R (2011). Crystal Structure of the Mammalian GIRK2 K⁺ Channel and Gating Regulation by G Proteins, PIP₂, and Sodium Cell 147 :199-208. PubMed Id: 21962516. doi:10.1016/j.cell.2011.07.046.
*GIRK2 (Kir3.2) G-protein-gated K⁺ channel in complex with βγ G-protein subunits: Mus musculus* E Eukaryota (expressed in Pichia pastoris ), 3.45 Å** The β and γ subunits are from homo sapiens expressed in S. frugiperda	4KFM	Data File Jmol Viewer 4KFM	Whorton & MacKinnon (2013). Whorton MR & MacKinnon R (2013). X-ray structure of the mammalian GIRK2-βγ G-protein complex. Nature 498 :190-197. PubMed Id: 23739333. doi:10.1038/nature12241.
*GIRK2 (Kir3.2) G-protein-gated K⁺ channel, apo form: Mus musculus* E Eukaryota (expressed in Komagataella pastoris), 3.90 Å** cryo-EM structure in complex with PIP₂, 3.30 Å: 6XIT	6XIS	Data File Jmol Viewer 6XIS 6XIT	Niu et al. (2020). Niu Y, Tao X, Touhara KK, & MacKinnon R (2020). Cryo-EM analysis of PIP₂ regulation in mammalian GIRK channels. Elife 9 :e60552. PubMed Id: 32844743. doi:10.7554/eLife.60552.
*KirBac1.1 Inward-Rectifier Potassium channel (closed state): Burkholderia pseudomallei* B Bacteria, 3.65 Å** For re-refined structure, see 2WLL	1P7B	Data File Jmol Viewer 1P7B 2WLL KirBac1.1 potassium channel	Kuo et al (2003). Kuo A, Gulbis JM, Antcliff JF, Rahman T, Lowe ED, Zimmer J, Cuthbertson J, Ashcroft FM, Ezaki T, & Doyle DA (2003). Crystal structure of the potassium channel KirBac1.1 in the closed state. Science 300 :1922-1926. PubMed Id: 12738871.
*KirBac3.1 Inward-Rectifier Potassium channel (semi-latched): Magnetospirillum magnetotacticum* B Bacteria (expressed in E. coli), 2.60 Å** (Re-refinement of 1XL4) Latched State, 2.80 Å: 2WLK (re-refinement of 1XL6) Semi-latched State, 3.09 Å: 2WLI Semi-latched State, 4.20 Å: 2WLO Semi-latched State, 3.61 Å: 2WLM Unlatched State, 3.44 Å: 2WLN Unlatched State, 3.28 Å: 2WLH Q170A mutant (stalled), 3.10 Å: 2X6A Q170A mutant (blocked with Ba⁺⁺), 3.30 Å: 2X6B Q170A mutant (conductive), 2.70 Å: 2X6C	2WLJ	Data File Jmol Viewer 2WLJ 2WLM 2WLI 2X6A 2WLO 2X6B 2WLK 1XL6 2X6C 2WLN 2WLH 1XL4	Clarke et al. (2010). Clarke OB, Caputo AT, Hill AP, Vandenberg JI, Smith BJ & Gulbis JM (2010). Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels. Cell 141 :1018-1029. PubMed Id: 20564790.
*KirBac3.1 Open-State Channel (S129R mutant): Magnetospirillum magnetotacticum* B Bacteria (expressed in E. coli), 3.05 Å**	3ZRS	Data File Jmol Viewer 3ZRS	Bavro et al. (2012). Bavro VN, De Zorzi R, Schmidt MR, Muniz JR, Zubcevic L, Sansom MS, Vénien-Bryan C, & Tucker SJ (2012). Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating. Nature Struc Mol Biol 19 :158-163. PubMed Id: 22231399. doi:10.1038/nsmb.2208.
*KirBac3.1 Open-State Channel (S129R/S205L mutant): Magnetospirillum magnetotacticum* B Bacteria (expressed in E. coli), 2.46 Å**	4LP8	Data File Jmol Viewer 4LP8	Zubcevic et al. (2014). Zubcevic L, Bavro VN, Muniz JR, Schmidt MR, Wang S, De Zorzi R, Venien-Bryan C, Sansom MS, Nichols CG, & Tucker SJ (2014). Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains. J Biol Chem 289 :143-151. PubMed Id: 24257749. doi:10.1074/jbc.M113.501833 .
*KirBac3.1 Inward-Rectifier Potassium channel: Magnetospirillum magnetotacticum* B Bacteria (expressed in E. coli), 2.00 Å** S129C-F135C mutant, 3.09 Å: 6O9V A133C-T136C mutant, 4.01 Å: 6O9T	6O9U	Data File Jmol Viewer 6O9U 6O9V 6O9T	Black et al. (2020). Black KA, He S, Jin R, Miller DM, Bolla JR, Clarke OB, Johnson P, Windley M, Burns CJ, Hill AP, Laver D, Robinson CV, Smith BJ, & Gulbis JM (2020). A constricted opening in Kir channels does not impede potassium conduction. Nat Commun 11 1:3024. PubMed Id: 32541684. doi:10.1038/s41467-020-16842-0.
*KirBac3.1 Inward-Rectifier Potassium channel, C71S C262S mutant: Magnetospirillum magnetotacticum* B Bacteria (expressed in E. coli), 2.40 Å** L124M mutant, 2.72 Å 7N9K	7N9L	Data File Jmol Viewer 7N9L 7N9K	Jin et al. (2022). Jin R, He S, Black KA, Clarke OB, Wu D, Bolla JR, Johnson P, Periasamy A, Wardak A, Czabotar P, Colman PM, Robinson CV, Laver D, Smith BJ, & Gulbis JM (2022). Ion currents through Kir potassium channels are gated by anionic lipids. Nat Commun 13 1:490. PubMed Id: 35079013. doi:10.1038/s41467-022-28148-4.
*KirBac3.1 Inward-Rectifier Potassium channel, W46R mutant: Magnetospirillum magnetotacticum* B Bacteria (expressed in E. coli), 2.80 Å**	7ADI	Data File Jmol Viewer 7ADI	Fagnen et al. (2021). Fagnen C, Bannwarth L, Oubella I, Zuniga D, Haouz A, Forest E, Scala R, Bendahhou S, De Zorzi R, Perahia D, & Vénien-Bryan C (2021). Integrative Study of the Structural and Dynamical Properties of a KirBac3.1 Mutant: Functional Implication of a Highly Conserved Tryptophan in the Transmembrane Domain. Int J Mol Sci 23 1:335. PubMed Id: 35008764. doi:10.3390/ijms23010335.
*SUR1/Kir6.2 pancreatic ATP-sensitive K⁺ channel: Cricetus cricetus/Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 6.3 Å** cryo-EM strucuture. Chimeric protein, SUR1 is from hamster (C. cricetus) and Kir6.2 from rat.	5TWV	Data File Jmol Viewer 5TWV	Martin et al. (2017). Martin GM, Yoshioka C, Rex EA, Fay JF, Xie Q, Whorton MR, Chen JZ, & Shyng SL (2017). Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating. Elife 6 :e2419. PubMed Id: 28092267. doi:10.7554/eLife.24149.
*SUR1/Kir6.2 pancreatic ATP-sensitive K⁺ channel: C. cricetus/Rattus norvegicus* E Eukaryota (expressed in INS-1 insulinoma cells), 3.63 Å** cryo-EM structure. Reveals ATP binding site.	6BAA	Data File Jmol Viewer 6BAA	Martin et al. (2017). Martin GM, Kandasamy B, DiMaio F, Yoshioka C, & Shyng SL (2017). Anti-diabetic drug binding site in a mammalian K_ATP channel revealed by Cryo-EM. Elife 6 :e31054. PubMed Id: 29035201. doi:10.7554/eLife.31054.
*SUR1/Kir6.2 pancreatic ATP-sensitive K⁺ channel, SUR1 bound to ATP and repaglinide: Cricetus cricetus/Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.65 Å** cryo-EM structure SUR1 bound to ATP and glibenclamide, 3.74 Å: 6PZA SUR1 bound to carbamazepine, 4.34 Å: 6PZC SUR1 bound to ATP only, 4.5 Å: 6PZI	6PZ9	Data File Jmol Viewer 6PZ9 6PZC 6PZI 6PZA	Martin et al. (2019). Martin GM, Sung MW, Yang Z, Innes LM, Kandasamy B, David LL, Yoshioka C, & Shyng SL (2019). Mechanism of pharmacochaperoning in a mammalian K_ATP channel revealed by cryo-EM. Elife 8 :e46417. PubMed Id: 31343405. doi:10.7554/eLife.46417.
SUR1/Kir6.2 pancreatic ATP-sensitive K⁺ channel, bound to ATP and repaglinide with Kir6.2-CTD in the up conformation: Cricetus cricetus/Rattus norvegicus E Eukaryota (expressed in Rattus norvegicus), 3.41 Å cryo-EM structure in the down conformation, 3.60 Å: 7TYT bound to ATP and repaglinide with SUR1-in conformation, 3.90 Å: 7U1Q bound to ATP and repaglinide with SUR1-out conformation, 3.80 Å: 7U1S in the presence of glibenclamide and ATP with Kir6.2-CTD in the down conformation, 7.40 Å: 7U6Y in the presence of carbamazepine and ATP with Kir6.2-CTD in the up conformation, 5.20 Å: 7U7M in the presence of carbamazepine and ATP with Kir6.2-CTD in the down conformation, 4.10 Å: 7U2X in the ATP-bound state with Kir6.2-CTD in the up conformation, 5.70 Å: 7UAA bound to ATP with Kir6.2-CTD in the down conformation, 4.52 Å: 7U1E	7TYS	Data File Jmol Viewer 7TYS 7U1Q 7UAA 7TYT 7U1E 7U6Y 7U1S 7U2X 7U7M	Sung et al. (2022). Sung MW, Driggers CM, Mostofian B, Russo JD, Patton BL, Zuckerman DM, & Shyng SL (2022). Ligand-mediated Structural Dynamics of a Mammalian Pancreatic K_ATP Channel. J Mol Biol 434 19:e167789. PubMed Id: 35964676. doi:10.1016/j.jmb.2022.167789.
SUR1/Kir6.2 pancreatic ATP-sensitive K⁺ channel, Q52R mutant, with bound PIP2, open conformation, NBD2 modeled: Mesocricetus auratus/Rattus norvegicus E Eukaryota (expressed in C. aethiops), 3.28 Å cryo-EM structure NBD2 not modeled, 2.90 Å: 8TI1	8TI2	Data File Jmol Viewer 8TI2 8TI1	Driggers et al. (2024). Driggers CM, Kuo YY, Zhu P, ElSheikh A, & Shyng SL (2024). Structure of an open KATP channel reveals tandem PIP2 binding sites mediating the Kir6.2 and SUR1 regulatory interface. Nat Commun 15 1:2502. PubMed Id: 38509107. doi:10.1038/s41467-024-46751-5.
*SUR1/Kir6.2 pancreatic ATP-sensitive K⁺ channel: Mesocricetus auratus/Mus musculus* E Eukaryota (expressed in HEK293 cells), 5.6 Å** cryo-EM structure Chimeric protein, SUR1 is from golden hamster (M. auratus) and Kir6.2 from mouse (M. musculus).	5WUA	Data File Jmol Viewer 5WUA	Li et al. (2017). Li N, Wu JX, Ding D, Cheng J, Gao N, & Chen L (2017). Structure of a Pancreatic ATP-Sensitive Potassium Channel. Cell 168 :101-110.e10. PubMed Id: 28086082. doi:10.1016/j.cell.2016.12.028.
*SUR1/Kir6.2 pancreatic ATP-sensitive K⁺ channel with bound bound with ATPγS: Mesocricetus auratus/Mus musculus* E Eukaryota (expressed in HEK293 cells), 4.4 Å** cryo-EM structure with bound glibenclamide and ATPγS (focused refinement on TM) 4.11 Å: 5YKE 3D class1, 4.33 Å: 5YKF 3D class 2, 4.57 Å: 5YKG focused refinement on SUR1, 4.4 Å: 5YW7 with bound ATPγS, 5 Å: 5YW9 bound with ATPγS (CTD class 2), 6.1 Å: 5YWA with bound with Mg-ADP (CTD class1), 4.3 Å: 5YWC with Mg-ADP (CTD class2), 5.2 Å: 5YWB with Mg-ADP (focused refinement of SUR1), 4.22 Å: 5YWD	5YW8	Data File Jmol Viewer 5YW8 5YW7 5YKE 5YKG 5YWB 5YW9 5YWC 5YWD 5YWA 5YKF	Wu et al. (2018). Wu JX, Ding D, Wang M, Kang Y, Zeng X, & Chen L (2018). Ligand binding and conformational changes of SUR1 subunit in pancreatic ATP-sensitive potassium channels. Protein Cell 9 6:553-567. PubMed Id: 29594720. doi:10.1007/s13238-018-0530-y.
*SUR1/Kir6.2 pancreatic ATP-sensitive K⁺ channel with bound repaglinide: Mesocricetus auratus/Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.3 Å** cryo-EM structure Chimeric protein, SUR1 is from golden hamster (M. auratus) and Kir6.2 from mouse (M. musculus) SUR1 TM region, 3.5 Å: 6JB3	6JB1	Data File Jmol Viewer 6JB1 6JB3	Ding et al. (2019). Ding D, Wang M, Wu JX, Kang Y, & Chen L (2019). The Structural Basis for the Binding of Repaglinide to the Pancreatic K_ATP Channel. Cell Rep 27 6:1848-1857.e4. PubMed Id: 31067468. doi:10.1016/j.celrep.2019.04.050.
*SUR1/Kir6.2 pancreatic ATP-sensitive K⁺ channel H175K mutant, pre-open state: Mesocricetus auratus/Mus musculus* E Eukaryota (expressed in HEK293 cells), 2.96 Å** cryo-EM structure closed state, 3.19 Å 7W4P	7W4O	Data File Jmol Viewer 7W4O 7W4P	Wang et al. (2022). Wang M, Wu JX, Ding D, & Chen L (2022). Structural insights into the mechanism of pancreatic K_ATP channel regulation by nucleotides. Nat Commun 13 1:2770. PubMed Id: 35589716. doi:10.1038/s41467-022-30430-4.
*SUR1/Kir6.2 pancreatic ATP-sensitive K⁺ channel, bound to ATP and ADP in quatrefoil form: Homo sapiens* E Eukaryota (expressed in HEK293S cells), 3.9 Å** cryo-EM structure bound to ATP and ADP in propeller form, 5.6 Å: 6C3P	6C3O	Data File Jmol Viewer 6C3O 6C3P	Lee et al. (2017). Lee KPK, Chen J, & MacKinnon R (2017). Molecular structure of human KATP in complex with ATP and ADP. Elife 6 :e32481. PubMed Id: 29286281. doi:10.7554/eLife.32481.
*K_ATP channel in open conformation, focused on Kir (C166S G334D double mutant) and SUR TMD0: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure open conformation, focused on SUR, 3.30 Å 7S5V open conformation, focused on Kir and one SUR, position 1, 3.70 Å 7S5X open conformation, focused on Kir and one SUR, position 2, 3.90 Å 7S5Y open conformation, focused on Kir and one SUR, position 3, 3.90 Å 7S5Z open conformation, focused on Kir and one SUR, position 4, 3.70 Å 7S60 open conformation, focused on Kir and one SUR, position 5, 4.00 Å 7S61	7S5T	Data File Jmol Viewer 7S5T 7S60 7S5Z 7S61 7S5V 7S5Y 7S5X	Zhao & MacKinnon (2021). Zhao C, & MacKinnon R (2021). Molecular structure of an open human KATP channel. Proc Natl Acad Sci U S A 118 48:e2112267118. PubMed Id: 34815345. doi:10.1073/pnas.2112267118.
*NaK channel (Na⁺complex): Bacillus cereus* B Bacteria (expressed in E. coli), 2.4 Å** K⁺ complex, 2.8 Å: 2AHZ.	2AHY	Data File Jmol Viewer 2AHY 2AHZ NaK channel, Na+ complex	Shi et al. (2006). Shi N, Ye S, Alam A, Chen L, & Jiang Y (2006). Atomic structure of a Na+- and K+-conducting channel. Nature 440 :570-574. PubMed Id: 16467789.
*NaK channel with bound calcium, D66A mutant: Bacillus cereus* B Bacteria (expressed in E. coli), 2.30 Å** D66A/S70E mutant, 2.50 Å: 2Q68. D66N mutant, 2.40 Å: 2Q69. D66E mutant, 2.60 Å: 2Q6A.	2Q67	Data File Jmol Viewer 2Q67 2Q6A 2Q69 2Q68	Alam et al. (2007). Alam A, Shi N, & Jiang Y (2007). Structural insight into Ca2+ specificity in tetrameric cation channels. Proc Natl Acad Sci USA 104 :15334-15339. PubMed Id: 17878296.
*NaK channel in open state (NΔ19 mutant): Bacillus cereus* B Bacteria (expressed in E. coli), 1.60 Å**	3E86	Data File Jmol Viewer 3E86	Alam & Jiang (2009). Alam A & Jiang Y (2009). High-resolution structure of the open NaK channel. Nat Struct Mol Biol 16 :30-34. PubMed Id: 19098917.
*CNG-mimicking NaK channel mutant; NaK-ETPP/K⁺ complex: Bacillus cereus* B Bacteria (expressed in E. coli), 1.95 Å** CNG-mimicking mutant; NaK-NTPP/K⁺ complex, 1.58 Å: 3K06 CNG-mimicking mutant; NaK-ETPP/Na⁺ complex, 1.95 Å: 3K0G CNG-mimicking mutant; NaK-DTPP/Na⁺ complex, 1.58 Å: 3K04 CNG-mimicking mutant; NaK-NTPP/Na⁺ complex, 1.62 Å: 3K08	3K0D	Data File Jmol Viewer 3K0D 3K08 3K0G 3K04 3K06	Derebe et al. (2011). Derebe MG, Zeng W, Li Y, Alam A, & Jiang Y (2011). Structural studies of ion permeation and Ca²⁺blockage of a bacterial channel mimicking the cyclic nucleotide-gated channel pore. Proc Natl Acad Sci USA 108 :592-597. PubMed Id: 21187429.
*NaK channel; K⁺ selective mutant (NaK2K): Bacillus cereus* B Bacteria (expressed in E. coli), 1.55 Å** CNG-mimicking mutant; NaK-DTPP/K⁺ complex, 1.62 Å: 3K03 MthK channel T59A mutant, 1.75 Å: 3OUS	3OUF	Data File Jmol Viewer 3OUF 3K03 3OUS	Derebe et al. (2011). Derebe MG, Sauer DB, Zeng W, Alam A, Shi N, & Jiang Y (2011). Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites. Proc Natl Acad Sci USA 108 :598-602. PubMed Id: 21187421.
*NaK/NaK2K channel mutants; NaK-D66Y: Bacillus cereus* B Bacteria (expressed in E. coli), 1.80 Å** NaK-N68D, 1.95 Å: 3T2M NaK2K-Y66F, 1.90 Å: 3TET NaK2K-Y55W, 1.90 Å: 3T4Z NaK2K-Y55F, 1.70 Å: 3T4D NaK2K-D68E, 1.75 Å: 3TCU	3T1C	Data File Jmol Viewer 3T1C 3T4Z 3TCU 3T2M 3TET 3T4D	Sauer et al. (2011). Sauer DB, Zeng W, Raghunathan S, & Jiang Y (2011). Protein interactions central to stabilizing the K⁺ channel selectivity filter in a four-sited configuration for selective K⁺ permeation. Proc Natl Acad Sci USA 108 :16634-16639. PubMed Id: 21933962. doi:10.1073/pnas.1111688108.
*NaK channel: Bacillus cereus* B Bacteria (expressed in E. coli), 1.53 Å**	6V8Y	Data File Jmol Viewer 6V8Y	Roy et al. (2021). Roy RN, Hendriks K, Kopec W, Abdolvand S, Weiss KL, de Groot BL, Lange A, Sun H, & Coates L (2021). Structural plasticity of the selectivity filter in a nonselective ion channel. IUCrJ 8 :421-430. PubMed Id: 33953928. doi:10.1107/S205225252100213X.
*NaK channel chimera with grafted C-terminal region of a NaV channel: Bacillus weihenstephanensis (NaK) and Sulfitobacter pontiacus (NaV)* B Bacteria (expressed in E. coli), 3.20 Å** The NaVSulP C-terminal region grafted onto the C-terminus of NaK forms a four-helix bundle.	3VOU	Data File Jmol Viewer 3VOU	Irie et al. (2012). Irie K, Shimomura T, & Fujiyoshi Y (2012). The C-terminal helical bundle of the tetrameric prokaryotic sodium channel accelerates the inactivation rate. Nature Commun 3 :793. PubMed Id: 22531178. doi:10.1038/ncomms1797.
*Voltage-Gated Sodium Channel (Na_V), I217C mutant: Arcobacter butzleri* B Bacteria (expressed in Trichoplusia ni), 2.70 Å** Na_VAb is the first structure of a voltage-dependent sodium channel. It is a member of the NaChBac family. I217C mutant, 2.80 Å: 3RVZ M221C mutant, 2.95 Å: 3RW0	3RVY	Data File Jmol Viewer 3RVY 3RW0 3RVZ	Payandeh et al. (2011). Payandeh J, Scheuer T, Zheng N, & Catterall WA (2011). The crystal structure of a voltage-gated sodium channel. Nature 475 :353-358. PubMed Id: 21743477. doi:10.1038/nature10238.
*Voltage-Gated Sodium Channel (Na_V), wild-type: Arcobacter butzleri* B Bacteria (expressed in Trichoplusia ni), 3.21 Å** Shows channel in two potentially inactivated states.	4EKW	Data File Jmol Viewer 4EKW	Payandeh et al. (2012). Payandeh J, Gamal El-Din TM, Scheuer T, Zheng N, & Catterall WA (2012). Crystal structure of a voltage-gated sodium channel in two potentially inactivated states. Nature 486 :135-139. PubMed Id: 22678296. doi:10.1038/nature11077.
*Voltage-Gated Sodium Channel (Na_V) in closed state (Na_VAb/FY): Arcobacter butzleri* B Bacteria (expressed in Trichoplusia ni), 3.2 Å** in open state (Na_VAb/1-226), 2.85 Å: 5VB8	5VB2	Data File Jmol Viewer 5VB2 5VB8	Lenaeus et al. (2017). Lenaeus MJ, Gamal El-Din TM, Ing C, Ramanadane K, Pomès R, Zheng N, & Catterall WA (2017). Structures of closed and open states of a voltage-gated sodium channel. Proc Natl Acad Sci USA 114 :E3051-E3060. PubMed Id: 28348242. doi:10.1073/pnas.1700761114.
*Voltage-Gated Sodium Channel (Na_V) R3G mutant: Arcobacter butzleri* B Bacteria (expressed in Trichoplusia ni), 2.52 Å** R2G mutant+guanidinium, 2.7 Å: 6C1K R2G+methylguanidinium, 2.52 Å: 6C1M R2G mutant, 2.9 Å: 6C1P	6C1E	Data File Jmol Viewer 6C1E 6C1K 6C1M 6C1P	Jiang et al. (2018). Jiang D, Gamal El-Din TM, Ing C, Lu P, Pomès R, Zheng N, & Catterall WA (2018). Structural basis for gating pore current in periodic paralysis. Nature 557 7706:590-594. PubMed Id: 29769724. doi:10.1038/s41586-018-0120-4.
*Voltage-Gated Sodium Channel (Na_V), residues 1-239: Arcobacter butzleri* B Bacteria (expressed in Trichoplusia ni), 2.4 Å** T206A mutant, 2.6 Å: 6MWB T206S mutant, 2.33 Å: 6MWD T206V mutant, 2.50 Å: 6MWG	6MWA	Data File Jmol Viewer 6MWA 6MWD 6MWG 6MWB	Gamal El-Din et al. (2019). Gamal El-Din TM, Lenaeus MJ, Ramanadane K, Zheng N, & Catterall WA (2019). Molecular dissection of multiphase inactivation of the bacterial sodium channel Na_VAb. J Gen Physiol 151 2:174-185. PubMed Id: 30510035. doi:10.1085/jgp.201711884.
*Voltage-Gated Sodium Channel (Na_V), I217C/F203A mutant: Arcobacter butzleri* B Bacteria (expressed in Trichoplusia ni), 2.9 Å** I217C/F203W mutant, 3.20 Å: 6MVW I217C mutant in complex with flecainide, 3.46 Å: 6MVX residues 1-126 in complex with lidocaine, 3.00 Å: 6MVY	6MVV	Data File Jmol Viewer 6MVV 6MVW 6MVX 6MVY	Gamal El-Din et al. (2018). Gamal El-Din TM, Lenaeus MJ, Zheng N, & Catterall WA (2018). Fenestrations control resting-state block of a voltage-gated sodium channel. Proc Natl Acad Sci USA 115 51:13111-13116. PubMed Id: 30518562. doi:10.1073/pnas.1814928115.
*Voltage-Gated Sodium Channel (Na_V), G94C/Q150C mutant in the activated state: Arcobacter butzleri* B Bacteria (expressed in Trichoplusia ni)), 2.75 Å** V100C/Q150C disulfide cross-linked mutant in the activated state, 2.89 Å: 6P6Y N49K/L109A/M116V/G94C/Q150C disulfide cross-linked mutant in the resting state, 4 Å: 6P6W	6P6X	Data File Jmol Viewer 6P6X 6P6Y 6P6W	Wisedchaisri et al. (2019). Wisedchaisri G, Tonggu L, McCord E, Gamal El-Din TM, Wang L, Zheng N, & Catterall WA (2019). Resting-State Structure and Gating Mechanism of a Voltage-Gated Sodium Channel. Cell 178 4:993-1003.e12. PubMed Id: 31353218. doi:10.1016/j.cell.2019.06.031.
*Na_x channel in complex with β₃ subunit in nanodisc: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure in glyco-diosgenin (GDN), 2.90 Å	7TJ8	Data File Jmol Viewer 7TJ8	Noland et al. (2022). Noland CL, Chua HC, Kschonsak M, Heusser SA, Braun N, Chang T, Tam C, Tang J, Arthur CP, Ciferri C, Pless SA, & Payandeh J (2022). Structure-guided unlocking of Na_X reveals a non-selective tetrodotoxin-sensitive cation channel. Nat Commun 13 1:1416. PubMed Id: 35301303. doi:10.1038/s41467-022-28984-4.
*NaChBac voltage-gated Na⁺ (Na_V) channel in glyo-diosgenin (GDN) detergent: Bacillus halodurans* B Bacteria (expressed in E. coli), 3.70 Å** cryo-EM structure in nanodiscs, 3.10 Å: 6VWX NaChBac-Na_V1.7VSD_II chimera in nanodiscs, 3.50 Å: 6VXO NaChBac-Na_V1.7VSD_II in complex with HWTX-VI, 3.20 Å: 6W6O	6VX3	Data File Jmol Viewer 6VX3 6VXO 6W6O 6VWX	Gao et al. (2020). Gao S, Valinsky WC, On NC, Houlihan PR, Qu Q, Liu L, Pan X, Clapham DE, & Yan N (2020). Employing NaChBac for cryo-EM analysis of toxin action on voltage-gated Na⁺ channels in nanodisc. Proc Natl Acad Sci USA 117 25:14187-14193. PubMed Id: 32513729. doi:10.1073/pnas.1922903117.
*Voltage-Gated Sodium Channel (Na_V): Alpha proteobacterium himb114 (Rickettsiales sp. HIMB114)* B Bacteria (expressed in E. coli), 3.05 Å** Structure is probably of the channel in an inactivated state.	4DXW	Data File Jmol Viewer 4DXW	Zhang et al. (2012). Zhang X, Ren W, DeCaen P, Yan C, Tao X, Tang L, Wang J, Hasegawa K, Kumasaka T, He J, Wang J, Clapham DE, & Yan N (2012). Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel. Nature 486 :130-134. PubMed Id: 22678295.
*Voltage-Gated Sodium Channel (Na_V): Magnetococcus marinus* B Bacteria (expressed in E. coli), 3.49 Å** Shows channel in an open conformation.	4F4L	Data File Jmol Viewer 4F4L	McCusker et al. (2012). McCusker EC, Bagnéris C, Naylor CE, Cole AR, D'Avanzo N, Nichols CG, & Wallace BA (2012). Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing. Nat Commun 3 :1102. PubMed Id: 23033078. doi:10.1038/ncomms2077.
*Voltage-Gated Sodium Channel (Na_V), complete structure with C-terminal domain: Magnetococcus marinus* B Bacteria (expressed in E. coli), 2.92 Å**	3ZJZ	Data File Jmol Viewer 3ZJZ	Bagnéris et al. (2013). Bagnéris C, Decaen PG, Hall BA, Naylor CE, Clapham DE, Kay CW, & Wallace BA (2013). Role of the C-terminal domain in the structure and function of tetrameric sodium channels. Nat Commun 4 :2465. PubMed Id: 24051986. doi:10.1038/ncomms3465.
*Voltage-Gated Sodium Channel (Na_V), apo open form: Magnetococcus marinus* B Bacteria (expressed in E. coli), 2.66 Å** Wild-type with Pl1 blocker by soaking crystal, 2.89 Å: 4P9O Wild-type with Pl1 blocker co-crystallized, 3.43 Å: 4PA9 T207A/F214A apo mutant, 3.08 Å: 4P2Z T207A/F214A mutant with bound Pl1, 3.31 Å: 4P30 Wild-type with bound Pl2 blocker, 2.80 Å: 4OXS Wild-type with bound Pl3 blocker, 3.25 Å: 4PA3 Wild-type with bound Pl4 blocker, 3.02 Å: 4PA4 Wild-type with bound Pl5 blocker, 2.91 Å: 4P9P Wild-type with bound Pl6 blocker, 3.36 Å: 4PA6 Wild-type with bound Pl7 blocker, 3.02 Å: 4PA7	4CBC	Data File Jmol Viewer 4CBC 4P9O 4PA9 4OXS 4PA7 4PA4 4P30 4PA3 4PA6 4P9P 4P2Z	Bagnéris et al. (2014). Bagnéris C, DeCaen PG, Naylor CE, Pryde DC, Nobeli I, Clapham DE, & Wallace BA (2014). Prokaryotic NavMs channel as a structural and functional model for eukaryotic sodium channel antagonism. Proc Natl Acad Sci USA 111 :8428-8433. PubMed Id: 24850863. doi:10.1073/pnas.1406855111.
*Voltage-Gated Sodium Channel (Na_V) channel pore and C-terminal domain: Magnetococcus marinus* B Bacteria (expressed in E. coli), 2.7 Å** E178D selectivity-filter mutant, 3.5 Å: 4X88	5BZB	Data File Jmol Viewer 5BZB 4X88	Naylor et al. (2016). Naylor CE, Bagnéris C, DeCaen PG, Sula A, Scaglione A, Clapham DE, & Wallace BA (2016). Molecular basis of ion permeability in a voltage-gated sodium channel. EMBO J 35 :820-830. PubMed Id: 26873592. doi:10.15252/embj.201593285.
*Voltage-Gated Sodium Channel (Na_V), full length in activated open state: Magnetococcus marinus* B Bacteria (expressed in E. coli), 2.45 Å** I218C mutant in open form, 2.6 Å: 5HVD	5HVX	Data File Jmol Viewer 5HVX 5HVD	Sula et al. (2017). Sula A, Booker J, Ng LC, Naylor CE, DeCaen PG, & Wallace BA (2017). The complete structure of an activated open sodium channel. Nat Commun 8 . PubMed Id: 28205548. doi:10.1038/ncomms14205.
*Voltage-Gated Sodium Channel (Na_V) full length F208L mutant open-form: Magnetococcus marinus* B Bacteria (expressed in E. coli), 2.20 Å** in complex with 4-hydroxytamoxifen, 2.40 Å: 6SXG F208L mutant in complex with 4-hydroxytamoxifen, 2.50 Å: 6SXC F208L mutant in complex with Endoxifen, 2.60 Å: 6SXE F208L mutant in complex with N-desmethyltamoxifen, 3.20 Å: 6Z8C F208L mutant alone, 2.50 Å: 6SX7	6SX5	Data File Jmol Viewer 6SX5 6SXC 6SXE 6Z8C 6SX7 6SXG	Sula et al. (2021). Sula A, Hollingworth D, Ng LCT, Larmore M, DeCaen PG, & Wallace BA (2021). A tamoxifen receptor within a voltage-gated sodium channel. Mol Cell 81 6:1160-1169.e5. PubMed Id: 33503406. doi:10.1016/j.molcel.2020.12.048.
*FPC1 cockroach voltage-gated sodium channel (Na_VPaS): Periplaneta americana* E Eukaryota (expressed in HEK293F), 3.8 Å** cryo-EM structure	5X0M	Data File Jmol Viewer 5X0M	Shen et al. (2017). Shen H, Zhou Q, Pan X, Li Z, Wu J, & Yan N (2017). Structure of a eukaryotic voltage-gated sodium channel at near-atomic resolution. Science 355 :924. PubMed Id: 28183995. doi:10.1126/science.aal4326. Article summary. See Electronic Pub Id (doi) for full article
*Na_VPaS with bound Dc1a toxin from brush spider Diguetia canities: Periplaneta americana* E Eukaryota (expressed in HEK293F cells), 2.8 Å** cryo-EM structure with bound Dc1a and TTX, 2.6 Å: 6A95 with bound Dc1a and saxitoxin, 3.2 Å: 6A91	6A90	Data File Jmol Viewer 6A90 6A95 6A91	Shen et al. (2018). Shen H, Li Z, Jiang Y, Pan X, Wu J, Cristofori-Armstrong B, Smith JJ, Chin YKY, Lei J, Zhou Q, King GF, & Yan N (2018). Structural basis for the modulation of voltage-gated sodium channels by animal toxins. Science 362 6412:eaau2596. PubMed Id: 30049784. doi:10.1126/science.aau2596.
*Voltage-Gated Sodium Channel (Na_V), human/cockroach chimera: Homo sapiens/Periplaneta americana* E Eukaryota (expressed in HEK293 cells), 3.4 Å** cryo-EM structure with bound alpha-scorpion toxin AaH2, 3.5 Å: 6NT4	6NT3	Data File Jmol Viewer 6NT3 6NT4	Clairfeuille et al. (2019). Clairfeuille T, Cloake A, Infield DT, Llongueras JP, Arthur CP, Li ZR, Jian Y, Martin-Eauclaire MF, Bougis PE, Ciferri C, Ahern CA, Bosmans F, Hackos DH, Rohou A, & Payandeh J (2019). Structural basis of α-scorpion toxin action on Na_v channels. Science 363 6433. PubMed Id: 30733386. doi:10.1126/science.aav8573.
*Na_v1.1-β4 complex: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	7DTD	Data File Jmol Viewer 7DTD	Pan et al. (2021). Pan X, Li Z, Jin X, Zhao Y, Huang G, Huang X, Shen Z, Cao Y, Dong M, Lei J, & Yan N (2021). Comparative structural analysis of human Na_v1.1 and Na_v1.5 reveals mutational hotspots for sodium channelopathies. Proc Natl Acad Sci U S A 118 11:e2100066118. PubMed Id: 33712547. doi:10.1073/pnas.2100066118.
*Na_V1.2-β2 complex with bound μ-conotoxin KIIIA: Homo sapiens/Conus kinoshitai* E Eukaryota (expressed in HEK293 cells), 3 Å** cryo-EM structure	6J8E	Data File Jmol Viewer 6J8E	Pan et al. (2019). Pan X, Li Z, Huang X, Huang G, Gao S, Shen H, Liu L, Lei J, & Yan N (2019). Molecular basis for pore blockade of human Na⁺ channel Na_V1.2 by the μ-conotoxin KIIIA. Science 363 6433:1309-1313. PubMed Id: 30765605. doi:10.1126/science.aaw2999.
*Na_V1.3-β1-β2 complex with bound antagonist ICA121431: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.35 Å** cryo-EM structure with bound bulleyaconitineA, 3.30 Å 7W77	7W7F	Data File Jmol Viewer 7W7F 7W77	Li et al. (2022). Li X, Xu F, Xu H, Zhang S, Gao Y, Zhang H, Dong Y, Zheng Y, Yang B, Sun J, Zhang XC, Zhao Y, & Jiang D (2022). Structural basis for modulation of human Na_V1.3 by clinical drug and selective antagonist. Nat Commun 13 1:1286. PubMed Id: 35277491. doi:10.1038/s41467-022-28808-5.
*Na_V1.4-β₁ complex: Electrophorus electricus* E Eukaryota, 4.0 Å** cryo-EM structure	5XSY	Data File Jmol Viewer 5XSY	Yan et al. (2017). Yan Z, Zhou Q, Wang L, Wu J, Zhao Y, Huang G, Peng W, Shen H, Lei J, & Yan N (2017). Structure of the Nav1.4-β1 Complex from Electric Eel. Cell 170 :470-482.e11. PubMed Id: 28735751. doi:10.1016/j.cell.2017.06.039.
*Na_V1.4-β1 complex: Homo sapiens* E Eukaryota (expressed in sf9 cells), 3.2 Å** cryo-EM structure	6AGF	Data File Jmol Viewer 6AGF	Pan et al. (2018). Pan X, Li Z, Zhou Q, Shen H, Wu K, Huang X, Chen J, Zhang J, Zhu X, Lei J, Xiong W, Gong H, Xiao B, & Yan N (2018). Structure of the human voltage-gated sodium channel Na_v1.4 in complex with β1. Science 362 6412:eaau2486. PubMed Id: 30190309. doi:10.1126/science.aau2486.
*Na_V1.4 C-Terminal domain in complex with apo rat calmodulin: Homo sapiens* E Eukaryota (expressed in E. coli), 1.80 Å** C-Terminal (1599-1754) domain in complex with calcium-bound calmodulin, 3.3 Å: 6MC9	6MBA	Data File Jmol Viewer 6MBA 6MC9	Yoder et al. (2019). Yoder JB, Ben-Johny M, Farinelli F, Srinivasan L, Shoemaker SR, Tomaselli GF, Gabelli SB, & Amzel LM (2019). Ca²⁺-dependent regulation of sodium channels Na_V1.4 and Na_V1.5 is controlled by the post-IQ motif. Nat Commun 10 1. PubMed Id: 30944319. doi:10.1038/s41467-019-09570-7.
*Na_V1.5 cardiac sodium channel: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.5 Å** cryo-EM structure with bound flecainide, 3.24 Å: 6UZ0	6UZ3	Data File Jmol Viewer 6UZ3 6UZ0	Jiang et al. (2020). Jiang D, Shi H, Tonggu L, Gamal El-Din TM, Lenaeus MJ, Zhao Y, Yoshioka C, Zheng N, & Catterall WA (2020). Structure of the Cardiac Sodium Channel. Cell 180 1:122-134.e10. PubMed Id: 31866066. doi:10.1016/j.cell.2019.11.041.
*Na_V1.5 cardiac sodium channel with bound α-toxin LqhIII from deathstalker scorpion: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	7K18	Data File Jmol Viewer 7K18	Jiang et al. (2021). Jiang D, Tonggu L, Gamal El-Din TM, Banh R, Pomès R, Zheng N, & Catterall WA (2021). Structural basis for voltage-sensor trapping of the cardiac sodium channel by a deathstalker scorpion toxin. Nat Commun 12 1. PubMed Id: 33397917. doi:10.1038/s41467-020-20078-3.
*Na_V1.5 cardiac sodium channel, open state: Rattus norvegicus* E Eukaryota (expressed in Mammalian 1 orthobornavirus), 3.40 Å** cryo-EM structure	7FBS	Data File Jmol Viewer 7FBS	Jiang et al. (2021). Jiang D, Banh R, Gamal El-Din TM, Tonggu L, Lenaeus MJ, Pomès R, Zheng N, & Catterall WA (2021). Open-state structure and pore gating mechanism of the cardiac sodium channel. Cell 184 20:5151-5162.e11. PubMed Id: 34520724. doi:10.1016/j.cell.2021.08.021.
*Na_V1.5 cardiac sodium channel, E1784K mutant: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	7DTC	Data File Jmol Viewer 7DTC	Li et al. (2021). Li Z, Jin X, Wu T, Zhao X, Wang W, Lei J, Pan X, & Yan N (2021). Structure of human Nav1.5 reveals the fast inactivation-related segments as a mutational hotspot for the long QT syndrome. Proc Natl Acad Sci U S A 118 11:e2100069118. PubMed Id: 33712541. doi:10.1073/pnas.2100069118.
*Na_V1.6 with β1 and β2 subunits, apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure with β1 and β2-4 subunits in complex with 9-anhydro-tetrodotoxin, 3.30 Å: 8GZ2	8GZ1	Data File Jmol Viewer 8GZ1 8GZ2	Li et al. (2023). Li Y, Yuan T, Huang B, Zhou F, Peng C, Li X, Qiu Y, Yang B, Zhao Y, Huang Z, & Jiang D (2023). Structure of human NaV1.6 channel reveals Na+ selectivity and pore blockade by 4,9-anhydro-tetrodotoxin. Nat Commun 14 1:1030. PubMed Id: 36823201. doi:10.1038/s41467-023-36766-9.
*Na_V1.6 voltage-gated sodium channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure	8FHD	Data File Jmol Viewer 8FHD	Fan et al. (2023). Fan X, Huang J, Jin X, & Yan N (2023). Cryo-EM structure of human voltage-gated sodium channel Nav1.6. Proc Natl Acad Sci U S A 120 5:e2220578120. PubMed Id: 36696443. doi:10.1073/pnas.2220578120.
*Na_V1.7 VSD4 voltage dependent sodium channel: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.5 Å** Chimera: Portions of Na_V1.7 on to the bacterial (Arcobacter butzleri) channel Na_V	5EK0	Data File Jmol Viewer 5EK0	Ahuja et al. (2015). Ahuja S, Mukund S, Deng L, Khakh K, Chang E, Ho H, Shriver S, Young C, Lin S, Johnson JP Jr, Wu P, Li J, Coons M, Tam C, Brillantes B, Sampang H, Mortara K, Bowman KK, Clark KR, Estevez A, Xie Z, Verschoof H, Grimwood M, Dehnhardt C, Andrez JC, Focken T, Sutherlin DP, Safina BS, Starovasnik MA, Ortwine DF, Franke Y, Cohen CJ, Hackos DH, Koth CM, & Payandeh J (2015). Structural basis of Nav1.7 inhibition by an isoform-selective small-molecule antagonist. Science 350 6267:1491. PubMed Id: 26680203. doi:10.1126/science.aac5464.
*Na_V1.7 sodium channel voltage-sensor domain with bound ProTx2: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.54 Å** crystallographic structure. ProTx2 is from Thrixopelma pruriens Cryo-EM structures: Nav1.7 VSD2 (deactivated state) in complex with ProTx2, 4.2 Å:6N4R Nav1.7 VSD2 (activated state) in complex with ProTx2, 3.6 Å: 6N4Q	6N4I	Data File Jmol Viewer 6N4I 6N4Q 6N4R	Xu et al. (2019). Xu H, Li T, Rohou A, Arthur CP, Tzakoniati F, Wong E, Estevez A, Kugel C, Franke Y, Chen J, Ciferri C, Hackos DH, Koth CM, & Payandeh J (2019). Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin. Cell 176 4:702-715.e14. PubMed Id: 30661758. doi:10.1016/j.cell.2018.12.018.
*Na_V1.7 with β1β2 subunits in complex with huwentoxin-IV and saxitoxin (Y1755 up): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.2 Å** cryo-EM structure in complex with huwentoxin-IV and saxitoxin (Y1755 down), 3.2 Å: 6J8H in complex with ProTx-II and tetrodotoxin (Y1755 up), 3.2 Å: 6J8I in complex with ProTx-II and tetrodotoxin (Y1755 down), 3.2 Å: 6J8J	6J8G	Data File Jmol Viewer 6J8G 6J8I 6J8H 6J8J	Shen et al. (2019). Shen H, Liu D, Wu K, Lei J, & Yan N (2019). Structures of human Na_V1.7 channel in complex with auxiliary subunits and animal toxins. Science 363 6433:1303-1308. PubMed Id: 30765606. doi:10.1126/science.aaw2493.
*Na_V1.7/Na_VAb chimera-VS2A chimera trapped in the resting state by tarantula toxin: Homo sapiens/Arcobacter butzleri* E Eukaryota (expressed in Trichoplusia ni), 3.60 Å** cryo-EM structure	7K48	Data File Jmol Viewer 7K48	Wisedchaisri et al. (2021). Wisedchaisri G, Tonggu L, Gamal El-Din TM, McCord E, Zheng N, & Catterall WA (2021). Structural Basis for High-Affinity Trapping of the Na_V1.7 Channel in Its Resting State by Tarantula Toxin. Mol Cell 81 1:38-48.e4. PubMed Id: 33232657. doi:10.1016/j.molcel.2020.10.039.
*Na_V1.7/β1/β2 VSD4 voltage dependent sodium channel with XEN907: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.22 Å** cryo-EM structure with TCN, 3.07 Å: 7XMF with TCN-1752, 3.09 Å: 7XMG	7XM9	Data File Jmol Viewer 7XM9 7XMF 7XMG	Zhang et al. (2022). Zhang J, Shi Y, Huang Z, Li Y, Yang B, Gong J, & Jiang D (2022). Structural basis for Na_V1.7 inhibition by pore blockers. Nat Struct Mol Biol 29 12:1208-1216. PubMed Id: 36424527. doi:10.1038/s41594-022-00860-1.
*Na_v1.7 voltage-gated sodium channel, with bound CBD: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.80 Å** cryo-EM structure	8G1A	Data File Jmol Viewer 8G1A	Huang et al. (2023). Huang J, Fan X, Jin X, Jo S, Zhang HB, Fujita A, Bean BP, & Yan N (2023). Cannabidiol inhibits Nav channels through two distinct binding sites. Nat Commun 14 1:3613. PubMed Id: 37330538. doi:10.1038/s41467-023-39307-6.
*Na_V1.7 VSD4 voltage dependent sodium channel with bound bupivacaine: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.70 Å** cryo-EM structure with bound PF-05089771, 2.70 Å: 8I5G with bound vinpocetine, 2.90 Å: 8I5X with bound vixotrigine, 2.60 Å: 8I5Y with bound hardwickiic acid, 3.00 Å: 8J4F with bound lacosamide, 2.90 Å: 8S9B with bound carbamazepine, 3.20 Å: 8S9C	8I5B	Data File Jmol Viewer 8I5B 8S9B 8J4F 8I5X 8I5Y 8I5G 8S9C	Wu et al. (2023). Wu Q, Huang J, Fan X, Wang K, Jin X, Huang G, Li J, Pan X, & Yan N (2023). Structural mapping of Nav1.7 antagonists. Nat Commun 14 1:3224. PubMed Id: 37270609. doi:10.1038/s41467-023-38942-3.
*Na_V1.7 VSD4 voltage dependent sodium channel, with bound riluzole: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure with bound lamotrigine, 2.70 Å: 8THH	8THG	Data File Jmol Viewer 8THG 8THH	Huang et al. (2023). Huang J, Fan X, Jin X, Teng L, & Yan N (2023). Dual-pocket inhibition of Nav channels by the antiepileptic drug lamotrigine. Proc Natl Acad Sci U S A 120 41:e2309773120. PubMed Id: 37782796. doi:10.1073/pnas.2309773120.
*Na_v1.8 with A-803467, class I: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.70 Å** cryo-EM structure with A-803467, class II, 3.20 Å: 7WEL with A-803467, class III, 3.00 Å: 7WFR Apo Na_v1.8, 3.10 Å: 7WFW	7WE4	Data File Jmol Viewer 7WE4 7WFW 7WEL 7WFR	Huang et al. (2022). Huang X, Jin X, Huang G, Huang J, Wu T, Li Z, Chen J, Kong F, Pan X, & Yan N (2022). Structural basis for high-voltage activation and subtype-specific inhibition of human Na_v1.8. Proc Natl Acad Sci U S A 119 30:e220821119. PubMed Id: 35858452. doi:10.1073/pnas.2208211119.
*Na_VAe1p pore-only volt-gated sodium channel (crystal I; I222 space group; high Ca²⁺): Alkalilimnicola ehrlichii* B Bacteria (expressed in E. coli), 3.46 Å** crystal II, high Ca²⁺, 3.80 Å: 4LTP P4₂ space group, low Ca²⁺, 5.50 Å: 4LTQ H245G mutant, 5.80 Å: 4LTR	4LTO	Data File Jmol Viewer 4LTO 4LTP 4LTR 4LTQ	Shaya et al. (2014). Shaya D, Findeisen F, Abderemane-Ali F, Arrigoni C, Wong S, Nurva SR, Loussouarn G, & Minor DL Jr (2014). Structure of a Prokaryotic Sodium Channel Pore Reveals Essential Gating Elements and an Outer Ion Binding Site Common to Eukaryotic Channels. J Mol Biol 426 :467-483. PubMed Id: 24120938. doi:10.1016/j.jmb.2013.10.010.
*Voltage-sensing domain of a voltage-sensitive phosphatase (R217E mutant): Ciona intestinalis* E Eukaryota (expressed in E. coli), 2.50 Å** R217E mutant, 2.80 Å: 4G7Y wild-type, 3.58 Å: 4G80	4G7V	Data File Jmol Viewer 4G7V 4G7Y 4G80	Li et al. (2014). Li Q, Wanderling S, Paduch M, Medovoy D, Singharoy A, McGreevy R, Villalba-Galea CA, Hulse RE, Roux B, Schulten K, Kossiakoff A, & Perozo E (2014). Structural mechanism of voltage-dependent gating in an isolated voltage-sensing domain. Nat Struct Mol Biol 21 :244-252. PubMed Id: 24487958. doi:10.1038/nsmb.2768.
*Hv1 chimeric (VSOP/Hv1) voltage-gated proton channel: Mus musculus* E Eukaryota (expressed in S. frugiperda), 3.45 Å**	3WKV	Data File Jmol Viewer 3WKV	Takeshita et al. (2014). Takeshita K, Sakata S, Yamashita E, Fujiwara Y, Kawanabe A, Kurokawa T, Okochi Y, Matsuda M, Narita H, Okamura Y, & Nakagawa A (2014). X-ray crystal structure of voltage-gated proton channel. Nat Struct Mol Biol 21 :352-357. PubMed Id: 24584463. doi:10.1038/nsmb.2783.
*Hv1 voltage-gated proton channel: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure**	5OQK	Data File Jmol Viewer 5OQK	Bayrhuber et al. (2019). Bayrhuber M, Maslennikov I, Kwiatkowski W, Sobol A, Wierschem C, Eichmann C, Frey L, & Riek R (2019). Nuclear Magnetic Resonance Solution Structure and Functional Behavior of the Human Proton Channel. Biochemistry 58 39:4017-4027. PubMed Id: 31365236. doi:10.1021/acs.biochem.9b00471.
*Trimeric intracellular cation (TRIC) channel orthologue: Saccharolobus solfataricus* B Bacteria (expressed in E. coli), 2.64 Å**	5H35	Data File Jmol Viewer 5H35	Kasuya et al. (2016). Kasuya G, Hiraizumi M, Maturana AD, Kumazaki K, Fujiwara Y, Liu K, Nakada-Nakura Y, Iwata S, Tsukada K, Komori T, Uemura S, Goto Y, Nakane T, Takemoto M, Kato HE, Yamashita K, Wada M, Ito K, Ishitani R, Hattori M, & Nureki O (2016). Crystal structures of the TRIC trimeric intracellular cation channel orthologues. Cell Res 26 12:1288-1301. PubMed Id: 27909292. doi:10.1038/cr.2016.140.
*Trimeric intracellular cation (TRIC) channel orthologue: Rhodobacter sphaeroides* B Bacteria (expressed in E. coli), 3.41 Å**	5H36	Data File Jmol Viewer 5H36	Kasuya et al. (2016). Kasuya G, Hiraizumi M, Maturana AD, Kumazaki K, Fujiwara Y, Liu K, Nakada-Nakura Y, Iwata S, Tsukada K, Komori T, Uemura S, Goto Y, Nakane T, Takemoto M, Kato HE, Yamashita K, Wada M, Ito K, Ishitani R, Hattori M, & Nureki O (2016). Crystal structures of the TRIC trimeric intracellular cation channel orthologues. Cell Res 26 12:1288-1301. PubMed Id: 27909292. doi:10.1038/cr.2016.140.
*Trimeric intracellular cation (TRIC) channel, B1 isoform with bound Ca²⁺: Caenorhabditis elegans* E Eukaryota (expressed in Komagataella pastoris), 3.3 Å** B2 isoform in absence of Ca²⁺, 2.3 Å: 5EIK	5EGI	Data File Jmol Viewer 5EGI 5EIK	Yang et al. (2016). Yang H, Hu M, Guo J, Ou X, Cai T, & Liu Z (2016). Pore architecture of TRIC channels and insights into their gating mechanism. Nature 538 :537-541. PubMed Id: 27698420. doi:10.1038/nature19767.
*Trimeric intracellular cation (TRIC) channel, type 2a crystal: Sulfolobus acidocaldarius* B Bacteria (expressed in E. coli), 1.6 Å** type 2b crystal, 1.90 Å: 5WUD type 3 crystal, 2.40 Å: 5WUE	5WUC	Data File Jmol Viewer 5WUC 5WUE 5WUD	Su et al. (2017). Su M, Gao F, Yuan Q, Mao Y, Li DL, Guo Y, Yang C, Wang XH, Bruni R, Kloss B, Zhao H, Zeng Y, Zhang FB, Marks AR, Hendrickson WA, & Chen YH (2017). Structural basis for conductance through TRIC cation channels. Nat Commun 8 :15103. PubMed Id: 28524849. doi:10.1038/ncomms15103.
*Trimeric intracellular cation (TRIC) channel: Colwellia psychrerythraea* B Bacteria (expressed in E. coli), 2.40 Å**	5WUF	Data File Jmol Viewer 5WUF	Su et al. (2017). Su M, Gao F, Yuan Q, Mao Y, Li DL, Guo Y, Yang C, Wang XH, Bruni R, Kloss B, Zhao H, Zeng Y, Zhang FB, Marks AR, Hendrickson WA, & Chen YH (2017). Structural basis for conductance through TRIC cation channels. Nat Commun 8 :15103. PubMed Id: 28524849. doi:10.1038/ncomms15103.
*Trimeric intracellular cation (TRIC) channel: Saccharolobus solfataricus* A Archaea (expressed in E. coli), 2.2 Å**	5WTR	Data File Jmol Viewer 5WTR	Ou et al. (2017). Ou X, Guo J, Wang L, Yang H, Liu X, Sun J, & Liu Z (2017). Ion- and water-binding sites inside an occluded hourglass pore of a trimeric intracellular cation (TRIC) channel. BMC Biol 15 1. PubMed Id: 28431535. doi:10.1186/s12915-017-0372-8.
*Trimeric intracellular cation (TRIC) channel, TRIC-A subtype, SeMet protein: Gallus gallus* E Eukaryota (expressed in Schizosaccharomyces pombe), 2.20 Å** native protein with bound Ca²⁺ (12 KeV data), 1.8 Å: 6IYX native protein with bound Ca²⁺ (7 KeV data), 2.0 Å: 6IZF native protein, Ca²⁺-free, 2.2 Å: 6IYZ K129A mutant with bound Ca²⁺, 2.3 Å: 6IZ0 K129Q mutant with bound Ca²⁺, 2.4 Å: 6IZ1	6IYU	Data File Jmol Viewer 6IYU 6IZ1 6IYX 6IZF 6IYZ 6IZ0	Wang et al. (2019). Wang XH, Su M, Gao F, Xie W, Zeng Y, Li DL, Liu XL, Zhao H, Qin L, Li F, Liu Q, Clarke OB, Lam SM, Shui GH, Hendrickson WA, & Chen YH (2019). Structural basis for activity of TRIC counter-ion channels in calcium release. Proc Natl Acad Sci USA 116 :4283-4243. PubMed Id: 30770441. doi:10.1073/pnas.1817271116.
*Trimeric intracellular cation (TRIC) channel, TRIC-B subtype, Ca²⁺-free, cubic (7 KeV data): Xenopus laevis* E Eukaryota (expressed in Schizosaccharomyces pombe), 3.70 Å** Ca²⁺-free trigonal (7 KeV data), 3.8 Å: 3.79 Å: 6IZ3 Ca²⁺-free tetrahedral, 3.10 Å: 6IZ4 with bound Ca²⁺ cubic (7 KeV data), 3.29 Å: 6IZ6	6IZ5	Data File Jmol Viewer 6IZ5 6IZ4 6IZ6 6IZ3	Wang et al. (2019). Wang XH, Su M, Gao F, Xie W, Zeng Y, Li DL, Liu XL, Zhao H, Qin L, Li F, Liu Q, Clarke OB, Lam SM, Shui GH, Hendrickson WA, & Chen YH (2019). Structural basis for activity of TRIC counter-ion channels in calcium release. Proc Natl Acad Sci USA 116 :4283-4243. PubMed Id: 30770441. doi:10.1073/pnas.1817271116.
*MlotK1 cyclic nucleotide-regulated K⁺-channel: Mesorhizobium loti* B Bacteria (expressed in E. coli), 3.1 Å**	3BEH	Data File Jmol Viewer 3BEH	Clayton et al. (2008). Clayton GM, Altieri S, Heginbotham L, Unger VM, & Morais-Cabral JH (2008). Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel. Proc Natl Acad Sci U S A 105 :1511-1515. PubMed Id: 18216238.
*MlotK1 cyclic nucleotide-regulated K⁺-channel, complete structure: Mesorhizobium loti* B Bacteria (expressed in E. coli), 4.5 Å** cryo-EM structure	6EO1	Data File Jmol Viewer 6EO1	Kowal et al. (2018). Kowal J, Biyani N, Chami M, Scherer S, Rzepiela AJ, Baumgartner P, Upadhyay V, Nimigean CM, & Stahlberg H (2018). High-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MloK1 in a Lipid Bilayer. Structure 26 :20-27.e3. PubMed Id: 29249605. doi:10.1016/j.str.2017.11.012.
*MlotK1 cyclic nucleotide-regulated K⁺-channel, complete structure: Mesorhizobium japonicum* B Bacteria (expressed in E. coli), 4 Å** cryo-EM structure from 2D crystals class 1 (extended conformation), 5.2 Å: 6IAX class 2 (intermediate conformation), 4.7 Å: 6CQY class 3 (intermediate extended conformation), 4.4 Å: 6QCZ class 4 (compact/open conformation), 4.5 Å: 6QD0 class 5 (intermediate compact conformation), 5.4 Å: 6QD1 class 6 (intermediate compact conformation), 4.8 Å: 6QD2 class 7 (intermediate conformation), 5 Å: 6QD3 class 8 (intermediate conformation), 5.6 Å: 6QD4	6I9D	Data File Jmol Viewer 6I9D 6QCZ 6CQY 6QD1 6IAX 6QD0 6QD2 6QD3 6QD4	Righetto et al. (2019). Righetto RD, Biyani N, Kowal J, Chami M, & Stahlberg H (2019). Retrieving high-resolution information from disordered 2D crystals by single-particle cryo-EM. Nat Commun 10 1:1722. PubMed Id: 30979902. doi:10.1038/s41467-019-09661-5.
*Cyclic-nucleotide-gated (CNG) channel TAX-4, liganded open state: Caenorhabditis elegans* E Eukaryota (expressed in Trichoplusia ni), 3.5 Å** cryo-EM structure.	5H3O	Data File Jmol Viewer 5H3O	Li et al. (2017). Li M, Zhou X, Wang S, Michailidis I, Gong Y, Su D, Li H, Li X, & Yang J (2017). Structure of a eukaryotic cyclic-nucleotide-gated channel. Nature 7639:60-65. PubMed Id: 28099415. doi:10.1038/nature20819.
*Cyclic-nucleotide-gated (CNG) channel TAX-4 in lipid nanodiscs, cGMP-unbound: Caenorhabditis elegans* E Eukaryota (expressed in Spodoptera frugiperda), 2.60 Å** cryo-EM structure cGMP-bound, 2.70 Å: 6WEK cGMP-unbound, F403V/V407A mutant, 2.50 Å: 6WEL	6WEJ	Data File Jmol Viewer 6WEJ 6WEL 6WEK	Zheng et al. (2020). Zheng X, Fu Z, Su D, Zhang Y, Li M, Pan Y, Li H, Li S, Grassucci RA, Ren Z, Hu Z, Li X, Zhou M, Li G, Frank J, & Yang J (2020). Mechanism of ligand activation of a eukaryotic cyclic nucleotide-gated channel. Nat Struct Mol Biol 27 7:625-634. PubMed Id: 32483338. doi:10.1038/s41594-020-0433-5.
*Cyclic-nucleotide-gated (CNG) channel TAX-4, R421W mutant, apo open state: Caenorhabditis elegans* E Eukaryota (expressed in Spodoptera frugiperda), 3.10 Å** cryo-EM structure apo closed state, 3.20 Å 7N16 cGMP-bound open state, 2.90 Å 7N15	7N17	Data File Jmol Viewer 7N17 7N16 7N15	Zheng et al. (2022). Zheng X, Li H, Hu Z, Su D, & Yang J (2022). Structural and functional characterization of an achromatopsia-associated mutation in a phototransduction channel. Commun Biol 5 1:190. PubMed Id: 35233102. doi:10.1038/s42003-022-03120-6.
*Cyclic-nucleotide-gated (CNG) channel: Leptospira licerasiae* B Bacteria (expressed in E. coli), 4.2 Å** cryo-EM structure	5V4S	Data File Jmol Viewer 5V4S	James et al. (2017). James ZM, Borst AJ, Haitin Y, Frenz B, DiMaio F, Zagotta WN, & Veesler D (2017). CryoEM structure of a prokaryotic cyclic nucleotide-gated ion channel. Proc Natl Acad Sci USA 114 :4430-4435. PubMed Id: 28396445. doi:10.1073/pnas.1700248114.
*Cyclic-nucleotide-gated (CNG) channel, apo form in K⁺/Ca²⁺: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.60 Å** cryo-EM structure cGMP-bound open state, 2.90 Å: 7LFW cGMP-bound open state in Na⁺, 3.60 Å: 7LFY cGMP-bound open state in Na⁺/Ca²⁺, 3.10 Å: 7LFX cGMP-bound E365Q mutant in Na⁺/Ca²⁺, 2.70 Å: 7LG1	7LFT	Data File Jmol Viewer 7LFT 7LG1 7LFY 7LFX 7LFW	Xue et al. (2021). Xue J, Han Y, Zeng W, Wang Y, & Jiang Y (2021). Structural mechanisms of gating and selectivity of human rod CNGA1 channel. Neuron 109 8:1302-1313.e4. PubMed Id: 33651975. doi:10.1016/j.neuron.2021.02.007.
*photoreceptor Cyclic-nucleotide-gated (CNGA1/B1) heterotetrameric channel, apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.61 Å** cryo-EM structure with CLZ coiled coil, 3.03 Å 7RHL cAMP-bound state, 2.88 Å 7RHG cGMP-bound openI state, 3.31 Å 7RHH cGMP-bound openII state, 3.31 Å 7RHI L-cis-Diltiazem-blocked open state, 2.88 Å 7RHJ L-cis-Diltiazem-trapped closed state, 3.27 Å 7RHK	7RH9	Data File Jmol Viewer 7RH9 7RHK 7RHL 7RHI 7RHG 7RHH 7RHJ	Xue et al. (2022). Xue J, Han Y, Zeng W, & Jiang Y (2022). Structural mechanisms of assembly, permeation, gating, and pharmacology of native human rod CNG channel. Neuron 110 1:86-95.e5. PubMed Id: 34699778. doi:10.1016/j.neuron.2021.10.006.
*photoreceptor Cyclic-nucleotide-gated (CNGA1/B1) heterotetrameric channel, apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.93 Å** cryo-EM structure	7RHS	Data File Jmol Viewer 7RHS	Zheng et al. (2022). Zheng X, Hu Z, Li H, & Yang J (2022). Structure of the human cone photoreceptor cyclic nucleotide-gated channel. Nat Struct Mol Biol 29 1:40-46. PubMed Id: 34969976. doi:10.1038/s41594-021-00699-y.
*photoreceptor Cyclic-nucleotide-gated (CNGA1/B1) heterotetrameric channel: Bos taurus* E Eukaryota, 3.40 Å** cryo-EM structure	7O4H	Data File Jmol Viewer 7O4H	Barret et al. (2022). Barret DCA, Schertler GFX, Benjamin Kaupp U, & Marino J (2022). The structure of the native CNGA1/CNGB1 CNG channel from bovine retinal rods. Nat Struct Mol Biol 29 1:32-39. PubMed Id: 34969975. doi:10.1038/s41594-021-00700-8.
*photoreceptor Cyclic-nucleotide-gated (CNGA1/B1) heterotetrameric channel with bound calmodulin: Bos taurus* E Eukaryota, 2.76 Å** cryo-EM structure	8BX7	Data File Jmol Viewer 8BX7	Barret et al. (2023). Barret DCA, Schuster D, Rodrigues MJ, Leitner A, Picotti P, Schertler GFX, Kaupp UB, Korkhov VM, & Marino J (2023). Structural basis of calmodulin modulation of the rod cyclic nucleotide-gated channel. Proc Natl Acad Sci U S A 120 15:e2300309120. PubMed Id: 37011209. doi:10.1073/pnas.2300309120.
*Cyclic nucleotide-gated (CNG) potassium channel SthK: Spirochaeta thermophila* B Bacteria (expressed in E. coli), 3.42 Å** cryo-EM structure in complex with cAMP, 3.35 Å: 6CJU in complex with cGMP, 3.46 Å: 6CJT	6CJQ	Data File Jmol Viewer 6CJQ 6CJT 6CJU	Rheinberger et al. (2018). Rheinberger J, Gao X, Schmidpeter PA, & Nimigean CM (2018). Ligand discrimination and gating in cyclic nucleotide-gated ion channels from apo and partial agonist-bound cryo-EM structures. Elife 7 :e39775. PubMed Id: 30028291. doi:10.7554/eLife.39775.
*Cyclic nucleotide-gated (CNG) potassium channel SthK, cAMP-bound closed state, in the presence of detergent: Spirochaeta thermophila* B Bacteria (expressed in E. coli), 3.60 Å** cryo-EM structure cAMP-bound closed state, in the presence of POPA, 2.41 Å:7TJ5 cAMP-bound open state, in the presence of POPA, 2.90 Å: 7TJ6	7TKT	Data File Jmol Viewer 7TKT 7TJ6 7TJ5	Schmidpeter et al. (2022). Schmidpeter PAM, Wu D, Rheinberger J, Riegelhaupt PM, Tang H, Robinson CV, & Nimigean CM (2022). Anionic lipids unlock the gates of select ion channels in the pacemaker family. Nat Struct Mol Biol 29 11:1092-1100. PubMed Id: 36352139. doi:10.1038/s41594-022-00851-2.
*Cyclic nucleotide-gated (CNG) potassium channel SthK, Y26F Closed State: Spirochaeta thermophila* B Bacteria (expressed in E. coli), 3.00 Å** cryo-EM structure R120A Closed State, 2.90 Å: 7RTF Y26F Activated State, 3.80 Å: 7RTJ R120A Open State 1, 4.30 Å: 7RU0 R120A Open State 2, 3.70 Å: 7RYS R120A Open State 3, 3.60 Å: 7RYR	7RSH	Data File Jmol Viewer 7RSH 7RYS 7RU0 7RTF 7RTJ 7RYR	Gao et al. (2022). Gao X, Schmidpeter PAM, Berka V, Durham RJ, Fan C, Jayaraman V, & Nimigean CM (2022). Gating intermediates reveal inhibitory role of the voltage sensor in a cyclic nucleotide-modulated ion channel. Nat Commun 13 1:6919. PubMed Id: 36376326. doi:10.1038/s41467-022-34673-z.
*HCN1 hyperpolarization-activated channel: Homo sapiens* E Eukaryota (expressed in HEK293S), 3.5 Å** cryo-EM structure with bound c-AMP, 3.51 Å: 5U6P	5U6O	Data File Jmol Viewer 5U6O 5U6P	Lee & MacKinnon (2017). Lee CH, & MacKinnon R (2017). Structures of the Human HCN1 Hyperpolarization-Activated Channel. Cell 168 :111-120.e11. PubMed Id: 28086084. doi:10.1016/j.cell.2016.12.023.
*HCN1 hyperpolarization-activated channel in hyperpolarized conformation: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.04 Å** cryoEM structure Y289D mutant, 3.54 Å: 6UQG	6UQF	Data File Jmol Viewer 6UQF 6UQG	Lee & MacKinnon (2019). Lee CH, & MacKinnon R (2019). Voltage Sensor Movements during Hyperpolarization in the HCN Channel. Cell 179 7:1582-1589.e7. PubMed Id: 31787376. doi:10.1016/j.cell.2019.11.006.
*AKT1 K⁺ hyperpolization-activated channel in MSP2N2 lipid nanodisc: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 2.80 Å** cryo-EM structure	7T4X	Data File Jmol Viewer 7T4X	Dickinson et al. (2022). Dickinson MS, Pourmal S, Gupta M, Bi M, & Stroud RM (2022). Symmetry Reduction in a Hyperpolarization-Activated Homotetrameric Ion Channel. Biochemistry 61 20:2177-2181. PubMed Id: 34964607. doi:10.1021/acs.biochem.1c00654.
*AKT1 K⁺ hyperpolization-activated channel: Arabidopsis thaliana* E Eukaryota (expressed in Spodoptera frugiperda), 3.40 Å** cryo-EM structure D379A constitutively-active mutant, 2.90 Å: 7FCV AKT1-AtKC1 complex, 3.30 Å: 7XUF	7WSW	Data File Jmol Viewer 7WSW 7XUF 7FCV	Lu et al. (2022). Lu Y, Yu M, Jia Y, Yang F, Zhang Y, Xu X, Li X, Yang F, Lei J, Wang Y, & Yang G (2022). Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis. Nat Commun 13 1:5682. PubMed Id: 36167696. doi:10.1038/s41467-022-33420-8.
*HCN4 hyperpolarization-activated channel stabilised in amphipol A8-35: Oryctolagus cuniculus* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure cAMP-free, stabilized in LMNG-CHS detergent mixture, 3.30 Å: 7NP3 cAMP-bound, stabilized in LMNG-CHS detergent mixture, 3.30 Å: 7NP4	7NMN	Data File Jmol Viewer 7NMN 7NP4 7NP3	Saponaro et al. (2021). Saponaro A, Bauer D, Giese MH, Swuec P, Porro A, Gasparri F, Sharifzadeh AS, Chaves-Sanjuan A, Alberio L, Parisi G, Cerutti G, Clarke OB, Hamacher K, Colecraft HM, Mancia F, Hendrickson WA, Siegelbaum SA, DiFrancesco D, Bolognesi M, Thiel G, Santoro B, & Moroni A (2021). Gating movements and ion permeation in HCN4 pacemaker channels. Mol Cell 81 14:2929-2943.e6. PubMed Id: 34166608. doi:10.1016/j.molcel.2021.05.033.
*KCNQ1 cardiac slow-delayed rectifier K⁺ channel in complex with calmodulin: Xenopus laevis* E Eukaryota (expressed in HEK293S cells), 3.7 Å** cryo-EM structure	5VMS	Data File Jmol Viewer 5VMS	Sun & MacKinnon (2017). Sun J, & MacKinnon R (2017). Cryo-EM Structure of a KCNQ1/CaM Complex Reveals Insights into Congenital Long QT Syndrome. Cell 169 6:1042-1050.e9. PubMed Id: 28575668. doi:10.1016/j.cell.2017.05.019.
*KCNQ1 cardiac slow-delayed rectifier K⁺ channel in complex with calmodulin (CaM): Xenopus laevis* E Eukaryota (expressed in HEK293 cells), 3.84 Å** cryo-EM structure with bound ML277, 3.90 Å 7TCI	7TCP	Data File Jmol Viewer 7TCP 7TCI	Willegems et al. (2022). Willegems K, Eldstrom J, Kyriakis E, Ataei F, Sahakyan H, Dou Y, Russo S, Van Petegem F, & Fedida D (2022). Structural and electrophysiological basis for the modulation of KCNQ1 channel currents by ML277. Nat Commun 13 1:3760. PubMed Id: 35768468. doi:10.1038/s41467-022-31526-7.
*KCNQ1 cardiac slow-delayed rectifier K⁺ channel in complex with calmodulin (CaM): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.1 Å** cryo-EM structure in complex with KCNE3 and CaM, 3.1 Å: 6V00 KCNQ1-KCNE3-CaM complex with PIP2, 3.9 Å: 6V01	6UZZ	Data File Jmol Viewer 6UZZ 6V00 6V01	Sun & MacKinnon (2020). Sun J, & MacKinnon R (2020). Structural Basis of Human KCNQ1 Modulation and Gating. Cell 180 2:340-347.e9. PubMed Id: 31883792. doi:10.1016/j.cell.2019.12.003.
*KCNQ1 cardiac slow-delayed rectifier K⁺ channel voltage sensor intermediate state: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure**	6MIE	Data File Jmol Viewer 6MIE	Taylor et al. (2020). Taylor KC, Kang PW, Hou P, Yang ND, Kuenze G, Smith JA, Shi J, Huang H, White KM, Peng D, George AL, Meiler J, McFeeters RL, Cui J, & Sanders CR (2020). Structure and physiological function of the human KCNQ1 channel voltage sensor intermediate state. Elife 9 :e53901. PubMed Id: 32096762. doi:10.7554/eLife.53901.
*KCNQ1 rectifier K⁺ channel in complex with CaM, apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure in complex with ML277, 2.60 Å: 7XNK KCNQ1-CaM-ML277-PIP2 complex in state A, 3.10 Å: 7XNL KCNQ1-CaM-ML277-PIP2 complex in state B, 2.50 Å: 7XNN	7XNI	Data File Jmol Viewer 7XNI 7XNK 7XNN 7XNL	Ma et al. (2022). Ma D, Zhong L, Yan Z, Yao J, Zhang Y, Ye F, Huang Y, Lai D, Yang W, Hou P, & Guo J (2022). Structural mechanisms for the activation of human cardiac KCNQ1 channel by electro-mechanical coupling enhancers. Proc Natl Acad Sci U S A 119 45:e2207067119. PubMed Id: 36763058. doi:10.1073/pnas.2207067119.
*KCNQ1 rectifier K⁺ channel in complex with CaM, up conformation: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure intermediate conformation, 6.20 Å: 8SIM down conformation, 6.80 Å: 8SIN	8SIK	Data File Jmol Viewer 8SIK 8SIM 8SIN	Mandala & MacKinnon (2023). Mandala VS, & MacKinnon R (2023). The membrane electric field regulates the PIP2-binding site to gate the KCNQ1 channel. Proc Natl Acad Sci U S A 120 21:e2301985120. PubMed Id: 37192161. doi:10.1073/pnas.2301985120.
*KCNQ2 rectifier K⁺ channel in complex with CaM, apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure in complex with ztz240 in absence of CaM, 3.40 Å: 7CR1 in complex with ztz240, 3.40 Å: 3.90 Å: 7CR4 in complex with retigabine in absence of CaM, 3.20 Å: 7CR2 in complex with retigabine, 3.70 Å: 7CR7	7CR3	Data File Jmol Viewer 7CR3 7CR4 7CR1 7CR2 7CR7	Li et al. (2020). Li X, Zhang Q, Guo P, Fu J, Mei L, Lv D, Wang J, Lai D, Ye S, Yang H, & Guo J (2020). Molecular basis for ligand activation of the human KCNQ2 channel. Cell Res . PubMed Id: 32884139. doi:10.1038/s41422-020-00410-8.
*KCNQ4 rectifier K⁺ channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.50 Å** cryo-EM structure with bound retigabine, 3.10 Å: 7BYM with bound linopirdine, 3.30 Å: 7BYN	7BYL	Data File Jmol Viewer 7BYL 7BYM 7BYN	Li et al. (2021). Li T, Wu K, Yue Z, Wang Y, Zhang F, & Shen H (2021). Structural Basis for the Modulation of Human KCNQ4 by Small-Molecule Drugs. Mol Cell 81 1:25-37.e4. PubMed Id: 33238160. doi:10.1016/j.molcel.2020.10.037.
*KCNQ4 rectifier K⁺ channel in complex with ML213 activator in digitonin: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.80 Å** cryo-EM structure in nanodisc, 2.96 Å 7VNQ complex with PIP2, 2.79 Å 7VNP	7VNR	Data File Jmol Viewer 7VNR 7VNQ 7VNP	Zheng et al. (2022). Zheng Y, Liu H, Chen Y, Dong S, Wang F, Wang S, Li GL, Shu Y, & Xu F (2022). Structural insights into the lipid and ligand regulation of a human neuronal KCNQ channel. Neuron 110 2:237-247.e4. PubMed Id: 34767770. doi:10.1016/j.neuron.2021.10.029.
*TMEM175 lysosomal K⁺ channel: Chamaesiphon minutus* E Eukaryota (expressed in E. coli), 3.3 Å**	5VRE	Data File Jmol Viewer 5VRE	Lee et al. (2017). Lee C, Guo J, Zeng W, Kim S, She J, Cang C, Ren D, & Jiang Y (2017). The lysosomal potassium channel TMEM175 adopts a novel tetrameric architecture. Nature 547 :472-475. PubMed Id: 28723891. doi:10.1038/nature23269.
*TMEM175 lysosomal K⁺ channel, open state in KCl: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.64 Å** cryo-EM structure closed state in KCl, 3.03 Å: 6WCA open state in CsCl, 3.17 Å: 6WCB closed state in CsCl, 3.24 Å: 6WCC	6WC9	Data File Jmol Viewer 6WC9 6WCA 6WCB 6WCC	Oh et al. (2020). Oh S, Paknejad N, & Hite RK (2020). Gating and selectivity mechanisms for the lysosomal K⁺ channel TMEM175. Elife 9 . PubMed Id: 32228865. doi:10.7554/eLife.53430.
*TMEM175 lysosomal K⁺ channel, open state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.45 Å** cryo-EM structure closed state, 2.61 Å 7UNM	7UNL	Data File Jmol Viewer 7UNL 7UNM	Oh et al. (2022). Oh S, Marinelli F, Zhou W, Lee J, Choi HJ, Kim M, Faraldo-Gómez JD, & Hite RK (2022). Differential ion dehydration energetics explains selectivity in the non-canonical lysosomal K⁺ channel TMEM175. Elife 11 :75122. PubMed Id: 35608336. doi:10.7554/eLife.75122.
*TMEM175 lysosomal K⁺ channel, in complex with 4-aminopyridine: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.73 Å** cryo-EM structure	8DHM	Data File Jmol Viewer 8DHM	Oh et al. (2022). Oh S, Stix R, Zhou W, Faraldo-Gómez JD, & Hite RK (2022). Mechanism of 4-aminopyridine inhibition of the lysosomal channel TMEM175. Proc Natl Acad Sci U S A 119 44:e2208882119. PubMed Id: 36279431. doi:10.1073/pnas.2208882119.
*TMEM175 lysosomal K⁺ channel, in complex with a Nanobody-MBP fusion protein: Marivirga tractuosa* B Bacteria (expressed in E. coli), 2.40 Å** TMEM175 with rubidium, 3.50 Å: 6HD9 TMEM175 with cesium, 3.80 Å: 6HDA TMEM175 with zinc, 2.90 Å: 6HDB T38A variant in complex with a Nanobody-MBP fusion protein, 3.40 Å: 6HDC TMEM175 T38A mutant soaked with zinc, 3.20 Å: 6SWR	6HD8	Data File Jmol Viewer 6HD8 6HDC 6HD9 6SWR 6HDA 6HDB	Brunner et al. (2020). Brunner JD, Jakob RP, Schulze T, Neldner Y, Moroni A, Thiel G, Maier T, & Schenck S (2020). Structural basis for ion selectivity in TMEM175 K⁺ channels. Elife 9 . PubMed Id: 32267231. doi:10.7554/eLife.53683.
*Odorant-gated ion channel receptor ORCO: Apocrypta bakeri* E Eukaryota (expressed in sf9 cells), 3.5 Å** cryo-EM structure	6C70	Data File Jmol Viewer 6C70	Butterwick et al. (2018). Butterwick JA, Del Mármol J, Kim KH, Kahlson MA, Rogow JA, Walz T, & Ruta V (2018). Cryo-EM structure of the insect olfactory receptor Orco. Nature 560 7719:447-452. PubMed Id: 30111839. doi:10.1038/s41586-018-0420-8.
*KAT1 Hyperpolarization-Activated Potassium Channel, tetramer: Arabidopsis thaliana* E Eukaryota (expressed in Spodoptera frugiperda), 3.50 Å** cryo-EM structure octamer, 3.80 Å: 6V1Y	6V1X	Data File Jmol Viewer 6V1X 6V1Y	Clark et al. (2020). Clark MD, Contreras GF, Shen R, & Perozo E (2020). Electromechanical coupling in the hyperpolarization-activated K⁺ channel KAT1. Nature 583 7814:145-149. PubMed Id: 32461693. doi:10.1038/s41586-020-2335-4.
*KAT1 Hyperpolarization-Activated Potassium Channel: Arabidopsis thaliana* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** cryo-EM structure	7CAL	Data File Jmol Viewer 7CAL	Li et al. (2020). Li S, Yang F, Sun D, Zhang Y, Zhang M, Liu S, Zhou P, Shi C, Zhang L, & Tian C (2020). Cryo-EM structure of the hyperpolarization-activated inwardly?rectifying potassium channel?KAT1?from?Arabidopsis. Cell Res 30 11:1049-1052. PubMed Id: 32901112. doi:10.1038/s41422-020-00407-3.
*Na⁺ leak channel non-selective (NALCN) in complex with FAM155A, in nanodisc: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.80 Å** cryo-EM structure	6XIW	Data File Jmol Viewer 6XIW	Kschonsak et al. (2020). Kschonsak M, Chua HC, Noland CL, Weidling C, Clairfeuille T, Bahlke OØ, Ameen AO, Li ZR, Arthur CP, Ciferri C, Pless SA, & Payandeh J (2020). Structure of the human sodium leak channel NALCN. Nature 587 7833:313-318. PubMed Id: 32698188. doi:10.1038/s41586-020-2570-8.
*Na⁺ leak channel non-selective (NALCN) in complex with FAM155A: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure	7CM3	Data File Jmol Viewer 7CM3	Xie et al. (2020). Xie J, Ke M, Xu L, Lin S, Huang J, Zhang J, Yang F, Wu J, & Yan Z (2020). Structure of the human sodium leak channel NALCN in complex with FAM155A. Nat Commun 11 1:5831. PubMed Id: 33203861. doi:10.1038/s41467-020-19667-z.
*Na⁺ leak channel non-selective (NALCN) in complex with FAM155A-UNC79-UNC80 with bound CaM, conformation 1/2: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure conformation 2/2, 3.50 Å: 7SX4	7SX3	Data File Jmol Viewer 7SX3 7SX4	Kschonsak et al. (2022). Kschonsak M, Chua HC, Weidling C, Chakouri N, Noland CL, Schott K, Chang T, Tam C, Patel N, Arthur CP, Leitner A, Ben-Johny M, Ciferri C, Pless SA, & Payandeh J (2022). Structural architecture of the human NALCN channelosome. Nature 603 7899:180-186. PubMed Id: 34929720. doi:10.1038/s41586-021-04313-5.
Channels: Calcium Ion-Selective
*Voltage-Gated Calcium Channel (Ca_V) created by mutation of the Na_VAb channel: Arcobacter butzleri* B Bacteria (expressed in Trichoplusia ni ), 2.75 Å** Mutation of the Na_V pore motif ¹⁷⁵TLESWSM¹⁸¹ to ¹⁷⁵TLDDWSN¹⁸¹. [Ca⁺²] = 15 mM [Ca⁺²] = 0.5 mM, 3.20 Å: 4MTF [Ca⁺²] = 2.5 mM, 3.30 Å: 4MTG [Ca⁺²] = 5.0 mM, 3.40 Å: 4MTO [Ca⁺²] = 10.0 mM, 3.20 Å: 4MVM [Ca⁺²] = 15.0 mM, 3.30 Å: 4MVO [Ca⁺²] = 15.0 mM, 3.30 Å: 4MW3 [Ca⁺²] = 15.0 mM, 3.20 Å: 4MVU Na_VAb mutants with ¹⁷⁵TLESWSM¹⁸¹ to ¹⁷⁵TLDDWSD¹⁸¹: [Ca⁺²] = 15.0 mM, 3.40 Å: 4MVQ [Mn⁺²] = 100 mM, 3.20 Å: 4MVR [Cd⁺²] = 100 mM, 3.30 Å: 4MVS [Ca⁺²] = 15.0 mM, 3.30 Å: 4MVZ Na_VAb wild-type: [Ca⁺²] = 15.0 mM, 3.26 Å: 4MW8	4MS2	Data File Jmol Viewer 4MS2 4MTF 4MW8 4MW3 4MVM 4MVQ 4MTG 4MVS 4MVU 4MVR 4MVZ 4MVO 4MTO	Tang et al. (2014). Tang L, Gamal El-Din TM, Payandeh J, Martinez GQ, Heard TM, Scheuer T, Zheng N, & Catterall WA (2014). Structural basis for Ca²⁺ selectivity of a voltage-gated calcium channel. Nature 505 :56-61. PubMed Id: 24270805. doi:10.1038/nature12775.
*Voltage-Gated Calcium Channel (Ca_V) created by mutation of the Na_VAb channel: Arcobacter butzleri* B Bacteria (expressed in Trichoplusia ni), 2.7 Å** [Ca²⁺] = 5mM W195Y mutant in complex with Br-dihydropyridine derivative UK-59811, 3.3 Å: 5KLG wild-type protein in complex with Br-dihydropyridine derivative UK-59811, 3.3 &Ariing;: 5KLS wild-type in complex with amlodipine, 3.2 Å: 5KMD wild-type in complex with nimodipine, 3.2 Å: 5KMF wild-type in complex with Br-verapamil, 3.2 Å: 5KMH	5KLB	Data File Jmol Viewer 5KLB 5KMD 5KMF 5KLG 5KLS 5KMH	Tang et al. (2016). Tang L, El-Din TM, Swanson TM, Pryde DC, Scheuer T, Zheng N, & Catterall WA (2016). Structural basis for inhibition of a voltage-gated Ca²⁺ channel by Ca²⁺ antagonist drugs. Nature 537 :117-121. PubMed Id: 27556947. doi:10.1038/nature19102.
*Ca_V1.1 L-type voltage-gated calcium channel: Oryctolagus cuniculus* E Eukaryota (expressed in E. coli), 4.2 Å** cryo-EM structure	3JBR	Data File Jmol Viewer 3JBR	Wu et al. (2015). Wu J, Yan Z, Li Z, Yan C, Lu S, Dong M, & Yan N (2015). Structure of the voltage-gated calcium channel Cav1.1 complex. Science 350 6267:1492. PubMed Id: 26680202. doi:10.1126/science.aad2395.
*Ca_V1.1 L-type voltage-gated calcium channel: Oryctolagus cuniculus* E Eukaryota (expressed in E. coli), 3.6 Å** cryo-EM structure class II reconstruction map, 3.9 Å: 5GJW	5GJV	Data File Jmol Viewer 5GJV 5GJW	Wu et al. (2016). Wu J, Yan Z, Li Z, Qian X, Lu S, Dong M, Zhou Q, & Yan N (2016). Structure of the voltage-gated calcium channel Ca_v1.1 at 3.6 Å resolution. Nature 537 :191-196. PubMed Id: 27580036. doi:10.1038/nature19321.
*Ca_V1.1 L-type voltage-gated calcium channel in complex with Nifedipine: Oryctolagus cuniculus* E Eukaryota (expressed in E. coli), 2.90 Å** cryo-EM structure in complex with Bay K8644, 2.70 Å: 6JP8 in complex with Verapamil, 2.60 Å: 6JPA in complex with Diltiazem, 2.90 Å: 6JPB	6JP5	Data File Jmol Viewer 6JP5 6JPA 6JPB 6JP8	Zhao et al. (2019). Zhao Y, Huang G, Wu J, Wu Q, Gao S, Yan Z, Lei J, & Yan N (2019). Molecular Basis for Ligand Modulation of a Mammalian Voltage-Gated Ca²⁺ Channel. Cell 177 6:1495-1506.e12. PubMed Id: 31150622. doi:10.1016/j.cell.2019.04.043.
*Ca_V1.1 L-type voltage-gated calcium channel in nanodiscs, in presence of amlodipine: Oryctolagus cuniculus* E Eukaryota, 2.9 Å** cryo-EM structure in presence 100 μM (R)-(+)-Bay K8644, 3.20 Å: 7JPW in presence 1 μM (R)-(+)-Bay K8644, 3.40 Å: 7JPV in presence of 100 μM (S)-(-)-Bay K8644, 3.00 Å: 7JPK	7JPX	Data File Jmol Viewer 7JPX 7JPV 7JPW 7JPK	Gao & Yan (2020). Gao S, & Yan N (2020). Structural Basis of the Modulation of the Voltage-Gated Calcium Ion Channel Ca_v1.1 by Dihydropyridine Compounds. Angew Chem Int Ed Engl 60 :3131-3137. PubMed Id: 33125829. doi:10.1002/anie.202011793.
*Ca_V1.1 L-type voltage-gated calcium channel in presence of 0.1 mM amiodarone: Oryctolagus cuniculus* E Eukaryota, 2.80 Å** cryo-EM structure in presence of 0.1 mM MNI-1, 2.80 Å: 8E57 in presence of 1 mM MNI-1, 3.00 Å: 8E58	8E56	Data File Jmol Viewer 8E56 8E57 8E58	Yao et al. (2022). Yao X, Gao S, Wang J, Li Z, Huang J, Wang Y, Wang Z, Chen J, Fan X, Wang W, Jin X, Pan X, Yu Y, Lagrutta A, & Yan N (2022). Structural basis for the severe adverse interaction of sofosbuvir and amiodarone on L-type Cav channels. Cell 185 25:4801-4810.e13. PubMed Id: 36417914. doi:10.1016/j.cell.2022.10.024.
*Ca_v1.2 L-type voltage-gated calcium channel, apo form: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure in the presence of amiodarone and sofosbuvir, 3.30 Å: 8FHS in the presence of calciseptine, 3.20 Å: 8WE7 in the presence of pinaverium, class I, 3.00 Å: 8WE9 in the presence of pinaverium, class II, 3.20 Å: 8WEA in the presence of calciseptine, amlodipine and pinaverium, 2.90 Å: 8WE8	8WE6	Data File Jmol Viewer 8WE6 8WEA 8WE9 8FHS 8WE8 8WE7	Gao et al. (2023). Gao S, Yao X, Chen J, Huang G, Fan X, Xue L, Li Z, Wu T, Zheng Y, Huang J, Jin X, Wang Y, Wang Z, Yu Y, Liu L, Pan X, Song C, & Yan N (2023). Structural basis for human Cav1.2 inhibition by multiple drugs and the neurotoxin calciseptine. Cell 186 24:5363-5374.e16. PubMed Id: 37972591. doi:10.1016/j.cell.2023.10.007.
*Ca_v1.2 L-type voltage-gated calcium channel in complex with L-leucine: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure See also 8EOI	8EOG	Data File Jmol Viewer 8EOG	Chen et al. (2023). Chen Z, Mondal A, Abderemane-Ali F, Jang S, Niranjan S, Montaño JL, Zaro BW, & Minor DL Jr (2023). EMC chaperone-Ca_V structure reveals an ion channel assembly intermediate. Nature 619 7969:410-419. PubMed Id: 37196677. doi:10.1038/s41586-023-06175-5.
*Ca_v1.2 L-type voltage-gated calcium channel with bound gabapentin: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure	8FD7	Data File Jmol Viewer 8FD7	Chen et al. (2023). Chen Z, Mondal A, & Minor DL Jr (2023). Structural basis for CaVα2δ:gabapentin binding. Nat Struct Mol Biol 30 6:735-739. PubMed Id: 36973510. doi:10.1038/s41594-023-00951-7.
*Ca_v1.3 L-type voltage-gated calcium channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure in the presence of cinnarizine, 3.1 Å: 7UHF	7UHG	Data File Jmol Viewer 7UHG 7UHF	Yao et al. (2022). Yao X, Gao S, & Yan N (2022). Structural basis for pore blockade of human voltage-gated calcium channel Ca_v1.3 by motion sickness drug cinnarizine. Cell Res 32 10:946-948. PubMed Id: 35477996. doi:10.1038/s41422-022-00663-5.
*Ca_V1.3 L-type voltage-gated calcium channel in presence of 0.14 mM amiodarone: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure in presence of 1.4 mM sofosbuvir, 3.30 Å: 8E5A in presence of 0.14 mM amidarone and 1.4 mM sofosbuvir, 3.30 Å:8E5B	8E59	Data File Jmol Viewer 8E59 8E5B 8E5A	Yao et al. (2022). Yao X, Gao S, Wang J, Li Z, Huang J, Wang Y, Wang Z, Chen J, Fan X, Wang W, Jin X, Pan X, Yu Y, Lagrutta A, & Yan N (2022). Structural basis for the severe adverse interaction of sofosbuvir and amiodarone on L-type Cav channels. Cell 185 25:4801-4810.e13. PubMed Id: 36417914. doi:10.1016/j.cell.2022.10.024.
*Ca_V2.2 N-type voltage-gated calcium channel, apo form: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.1 Å** cryo-EM structure in the presence of ziconotide, 3.0 Å: 7MIX	7MIY	Data File Jmol Viewer 7MIY 7MIX	Gao et al. (2021). Gao S, Yao X, & Yan N (2021). Structure of human Ca_v2.2 channel blocked by the painkiller ziconotide. Nature 596 7870:143-147. PubMed Id: 34234349. doi:10.1038/s41586-021-03699-6.
*Ca_V2.2 N-type voltage-gated calcium channel α2/δ1-β1 complex, apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.80 Å** cryo-EM structure bound to ziconotide, 3.00 Å 7VFU bound to PD173212, 3.00 Å 7VFV bound to Ca_V2.2-blocker1, 3.30 Å 7VFW	7VFS	Data File Jmol Viewer 7VFS 7VFW 7VFU 7VFV	Dong et al. (2021). Dong Y, Gao Y, Xu S, Wang Y, Yu Z, Li Y, Li B, Yuan T, Yang B, Zhang XC, Jiang D, Huang Z, & Zhao Y (2021). Closed-state inactivation and pore-blocker modulation mechanisms of human Ca_V2.2. Cell Rep 37 5:109931. PubMed Id: 34731621. doi:10.1016/j.celrep.2021.109931.
*Ca_v voltage-gated calcium channel α₂δ1 subunit alone: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.23 Å** cryo-EM structure with mirogabalin, 3.23 Å: 8IF3	8IF4	Data File Jmol Viewer 8IF4 8IF3	Kozai et al. (2023). Kozai D, Numoto N, Nishikawa K, Kamegawa A, Kawasaki S, Hiroaki Y, Irie K, Oshima A, Hanzawa H, Shimada K, Kitano Y, & Fujiyoshi Y (2023). Recognition Mechanism of a Novel Gabapentinoid Drug, Mirogabalin, for Recombinant Human α₂δ1, a Voltage-Gated Calcium Channel Subunit. J Mol Biol 435 10:168049. PubMed Id: 36933823. doi:10.1016/j.jmb.2023.168049.
*Ca_v2.3 R-type voltage-gated calcium channel, wild-type: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure ΔCH₂ mutant, 3.10 Å: 8EPM	8EPL	Data File Jmol Viewer 8EPL 8EPM	Yao et al. (2022). Yao X, Wang Y, Wang Z, Fan X, Wu D, Huang J, Mueller A, Gao S, Hu M, Robinson CV, Yu Y, Gao S, & Yan N (2022). Structures of the R-type human Ca_v2.3 channel reveal conformational crosstalk of the intracellular segments. Nat Commun 13 1:7358. PubMed Id: 36446785. doi:10.1038/s41467-022-35026-6.
*Ca_v2.3 R-type voltage-gated calcium channel in complex with the α2δ1 and β1 subunits, ligand-free (apo) state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure	7XLQ	Data File Jmol Viewer 7XLQ	Gao et al. (2023). Gao Y, Xu S, Cui X, Xu H, Qiu Y, Wei Y, Dong Y, Zhu B, Peng C, Liu S, Zhang XC, Sun J, Huang Z, & Zhao Y (2023). Molecular insights into the gating mechanisms of voltage-gated calcium channel Ca_V2.3. Nat Commun 14 1:516. PubMed Id: 36720859. doi:10.1038/s41467-023-36260-2.
*Ca_V3.1 T-type voltage-gated calcium channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.3 Å** cryoEM structure in complex with selective blocker Z944, 3.1 Å: 6KZP	6KZO	Data File Jmol Viewer 6KZO 6KZP	Zhao et al. (2019). Zhao Y, Huang G, Wu Q, Wu K, Li R, Lei J, Pan X, & Yan N (2019). Cryo-EM structures of apo and antagonist-bound human Ca_v3.1. Nature 576 7787:492-497. PubMed Id: 31766050. doi:10.1038/s41586-019-1801-3.
*Ca_V3.3 T-type voltage-gated calcium channel, apo form: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure in complex with mibefradil, 3.90 Å: 7WLJ in complex with otilonium bromide, 3.60 Å: 7WLK in complex with pimozide, 3.60 Å: 7WLL	7WLI	Data File Jmol Viewer 7WLI 7WLJ 7WLL 7WLK	He et al. (2022). He L, Yu Z, Geng Z, Huang Z, Zhang C, Dong Y, Gao Y, Wang Y, Chen Q, Sun L, Ma X, Huang B, Wang X, & Zhao Y (2022). Structure, gating, and pharmacology of human CaV3.3 channel. Nat Commun 13 1:2084. PubMed Id: 35440630. doi:10.1038/s41467-022-29728-0.
*Orai Calcium release-activated calcium (CRAC) channel: Drosophila melanogaster* E Eukaryota (expressed in Pichia pastoris), 3.35 Å** K163W mutant, 3.35 Å: 4HKS	4HKR	Data File Jmol Viewer 4HKR 4HKS	Hou et al. (2012). Hou X, Pedi L, Diver MM, & Long SB (2012). Crystal Structure of the Calcium Release-Activated Calcium Channel Orai. Science 338 :1308-1313. PubMed Id: 23180775. doi:10.1126/science.1228757.
*Orai Calcium release-activated calcium (CRAC) channel in open state, H206A gain-of-function mutant: Drosophila melanogaster* E Eukaryota (expressed in Komagataella pastoris), 6.71 Å** wild-type in intermediate conformation, 6.9 Å: 6BBG K163W loss-of-function mutant (I4₁ form), 6.1 Å: 6BBH K163W loss-of-function mutant (P4₂2₁2 form), 4.35 Å: 6BBI	6BBF	Data File Jmol Viewer 6BBF 6BBG 6BBI 6BBH	Hou et al. (2018). Hou X, Burstein SR, & Long SB (2018). Structures reveal opening of the store-operated calcium channel Orai. eLife 7 :e36758. PubMed Id: 30160233. doi:10.7554/eLife.36758.
*Orai Calcium release-activated calcium (CRAC) channel, P288L mutant: Drosophila melanogaster* E Eukaryota (expressed in HEK293 cells), 4.50 Å** cryo-EM structure	6AKI	Data File Jmol Viewer 6AKI	Liu et al. (2019). Liu X, Wu G, Yu Y, Chen X, Ji R, Lu J, Li X, Zhang X, Yang X, & Shen Y (2019). Molecular understanding of calcium permeation through the open Orai channel. PLoS Biol 17 4:e3000096. PubMed Id: 31009446. doi:10.1371/journal.pbio.3000096.
*Orai Calcium release-activated calcium (CRAC) channel, H206A mutant in an open conformation: Drosophila melanogaster* E Eukaryota (expressed in Komagataella pastoris), 3.30 Å** cryo-EM structure	7KR5	Data File Jmol Viewer 7KR5	Hou et al. (2020). Hou X, Outhwaite IR, Pedi L, & Long SB (2020). Cryo-EM structure of the calcium release-activated calcium channel Orai in an open conformation. Elife 9 :e62772. PubMed Id: 33252040. doi:10.7554/eLife.62772.
*Stromal interaction molecule 1 (STIM1) coiled-coil 1 fragment: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure** STIM1 modulates CRAC channel activation	6YEL	Data File Jmol Viewer 6YEL	Rathner et al. (2021). Rathner P, Fahrner M, Cerofolini L, Grabmayr H, Horvath F, Krobath H, Gupta A, Ravera E, Fragai M, Bechmann M, Renger T, Luchinat C, Romanin C, & Müller N (2021). Interhelical interactions within the STIM1 CC1 domain modulate CRAC channel activation. Nat Chem Biol 17 2:196-204. PubMed Id: 33106661. doi:10.1038/s41589-020-00672-8.
*YetJ pH-sensitive calcium-leak channel, pH 8 (closed form): Bacillus subtilis* B Bacteria (expressed in E. coli), 1.95 Å** pH 6 open form by soaking, 2.50 Å: 4PGS pH 7 open-closed form by back-soaking, 3.40 Å: 4PGU pH 8 closed form by back-soaking, 2.61 Å: 4PGV Open-form in C222₁ lattice, 3.60 Å: 4PGW	4PGR	Data File Jmol Viewer 4PGR 4PGV 4PGS 4PGW 4PGU	Chang et al. (2014). Chang Y, Bruni R, Kloss B, Assur Z, Kloppmann E, Rost B, Hendrickson WA, & Liu Q (2014). Structural basis for a pH-sensitive calcium leak across membranes. Science 344 :1131-1135. PubMed Id: 24904158. doi:10.1126/science.1252043.
*YetJ pH-sensitive calcium-leak channel: Bacillus subtilis* B Bacteria (expressed in E. coli), 2.5 Å** D171E mutant, 3.1 Å: 6NQ8 D195E mutant, 3.1 Å: 6NQ9	6NQ7	Data File Jmol Viewer 6NQ7 6NQ9 6NQ8	Guo et al. (2019). Guo G, Xu M, Chang Y, Luyten T, Seitaj B, Liu W, Zhu P, Bultynck G, Shi L, Quick M, & Liu Q (2019). Ion and pH Sensitivity of a TMBIM Ca²⁺ Channel. Structure 27 6:1013-1021.e3. PubMed Id: 30930064. doi:10.1016/j.str.2019.03.003.
*RyR1 ryanodine receptor, closed state in complex with FKBP12. Cryo-EM structure: Oryctolagus cuniculus* E Eukaryota, 3.8 Å**	3J8H	Data File Jmol Viewer 3J8H	Yan et al. (2015). Yan Z, Bai X, Yan C, Wu J, Li Z, Xie T, Peng W, Yin C, Li X, Scheres SH, Shi Y, & Yan N (2015). Structure of the rabbit ryanodine receptor RyR1 at near-atomic resolution. Nature 517 :50-55. PubMed Id: 25517095. doi:10.1038/nature14063.
*RyR1 ryanodine receptor, closed state in complex with FKBP12.6. Cryo-EM structure: Oryctolagus cuniculus* E Eukaryota, 4.8 Å**	3J8E	Data File Jmol Viewer 3J8E	Zalk et al. (2015). Zalk R, Clarke OB, Georges AD, Grassucci RA, Reiken S, Mancia F, Hendrickson WA, Frank J, & Marks AR (2015). Structure of a mammalian ryanodine receptor. Nature 517 :44-49. PubMed Id: 25470061. doi:10.1038/nature13950.
*RyR1 ryanodine receptor Repeat12 domain: Oryctolagus cuniculus* E Eukaryota (expressed in E. coli), 1.55 Å**	5C30	Data File Jmol Viewer 5C30	Yuchi et al. (2015). Yuchi Z, Yuen SM, Lau K, Underhill AQ, Cornea RL, Fessenden JD, & Van Petegem F (2015). Crystal structures of ryanodine receptor SPRY1 and tandem-repeat domains reveal a critical FKBP12 binding determinant. Nat Commun 6 :7947. PubMed Id: 26245150. doi:10.1038/ncomms8947.
*RyR1 ryanodine receptor in lipid nanodiscs in presence of Ca²⁺ & ATP: Oryctolagus cuniculus* E Eukaryota, 8.2 Å** cryo-EM structure in the presence of ryanodine, 7.3 Å: 6FG3	6FOO	Data File Jmol Viewer 6FOO 6FG3	Willegems & Efremov (2018). Willegems K, & Efremov RG (2018). Influence of Lipid Mimetics on Gating of Ryanodine Receptor. Structure 26 10:1303-1313.e4. PubMed Id: 30078641. doi:10.1016/j.str.2018.06.010.
*RyR1 ryanodine receptor in complex with Ca²⁺ and chlorantraniliprole (CHL): Oryctolagus cuniculus* E Eukaryota, 4.70 Å** cryo-EM structure in complex with Ca²⁺,CHL,Caffeine, ATP, and calmodulin, 3.80 Å: 6M2W	7CF9	Data File Jmol Viewer 7CF9 6M2W	Ma et al. (2020). Ma R, Haji-Ghassemi O, Ma D, Jiang H, Lin L, Yao L, Samurkas A, Li Y, Wang Y, Cao P, Wu S, Zhang Y, Murayama T, Moussian B, Van Petegem F, & Yuchi Z (2020). Structural basis for diamide modulation of ryanodine receptor. Nat Chem Biol 16 11:1246-1254. PubMed Id: 32807966. doi:10.1038/s41589-020-0627-5.
*RyR1 ryanodine receptor embedded in a lipid bilayer, primed model: Oryctolagus cuniculus* E Eukaryota, 3.36 Å** cryo-EM structure open model, 3.98 Å 7M6L	7M6A	Data File Jmol Viewer 7M6A 7M6L	Melville et al. (2022). Melville Z, Kim K, Clarke OB, & Marks AR (2022). High-resolution structure of the membrane-embedded skeletal muscle ryanodine receptor. Structure 30 :172-180. PubMed Id: 34469755. doi:10.1016/j.str.2021.08.001.
*RyR1 ryanodine receptor in the presence of AMP-PCP in nanodisc: Oryctolagus cuniculus* E Eukaryota, 4.30 Å** cryo-EM structure with AMP-PCP and high Ca²⁺, inactivated conformation (Dataset-A), 3.80 Å 7TDG with AMP-PCP and high Ca²⁺ in closed-inactivated conformation class 1(Dataset-A), 3.70 Å 7TDJ with AMP-PCP and high Ca2⁺ in closed-inactivated conformation class 2 (Dataset-A), 3.30 Å 7TDI with AMP-PCP and high Ca²⁺ in open conformation, 4.00 Å 7TDH	7K0T	Data File Jmol Viewer 7K0T 7TDG 7TDJ 7TDI 7TDH	Nayak & Samsó (2022). Nayak AR, & Samsó M (2022). Ca²⁺ inactivation of the mammalian ryanodine receptor type 1 in a lipidic environment revealed by cryo-EM. Elife 11 :e75568. PubMed Id: 35257661. doi:10.7554/eLife.75568.
*recombinant RyR1 ryanodine receptor, R164C mutant in complex with FKBP12.6: Oryctolagus cuniculus* E Eukaryota (expressed in HEK293 cells), 3.54 Å** cryo-EM structure type 2 mutant R176Q in complex with FKBP12.6 in nanodisc, 3.27 Å: 6WOU type 2 wild-type in complex with FKBP12.6, 5.10 Å: 6WOV	6WOT	Data File Jmol Viewer 6WOT 6WOU 6WOV	Iyer et al. (2020). Iyer KA, Hu Y, Nayak AR, Kurebayashi N, Murayama T, & Samsó M (2020). Structural mechanism of two gain-of-function cardiac and skeletal RyR mutations at an equivalent site by cryo-EM. Sci Adv 6 31:eabb2964. PubMed Id: 32832689. doi:10.1126/sciadv.abb2964.
*RyR1 ryanodine receptor disease mutant Y523S, embedded in lipidic nanodisc, closed state, in complex with FKBP12.6: Oryctolagus cuniculus* E Eukaryota (expressed in HEK293 cells), 4.00 Å** cryo-EM structure in complex with FKBP12.6, 4.05 Å: 7T65	7T64	Data File Jmol Viewer 7T64 7T65	Iyer et al. (2022). Iyer KA, Hu Y, Klose T, Murayama T, & Samsó M (2022). Molecular mechanism of the severe MH/CCD mutation Y522S in skeletal ryanodine receptor (RyR1) by cryo-EM. Proc Natl Acad Sci U S A 119 30:e2122140119. PubMed Id: 35867837. doi:10.1073/pnas.2122140119.
*RyR2 ryanodine receptor, closed state: Sus scrofa* E Eukaryota, 4.4 Å** Cryo-EM structure open-state structure, 4.2 Å: 5GOA	5GO9	Data File Jmol Viewer 5GO9 5GOA	Peng et al. (2016). Peng W, Shen H, Wu J, Guo W, Pan X, Wang R, Chen SR, & Yan N (2016). Structural basis for the gating mechanism of the type 2 ryanodine receptor RyR2. Science 354 :301. PubMed Id: 27708056. doi:10.1126/science.aah5324. One-page Research Article Summary on p. 301. For full article, follow the DOI.
*RyR2 ryanodine receptor bound to FKBP12.6 interacting with human calmodulin (CaM), apo CaM state: Sus scrofa* E Eukaryota, 3.6 Å** cryo-EM structure. FKBP12.6 and CaM expressed in E. coli. ATP/caffeine/low Ca/Cam-M, 4.2 Å: 6JII ATP/caffeine/low Ca, 4.2 Å: 6JI0 ATP/caffeine/low Ca/Cam-M, 4.2 /Ca-CaM, 4.2 Å: 6JIU CHAPS and DOPC treated, ATP/caffeine/low Ca, 3.9 Å: 6JRR CHAPS and DOPC treated, ATP/caffeine/low Ca/Ca-CaM, 3.7 Å: 6JRS ATP/caffeine/high Ca/Ca-CaM, 3.9 Å: 6JIY PCB95/low Ca/Ca-CaM, 4.4 Å: 6JV2	6JI8	Data File Jmol Viewer 6JI8 6JI0 6JRS 6JRR 6JIY 6JIU 6JV2 6JII	Gong et al. (2019). Gong D, Chi X, Wei J, Zhou G, Huang G, Zhang L, Wang R, Lei J, Chen SRW, & Yan N (2019). Modulation of cardiac ryanodine receptor 2 by calmodulin. Nature 572 7769:347-351. PubMed Id: 31278385. doi:10.1038/s41586-019-1377-y.
*RyR2 ryanodine receptor, Ca²⁺: Sus scrofa* E Eukaryota, 6.3 Å** cryo-EM structure F/P/Ca²⁺ dataset, 4.6 Å: 6JGZ F/A/Ca²⁺ dataset, 4.8 Å: 6JH6 F/C/Ca²⁺ dataset, 4.5 Å: 6JHN	6JG3	Data File Jmol Viewer 6JG3 6JGZ 6JH6 6JHN	Chi et al. (2019). Chi X, Gong D, Ren K, Zhou G, Huang G, Lei J, Zhou Q, & Yan N (2019). Molecular basis for allosteric regulation of the type 2 ryanodine receptor channel gating by key modulators. Proc Natl Acad Sci USA 116 51:25575-25582. PubMed Id: 31792195. doi:10.1073/pnas.1914451116.
*RyR2 ryanodine receptor SPRY1 domain critical in binding FKBP12: Mus musculus* E Eukaryota (expressed in E. coli), 1.21 Å**	5C33	Data File Jmol Viewer 5C33	Yuchi et al. (2015). Yuchi Z, Yuen SM, Lau K, Underhill AQ, Cornea RL, Fessenden JD, & Van Petegem F (2015). Crystal structures of ryanodine receptor SPRY1 and tandem-repeat domains reveal a critical FKBP12 binding determinant. Nat Commun 6 :7947. PubMed Id: 26245150. doi:10.1038/ncomms8947.
*RyR2 ryanodine receptor, EGTA dataset, class 1&2, closed state: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure EGTA dataset, class 1, closed state, 3.50 Å: 7VMM EGTA dataset, class 2, closed state, 3.50 Å: 7VMN Ca²⁺ dataset, class 1, open state, 3.50 Å: 7VMO Ca²⁺ dataset, class 2, open state, 3.50 Å: 7VMP Ca²⁺ dataset, class 3, open state, 3.70 Å: 7VMQ K4593A mutant (EGTA dataset), 3.30 Å: 7VMR K4593A mutant (Ca²⁺ dataset), 3.80Å: 7vMS	7VML	Data File Jmol Viewer 7VML 7VMP 7VMO 7VMN 7VMM 7vMS 7VMR 7VMQ	Kobayashi et al. (2022). Kobayashi T, Tsutsumi A, Kurebayashi N, Saito K, Kodama M, Sakurai T, Kikkawa M, Murayama T, & Ogawa H (2022). Molecular basis for gating of cardiac ryanodine receptor explains the mechanisms for gain- and loss-of function mutations. Nat Commun 13 1:2821. PubMed Id: 35595836. doi:10.1038/s41467-022-30429-x.
*InsP₃R1 Inositol-1,4,5-trisphosphate receptor: Rattus norvegicus* E Eukaryota, 4.7 Å** Cryo-EM structure	3JAV	Data File Jmol Viewer 3JAV	Fan et al. (2015). Fan G, Baker ML, Wang Z, Baker MR, Sinyagovskiy PA, Chiu W, Ludtke SJ, & Serysheva II (2015). Gating machinery of InsP₃R channels revealed by electron cryomicroscopy. Nature 527 :336-341. PubMed Id: 26458101. doi:10.1038/nature15249.
*InsP₃R1 Inositol-1,4,5-trisphosphate receptor in lipid nanodisc, the apo-state: Rattus norvegicus* E Eukaryota, 3.30 Å** cryo-EM structure solubilized in LNMG & lipid in the apo-state, 2.96 Å: 7LHF	7LHE	Data File Jmol Viewer 7LHE 7LHF	Baker et al. (2021). Baker MR, Fan G, Seryshev AB, Agosto MA, Baker ML, & Serysheva II (2021). Cryo-EM structure of type 1 IP₃R channel in a lipid bilayer. Commun Biol 4 1:625. PubMed Id: 34035440. doi:10.1038/s42003-021-02156-4.
*InsP₃R1 Inositol-1,4,5-trisphosphate receptor in the presence of Calcium/IP3/ATP: Rattus norvegicus* E Eukaryota, 3.50 Å** cryo-EM structure in high Ca²⁺, 3.26 Å: 8EAQ	8EAR	Data File Jmol Viewer 8EAR 8EAQ	Fan et al. (2022). Fan G, Baker MR, Terry LE, Arige V, Chen M, Seryshev AB, Baker ML, Ludtke SJ, Yule DI, & Serysheva II (2022). Conformational motions and ligand-binding underlying gating and regulation in IP₃R channel. Nat Commun 13 1:6942. PubMed Id: 36376291. doi:10.1038/s41467-022-34574-1.
*InsP₃R3 Inositol-1,4,5-trisphosphate receptor, apo state: Homo sapiens* E Eukaryota (expressed in Sf9 cells), 3.49 Å** cryo-EM structure IP3-bound, class 1, 3.33 Å: 6DQN IP3-bound, class 2, 3.82 Å: 6DQV IP3-bound, class 3, 4.12 Å: 6DQS IP3-bound, class 4, 6.01 Å: 6DQZ IP3-bound, class 5, 4.47 Å: 6DR0 Ca²⁺ bound, 4.33 Å: 6DR2 low IP3-Ca²⁺ bound, 3.96 Å: 6DRA high IP3-Ca²⁺ bound, 3.92 Å: 6DRC	6DQJ	Data File Jmol Viewer 6DQJ 6DQZ 6DRC 6DQN 6DRA 6DQS 6DR0 6DQV 6DR2	Paknejad & Hite (2018). Paknejad N, & Hite RK (2018). Structural basis for the regulation of inositol trisphosphate receptors by Ca²⁺ and IP₃. Nat Struct Mol Biol 25 8:660-668. PubMed Id: 30013099. doi:10.1038/s41594-018-0089-6.
*InsP₃R3 Inositol-1,4,5-trisphosphate receptor and presence of self-binding peptide: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.77 Å** cryo-EM structure	6UQK	Data File Jmol Viewer 6UQK	Azumaya et al. (2020). Azumaya CM, Linton EA, Risener CJ, Nakagawa T, & Karakas E (2020). Cryo-EM structure of human type-3 inositol triphosphate receptor reveals the presence of a self-binding peptide that acts as an antagonist. J Biol Chem 295 6:1743-1753. PubMed Id: 31915246. doi:10.1074/jbc.RA119.011570.
*IP3 and ATP bound type 3 IP3 receptor in the pre-active A state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** cryo-EM structure in the pre-active B state, 3.30 Å 7T3Q in the pre-active C state, 3.40 Å 7T3R in the active state, 3.80 Å 7T3T in the inactive state, 3.70 Å 7T3U	7T3P	Data File Jmol Viewer 7T3P 7T3U 7T3Q 7T3T 7T3R	Schmitz et al. (2022). Schmitz EA, Takahashi H, & Karakas E (2022). Structural basis for activation and gating of IP3 receptors. Nat Commun 13 1:1408. PubMed Id: 35301323. doi:10.1038/s41467-022-29073-2.
*InsP₃R3 Inositol-1,4,5-trisphosphate receptor, resting state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.49 Å** cryo-EM structure preactivated state, 3.70 Å: 8TKD preactivated state, with bound Ca²⁺, 3.60 Å: 8TKE activated state, 3.20 Å: 8TKF resting state, 2.50 Å: 8TKG labile resting state 1, 3.50 Å: 8TKH labile resting state 2, 3.60 Å: 8TKI resting state, 3.30 Å: 8TL9 higher-order inhibited state, 3.20 Å: 8TLA	8TK8	Data File Jmol Viewer 8TK8 8TLA 8TKF 8TL9 8TKG 8TKE 8TKI 8TKD 8TKH	Paknejad et al. (2023). Paknejad N, Sapuru V, & Hite RK (2023). Structural titration reveals Ca2+-dependent conformational landscape of the IP3 receptor. Nat Commun 14 1:6897. PubMed Id: 37898605. doi:10.1038/s41467-023-42707-3.
*Mitochondrial calcium uniporter (MCU): Caenorhabditis elegans* E Eukaryota (expressed in E. coli), NMR structure**	5ID3	Data File Jmol Viewer 5ID3	Oxenoid et al. (2016). Oxenoid K, Dong Y, Cao C, Cui T, Sancak Y, Markhard AL, Grabarek Z, Kong L, Liu Z, Ouyang B, Cong Y, Mootha VK, & Chou JJ (2016). Architecture of the mitochondrial calcium uniporter. Nature 533 :269-273. PubMed Id: 27135929. doi:10.1038/nature17656.
*Mitochondrial calcium uniporter (MCU), full length: Neurospora crassa* E Eukaryota (expressed in E. coli), 3.7 Å** cryo-EM structure	6DT0	Data File Jmol Viewer 6DT0	Yoo et al. (2018). Yoo J, Wu M, Yin Y, Herzik MA Jr, Lander GC, & Lee SY (2018). Cryo-EM structure of a mitochondrial calcium uniporter. Science 361 6401:506-511. PubMed Id: 29954988. doi:10.1126/science.aar4056.
*Mitochondrial calcium uniporter (MCU), full length: Neosartorya fischeri* E Eukaryota (expressed in E. coli), 3.8 Å** cryo-EM structure in complex with saposin, 5 Å: 6D80	6D7W	Data File Jmol Viewer 6D7W 6D80	Nguyen et al. (2018). Nguyen NX, Armache JP, Lee C, Yang Y, Zeng W, Mootha VK, Cheng Y, Bai XC, & Jiang Y (2018). Cryo-EM structure of a fungal mitochondrial calcium uniporter. Nature 559 7715:570-574. PubMed Id: 29995855. doi:10.1038/s41586-018-0333-6.
*Mitochondrial calcium uniporter (MCU), full length: Metarhizium acridum* E Eukaryota (expressed in E. coli), 3.10 Å** soluble domain, 3.10 Å: 6C5R	6C5W	Data File Jmol Viewer 6C5W 6C5R	Fan et al. (2018). Fan C, Fan M, Orlando BJ, Fastman NM, Zhang J, Xu Y, Chambers MG, Xu X, Perry K, Liao M, & Feng L (2018). X-ray and cryo-EM structures of the mitochondrial calcium uniporter. Nature 559 7715:575-579. PubMed Id: 29995856. doi:10.1038/s41586-018-0330-9.
*Mitochondrial calcium uniporter (MCU), full length: Cyphellophora europaea* E Eukaryota (expressed in Komagataella pastoris), 3.2 Å** cryo-EM structure	6DNF	Data File Jmol Viewer 6DNF	Baradaran et al. (2018). Baradaran R, Wang C, Siliciano AF, & Long SB (2018). Cryo-EM structures of fungal and metazoan mitochondrial calcium uniporters. Nature 559 7715:580-584. PubMed Id: 29995857. doi:10.1038/s41586-018-0331-8.
*Mitochondrial calcium uniporter (MCU) in complex with EMRE: Homo Sapiens* E Eukaryota (expressed in HEK293 cells), 3.8 Å** cryo-EM structure	6O58	Data File Jmol Viewer 6O58	Wang et al. (2019). Wang Y, Nguyen NX, She J, Zeng W, Yang Y, Bai XC, & Jiang Y (2019). Structural Mechanism of EMRE-Dependent Gating of the Human Mitochondrial Calcium Uniporter. Cell 177 5:1252-1261.e13. PubMed Id: 31080062. doi:10.1016/j.cell.2019.03.050.
*mitochondrial calcium uniporter (MCU) holocomplex, low Ca²⁺: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure high Ca²⁺, 3.60 Å: 6WDO	6WDN	Data File Jmol Viewer 6WDN 6WDO	Fan et al. (2020). Fan M, Zhang J, Tsai CW, Orlando BJ, Rodriguez M, Xu Y, Liao M, Tsai MF, & Feng L (2020). Structure and mechanism of the mitochondrial Ca²⁺ uniporter holocomplex. Nature 582 7810:129-133. PubMed Id: 32494073. doi:10.1038/s41586-020-2309-6.
*Mitochondrial calcium uniporter (MCU) holocomplex (uniplex) in nanodiscs, high calcium state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.17 Å** cryo-EM structure low-calcium blocking state, 4.60 Å: 6XJX	6XJV	Data File Jmol Viewer 6XJV 6XJX	Wang et al. (2020). Wang Y, Han Y, She J, Nguyen NX, Mootha VK, Bai XC, & Jiang Y (2020). Structural insights into the Ca²⁺-dependent gating of the human mitochondrial calcium uniporter. Elife 9 . PubMed Id: 32762847. doi:10.7554/eLife.60513.
*Mitochondrial calcium uniporter (MCU) in complex with MICU1/MICU2 subunits: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure	6K7Y	Data File Jmol Viewer 6K7Y	Zhuo et al. (2021). Zhuo W, Zhou H, Guo R, Yi J, Zhang L, Yu L, Sui Y, Zeng W, Wang P, & Yang M (2021). Structure of intact human MCU supercomplex with the auxiliary MICU subunits. Protein Cell 12 3:220-229. PubMed Id: 32862359. doi:10.1007/s13238-020-00776-w.
*RyR2 ryanodine receptor, PKA phosphorylated in the closed state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.11 Å** cryo-EM structure in the open state, 3.69 Å: 7U9R in the closed state in the presence of Calmodulin, 2.68 Å: 7U9T RyR2-R2474S in the closed state, 2.58 Å: 7U9X RyR2-R2474S in the open state, 3.29 Å: 7U9Z RyR2-R2474S in the closed state in the presence of ARM210, 2.99 Å: 7UA1 RyR2-R2474S in the closed state in the presence of Calmodulin, 2.97 Å: 7UA3 RyR2-R2474S in the open state in the presence of Calmodulin, 2.93 Å: 7UA4 dephosphorylated in the closed state, 2.83 Å: 7UA5 dephosphorylated in the open state, 3.59 Å: 7UA9	7U9Q	Data File Jmol Viewer 7U9Q 7U9R 7UA5 7U9X 7UA3 7U9T 7U9Z 7UA9 7UA4 7UA1	Miotto et al. (2022). Miotto MC, Weninger G, Dridi H, Yuan Q, Liu Y, Wronska A, Melville Z, Sittenfeld L, Reiken S, & Marks AR (2022). Structural analyses of human ryanodine receptor type 2 channels reveal the mechanisms for sudden cardiac death and treatment. Sci Adv 8 29:eabo1272. PubMed Id: 35857850. doi:10.1126/sciadv.abo1272.
Channels: Transient Receptor Potential (TRP) Non-selective cation channels responding to a wide range of chemical and physical stimuli
*TRP1 thermo-sensitive transient receptor potential channel in nanodiscs: Chlamydomonas reinhardtii* E Eukaryota (expressed in HEK293 cells), 3.45 Å** in glyco-diosgenin (GDN) detergent, 3.53 Å: 6PW4	6PW5	Data File Jmol Viewer 6PW5 6PW4	McGoldrick et al. (2019). McGoldrick LL, Singh AK, Demirkhanyan L, Lin TY, Casner RG, Zakharian E, & Sobolevsky AI (2019). Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii. Nat Commun 10 1:4180. PubMed Id: 31519888. doi:10.1038/s41467-019-12121-9.
*TRPA1 transient receptor potential channel (wasabi receptor): Homo sapiens* E Eukaryota (expressed in HEK293S GnTI^-), 4.24 Å** Structure determined using single-particle cryo-EM.	3J9P	Data File Jmol Viewer 3J9P	Paulsen et al. (2015). Paulsen CE, Armache JP, Gao Y, Cheng Y, & Julius D (2015). Structure of the TRPA1 ion channel suggests regulatory mechanisms. Nature 520 7548:511-517. PubMed Id: 25855297. doi:10.1038/nature14367.
*TRPA1 transient receptor potential channel, covalent agonist JT010: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.88 Å** cryo-EM structure with the covalent agonist BITC, 3.06 Å: 6PQP C621S mutant in the apo state, 2.81 Å: 6PQQ	6PQO	Data File Jmol Viewer 6PQO 6PQP 6PQQ	Suo et al. (2020). Suo Y, Wang Z, Zubcevic L, Hsu AL, He Q, Borgnia MJ, Ji RR, & Lee SY (2020). Structural Insights into Electrophile Irritant Sensing by the Human TRPA1 Channel. Neuron 105 5:882-894.e5. PubMed Id: 31866091. doi:10.1016/j.neuron.2019.11.023.
*TRPA1 transient receptor potential channel, modified by Bodipy-iodoacetamide with bound calcium in LMNG: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.60 Å** cryo-EM structure ligand-free with bound calcium in LMNG detergent, 3.10 Å: 6V9W TRPA1 modified by iodoacetamide in PMAL-C8, 3.30 Å: 6V9X bound with A-967079 in PMAL-C8, 3.60Å: 6V9Y	6V9V	Data File Jmol Viewer 6V9V 6V9Y 6V9X 6V9W	Zhao et al. (2020). Zhao J, Lin King JV, Paulsen CE, Cheng Y, & Julius D (2020). Irritant-evoked activation and calcium modulation of the TRPA1 receptor. Nature 585 7823:141-145. PubMed Id: 32641835. doi:10.1038/s41586-020-2480-9.
*TRPA1 transient receptor potential channel in complex with antagonist compound 21: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.05 Å** cryo-EM structure	7JUP	Data File Jmol Viewer 7JUP	Terrett et al. (2021). Terrett JA, Chen H, Shore DG, Villemure E, Larouche-Gauthier R, Déry M, Beaumier F, Constantineau-Forget L, Grand-Maître C, Lépissier L, Ciblat S, Sturino C, Chen Y, Hu B, Lu A, Wang Y, Cridland AP, Ward SI, Hackos DH, Reese RM, Shields SD, Chen J, Balestrini A, Riol-Blanco L, Lee WP, Liu J, Suto E, Wu X, Zhang J, Ly JQ, La H, Johnson K, Baumgardner M, Chou KJ, Rohou A, Rougé L, Safina BS, Magnuson S, & Volgraf M (2021). Tetrahydrofuran-Based Transient Receptor Potential Ankyrin 1 (TRPA1) Antagonists: Ligand-Based Discovery, Activity in a Rodent Asthma Model, and Mechanism-of-Action via Cryogenic Electron Microscopy. J Med Chem 64 7:3843-3869. PubMed Id: 33749283. doi:10.1021/acs.jmedchem.0c02023.
*TRPC3 ion channel, lipid-occupied closed state: Homo sapiens* E Eukaryota (expressed in HEK 293), 3.3 Å** cryo-EM structure	6CUD	Data File Jmol Viewer 6CUD	Fan et al. (2018). Fan C, Choi W, Sun W, Du J, & Lu W (2018). Structure of the human lipid-gated cation channel TRPC3. Elife 7 :e36852. PubMed Id: 29726814. doi:10.7554/eLife.36852.
*TRPC3 ion channel in high calcium state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.70 Å** cryo-EM structure in low calcium state, 3.06 Å:7DXC in 1340 nM free calcium state, 3.90 Å: 7DXD gain of function mutation R803C in 1340nM free calcium state, 3.20 Å: 7DXE	7DXB	Data File Jmol Viewer 7DXB 7DXC 7DXD 7DXE	Guo et al. (2022). Guo W, Tang Q, Wei M, Kang Y, Wu JX, & Chen L (2022). Structural mechanism of human TRPC3 and TRPC6 channel regulation by their intracellular calcium-binding sites. Neuron 110 6:1023-1035.e5. PubMed Id: 35051376. doi:10.1016/j.neuron.2021.12.023.
*TRPC4 ion channel, apo state: Danio rerio* E Eukaryota (expressed in HEK 293 cells), 3.6 Å** cryo-EM structure	6G1K	Data File Jmol Viewer 6G1K	Vinayagam et al. (2018). Vinayagam D, Mager T, Apelbaum A, Bothe A, Merino F, Hofnagel O, Gatsogiannis C, & Raunser S (2018). Electron cryo-microscopy structure of the canonical TRPC4 ion channel. Elife 7 . PubMed Id: 29717981. doi:10.7554/eLife.36615.
*TRPC4 ion channel in complex with inhibitor GFB-8438: Danio rerio* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure in complex with inhibitor GFB-9289, 3.15 Å: 7B16 in complex with inhibitor GFB-8749, 3.80 Å: 7B05 in complex with Calmodulin, 3.60 Å: 7B1G in LMNG detergent, 2.85 Å: 7B0J	7B0S	Data File Jmol Viewer 7B0S 7B1G 7B0J 7B16 7B05	Vinayagam et al. (2020). Vinayagam D, Quentin D, Yu-Strzelczyk J, Sitsel O, Merino F, Stabrin M, Hofnagel O, Yu M, Ledeboer MW, Nagel G, Malojcic G, & Raunser S (2020). Structural basis of TRPC4 regulation by calmodulin and pharmacological agents. Elife 9 :e60603. PubMed Id: 33236980. doi:10.7554/eLife.60603.
*TRPC4 ion channel, apo state: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.28 Å** cryo-EM structure	5Z96	Data File Jmol Viewer 5Z96	Duan et al. (2018). Duan J, Li J, Zeng B, Chen GL, Peng X, Zhang Y, Wang J, Clapham DE, Li Z, & Zhang J (2018). Structure of the mouse TRPC4 ion channel. Nat Commun 9 :3102. PubMed Id: 30082700. doi:10.1038/s41467-018-05247-9.
*TRPC5 ion channel, apo state: Homo sapiens* E Eukaryota (expressed in Sf9 cells), 3.00 Å** cryo-EM cells in complex with clemizole, 2.70 Å: 7D4P in complex with HC-070, 2.74 Å: 7D4Q	7E4T	Data File Jmol Viewer 7E4T 7D4Q 7D4P	Song et al. (2021). Song K, Wei M, Guo W, Quan L, Kang Y, Wu JX, & Chen L (2021). Structural basis for human TRPC5 channel inhibition by two distinct inhibitors. Elife 10 :e63429. PubMed Id: 33683200. doi:10.7554/eLife.63429.
*TRPC5 ion channel in complex with riluzole: Homo sapiens* E Eukaryota, 2.40 Å** cryo-EM structure	7WDB	Data File Jmol Viewer 7WDB	Yang et al. (2022). Yang Y, Wei M, & Chen L (2022). Structural identification of riluzole-binding site on human TRPC5. Cell Discov 8 1:67. PubMed Id: 35821012. doi:10.1038/s41421-022-00410-5.
*TRPC5 ion channel in a nanodisc, class 1: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.15 Å** cryo-EM structure class 1, in complex with Gα_i3 subunits, 3.93 Å: 7X6I class 2, 3.59 Å: 8GVW class 2, in complex with Gα_i3 subunits, 3.91 Å: 8GVX	7X6C	Data File Jmol Viewer 7X6C 8GVW 7X6I 8GVX	Won et al. (2023). Won J, Kim J, Jeong H, Kim J, Feng S, Jeong B, Kwak M, Ko J, Im W, So I, & Lee HH (2023). Molecular architecture of the Gαi-bound TRPC5 ion channel. Nat Commun 14 1:2550. PubMed Id: 37137991. doi:10.1038/s41467-023-38281-3.
*TRPC6 ion channel in complex with antagonist AM-1473: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.08 Å** cryo-EM structure in complex with agonist AM-0883, 2.84 Å: 6UZ8	6UZA	Data File Jmol Viewer 6UZA 6UZ8	Bai et al. (2020). Bai Y, Yu X, Chen H, Horne D, White R, Wu X, Lee P, Gu Y, Ghimire-Rijal S, Lin DC, & Huang X (2020). Structural basis for pharmacological modulation of the TRPC6 channel. Elife 9 :e53311. PubMed Id: 32149605. doi:10.7554/eLife.53311.
*TRPC6 ion channel in a nanodisc, high calcium state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure SAR7334-bound, 2.90 Å: 7DXG	7DXF	Data File Jmol Viewer 7DXF 7DXG	Guo et al. (2022). Guo W, Tang Q, Wei M, Kang Y, Wu JX, & Chen L (2022). Structural mechanism of human TRPC3 and TRPC6 channel regulation by their intracellular calcium-binding sites. Neuron 110 6:1023-1035.e5. PubMed Id: 35051376. doi:10.1016/j.neuron.2021.12.023.
*TRPM2 Ca²⁺-activated transient receptor potential channel, Ca²⁺-bound closed state: Nematostella vectensis* E Eukaryota (expressed in S. frugiperda), 3.07 Å** cryo-EM structure	6CO7	Data File Jmol Viewer 6CO7	Zhang et al. (2018). Zhang Z, Tóth B, Szollosi A, Chen J, & Csanády L (2018). Structure of a TRPM2 channel in complex with Ca²⁺ explains unique gating regulation. Elife 7 :e36409. PubMed Id: 29745897. doi:10.7554/eLife.36409.
*TRPM2 ion channel, apo state: Danio rerio* E Eukaryota (expressed in HEK293 cells), 3.8 Å** cryo-EM structure with bound ADP-ribose and Ca²⁺, 3.3 Å: 6DRJ	6DRK	Data File Jmol Viewer 6DRK 6DRJ	Huang et al. (2018). Huang Y, Winkler PA, Sun W, Lü W, & Du J (2018). Architecture of the TRPM2 channel and its activation mechanism by ADP-ribose and calcium. Nature 562 7725:145-149. PubMed Id: 30250252. doi:10.1038/s41586-018-0558-4.
*TRPM2 ion channel in apo state processed with C4 symmetry: Danio rerio* E Eukaryota (expressed in Sf9 cells), 4.3 Å** cryo-EM structure processed with C2 symmetry, 4.5 Å: 6PKW in the presence of Ca²⁺, 3.8 Å: 6D73 in the presence of ADPR and Ca²⁺, 4.2 Å: 6PKX	6PKV	Data File Jmol Viewer 6PKV 6PKX 6PKW 6D73	Yin et al. (2019). Yin Y, Wu M, Hsu AL, Borschel WF, Borgnia MJ, Lander GC, & Lee SY (2019). Visualizing structural transitions of ligand-dependent gating of the TRPM2 channel. Nat Commun 10 1. PubMed Id: 31431622. doi:10.1038/s41467-019-11733-5.
*TRPM2 ion channel, apo form: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.6 Å** cryo-EM structure ADPR-bound state, 6.1 Å: 6MIZ calcium- and ADPR-bound state, 6.36 Å: 6MJ2	6MIX	Data File Jmol Viewer 6MIX 6MJ2 6MIZ	Wang et al. (2018). Wang L, Fu TM, Zhou Y, Xia S, Greka A, & Wu H (2018). Structures and gating mechanism of human TRPM2. Science 362 6421. PubMed Id: 30467180. doi:10.1126/science.aav4809.
*TRPM2 ion channel, apo form: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.3 Å** cryo-EM structure bound to ADPR, 4.4 Å: 6PUR bound to ADPR and calcium, 3.7 Å: 6PUS bound to 8-Br-cADPR and calcium, 3.7 Å: 6PUU	6PUO	Data File Jmol Viewer 6PUO 6PUR 6PUU 6PUS	Huang et al. (2019). Huang Y, Roth B, Lü W, & Du J (2019). Ligand recognition and gating mechanism through three ligand-binding sites of human TRPM2 channel. Elife 8 . PubMed Id: 31513012. doi:10.7554/eLife.50175.
*TRPM2 ion channel, apo form: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.76 Å** cryo-EM structure channel TM domain, 3.68 Å 7VQ2	7VQ1	Data File Jmol Viewer 7VQ1 7VQ2	Yu et al. (2021). Yu X, Xie Y, Zhang X, Ma C, Liu L, Zhen W, Xu L, Zhang J, Liang Y, Zhao L, Gao X, Yu P, Luo J, Jiang LH, Nie Y, Yang F, Guo J, & Yang W (2021). Structural and functional basis of the selectivity filter as a gate in human TRPM2 channel. Cell Rep 37 7:110025. PubMed Id: 34788616. doi:10.1016/j.celrep.2021.110025.
*TRPM2 ion channel, apo form: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.18 Å** cryo-EM structure	7DYS	Data File Jmol Viewer 7DYS	Song et al. (2022). Song X, Li J, Tian M, Zhu H, Hu X, Zhang Y, Cao Y, Ye H, McCormick PJ, Zeng B, Fu Y, Duan J, & Zhang J (2022). Cryo-EM structure of mouse TRPML2 in lipid nanodiscs. J Biol Chem 298 2:e101487. PubMed Id: 34915027. doi:10.1016/j.jbc.2021.101487.
*TRPM4 Ca²⁺-activated transient receptor potential channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.8 Å** cryo-EM structure	5WP6	Data File Jmol Viewer 5WP6	Winkler et al. (2017). Winkler PA, Huang Y, Sun W, Du J, & Lü W (2017). Electron cryo-microscopy structure of a human TRPM4 channel. Nature 552 7684:200-204. PubMed Id: 29211723. doi:10.1038/nature24674.
*TRPM4 Ca²⁺-activated transient receptor potential channel in lipid nanodisc (calcium-free state): Homo sapiens* E Eukaryota (expressed in HEK 293 cells), 3.2 Å** cryo-EM structure with CaCl₂, 3.1 Å: 6BQV	6BQR	Data File Jmol Viewer 6BQR 6BQV	Autzen et al. (2018). Autzen HE, Myasnikov AG, Campbell MG, Asarnow D, Julius D, & Cheng Y (2018). Structure of the human TRPM4 ion channel in a lipid nanodisc. Science 359 :228-232. PubMed Id: 29217581. doi:10.1126/science.aar4510.
*TRPM4 Ca²⁺-activated transient receptor potential channel, full length: Homo sapiens* E Eukaryota (expressed in HEK 293S cells), 3.7 Å** cryo-EM structure.	6BWI	Data File Jmol Viewer 6BWI	Duan et al. (2018). Duan J, Li Z, Li J, Santa-Cruz A, Sanchez-Martinez S, Zhang J, & Clapham DE (2018). Structure of full-length human TRPM4. Proc Natl Acad Sci USA 115 10:2377-2382. PubMed Id: 29463718. doi:10.1073/pnas.1722038115.
*TRPM4 Ca²⁺-activated TRP channel, apo state with short coiled-coil: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.14 Å** cryo-EM structure apo state, long coiled-coil, 3.54 Å: 6BCL ATP-bound state, short coiled-coil, 2.9 Å: 6BCO ATP-bound state, long coiled-coil, 3.25 Å: 6BCQ	6BCJ	Data File Jmol Viewer 6BCJ 6BCQ 6BCL 6BCO	Guo et al. (2017). Guo J, She J, Zeng W, Chen Q, Bai XC, & Jiang Y (2017). Structures of the calcium-activated, non-selective cation channel TRPM4. Nature 552 7684:205-209. PubMed Id: 29211714. doi:10.1038/nature24997.
*TRPM7 α-kinase and divalent-ion permeable channel in the presence of EDTA: Mus musculus* E Eukaryota (expressed in Spodoptera frugiperda), 3.3 Å** cryo-EM structure with bound Mg²⁺, 3.7 Å: 6BWD divalent-free structure, 4.1 Å: 6BWF	5ZX5	Data File Jmol Viewer 5ZX5 6BWF 6BWD	Duan et al. (2018). Duan J, Li Z, Li J, Hulse RE, Santa-Cruz A, Valinsky WC, Abiria SA, Krapivinsky G, Zhang J, & Clapham DE (2018). Structure of the mammalian TRPM7, a magnesium channel required during embryonic development. Proc Natl Acad Sci USA 115 35:E8201-E8210. PubMed Id: 30108148. doi:10.1073/pnas.1810719115.
*TRPM8 cold- & menthol-sensing channel: Ficedula albicollis* E Eukaryota (expressed in HEK 293 cells), 4.1 Å** cryo-EM structure	6BPQ	Data File Jmol Viewer 6BPQ	Yin et al. (2018). Yin Y, Wu M, Zubcevic L, Borschel WF, Lander GC, & Lee SY (2018). Structure of the cold- and menthol-sensing ion channel TRPM8. Science 359 :237-241. PubMed Id: 29217583. doi:10.1126/science.aan4325.
*TRPM8 cold- & menthol-sensing channel in complex with high occupancy icilin, PI(4,5)P2, and calcium: Ficedula albicollis* E Eukaryota (expressed in HEK293 cells), 3.4 Å** cryo-EM structure in complex with with low occupancy icilin, PI(4,5)P2, and calcium; 4.3 Å: 6NR4 in complex with the menthol analog WS-12 and PI(4,5)P2; 4 Å: 6NR2	6NR3	Data File Jmol Viewer 6NR3 6NR4 6NR2	Yin et al. (2019). Yin Y, Le SC, Hsu AL, Borgnia MJ, Yang H, & Lee SY (2019). Structural basis of cooling agent and lipid sensing by the cold-activated TRPM8 channel. Science 363 6430. PubMed Id: 30733385. doi:10.1126/science.aav9334.
*TRPM8 cold- & menthol-sensing channel in amphipols, ligand-free: Ficedula albicollis* E Eukaryota (expressed in HEK293 cells), 3.6 Å** cryo-EM structure AMTB-bound, 3.2 Å: 6O6R TC-I 2014-bound state, 3 Å: 6O72 calcium-bound state, 3.2 Å: 6O77	6O6A	Data File Jmol Viewer 6O6A 6O72 6O77 6O6R	Diver et al. (2019). Diver MM, Cheng Y, & Julius D (2019). Structural insights into TRPM8 inhibition and desensitization. Science 365 :1434-1440. PubMed Id: 31488702. doi:10.1126/science.aax6672.
*TRPM8 cold- & menthol-sensing channel in complex with PI(4,5)P2: Ficedula albicollis* E Eukaryota (expressed in HEK293 cells), 3.51 Å** cryo-EM structure	8E4Q	Data File Jmol Viewer 8E4Q	Yin et al. (2022). Yin Y, Zhang F, Feng S, Butay KJ, Borgnia MJ, Im W, & Lee SY (2022). Activation mechanism of the mouse cold-sensing TRPM8 channel by cooling agonist and PIP2. Science 378 6616:eadd1268. PubMed Id: 36227998. doi:10.1126/science.add1268.
*TRPM8 cold- & menthol-sensing channel. Ligand- and PI(4,5)P2-free condition, Class I, C0 state: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.59 Å** cryo-EM structure closed C1-state, in complex with putative PI(4,5)P2, 3.43 Å: 8E4O closed C1-state, in complex with PI(4,5)P2, 3.07 Å: 8E4N intermediate C2-state, in complex with the cooling agonist C3 and PI(4,5)P2, 3.44 Å: 8E4M open state, in complex with the cooling agonist C3, AITC, and PI(4,5)P2, 3.32 Å: 8E4L	8E4P	Data File Jmol Viewer 8E4P 8E4O 8E4N 8E4L 8E4M	Yin et al. (2022). Yin Y, Zhang F, Feng S, Butay KJ, Borgnia MJ, Im W, & Lee SY (2022). Activation mechanism of the mouse cold-sensing TRPM8 channel by cooling agonist and PIP2. Science 378 6616:eadd1268. PubMed Id: 36227998. doi:10.1126/science.add1268.
*Endolysosomal TRPML1 channel in nanodiscs: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.59 Å** cryo-EM structure closed I conformation, 3.64 Å: 5WPQ closed II conformation, 3.75 Å: 5WPT	5WPV	Data File Jmol Viewer 5WPV 5WPQ 5WPT	Chen et al. (2017). Chen Q, She J, Zeng W, Guo J, Xu H, Bai XC, & Jiang Y (2017). Structure of mammalian endolysosomal TRPML1 channel in nanodiscs. Nature 550 :415-418. PubMed Id: 29019981. doi:10.1038/nature24035.
*Endolysosomal TRPML1 channel: Mus musculus* E Eukaryota (expressed in HEK293 cells), 2.60 Å** cryo-EM structure PI(3,5)P₂-bound, 2.41 Å 7SQ7 temsirolimus/PI(3,5)P₂-bound, 2.11 Å 7SQ9	7SQ8	Data File Jmol Viewer 7SQ8 7SQ7 7SQ9	Gan et al. (2022). Gan N, Han Y, Zeng W, Wang Y, Xue J, & Jiang Y (2022). Structural mechanism of allosteric activation of TRPML1 by PI(3,5)P₂ and rapamycin. Proc Natl Acad Sci U S A 119 7:e2120404119. PubMed Id: 35131932. doi:10.1073/pnas.2120404119.
*TRPML3 ion channel: Callithrix jacchus* E Eukaryota (expressed in S. frugiperda), 2.94 Å** cryo-EM structure	5W3S	Data File Jmol Viewer 5W3S	Hirschi et al. (2017). Hirschi M, Herzik MA Jr, Wie J, Suo Y, Borschel WF, Ren D, Lander GC, & Lee SY (2017). Cryo-electron microscopy structure of the lysosomal calcium-permeable channel TRPML3. Nature 550 :411-414. PubMed Id: 29019979. doi:10.1038/nature24055.
*TRPML3 ion channel, apo protein at pH 7.4: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 4.06 Å** cryo-EM structure ML-SA1 complex at pH 7.4, 3.62 Å: 6AYF apo-form at pH 4.8, 4.65 Å: 6AYG	6AYE	Data File Jmol Viewer 6AYE 6AYG 6AYF	Zhou et al. (2017). Zhou X, Li M, Su D, Jia Q, Li H, Li X, & Yang J (2017). Cryo-EM structures of the human endolysosomal TRPML3 channel in three distinct states. Nat Struct Mol Biol 24 12:1146-1154. PubMed Id: 29106414. doi:10.1038/nsmb.3502.
*TRPV1 transient receptor potential channel capsaicin receptor: Rattus norvegicus* E Eukaryota (expressed in HEK293S GnTI^- cells), 3.275 Å** cryo-EM structure Not only is this the first structure of a TRP channel, it is the first membrane protein whose structure was determined at atomic-resolution using single-particle cryo-EM.	3J5P	Data File Jmol Viewer 3J5P	Liao et al. (2013). Liao M, Cao E, Julius D, & Cheng Y (2013). Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504 :107-112. PubMed Id: 24305160. doi:10.1038/nature12822.
*TRPV1 transient receptor potential channel in complex with vanilloid agonist RTX: Rattus norvegicus* E Eukaryota (expressed in HEK293S GnTI^- cells), 3.8 Å** in complex with capsaicin, 4.2 Å: 3J5R	3J5Q	Data File Jmol Viewer 3J5Q 3J5R	Cao et al. (2013). Cao E, Liao M, Cheng Y, & Julius D (2013). TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504 :113-118. PubMed Id: 24305161. doi:10.1038/nature12823.
*TRPV1 transient receptor potential channel in nanodiscs: Rattus norvegicus* E Eukaryota (expressed in HEK293S GnTI^- cells), 3.28 Å** cryoEM structure in complex with DkTx and RTX, 2.95 Å: 5IRX in complex with capsazepine, 3.43 Å: 5IS0	5IRZ	Data File Jmol Viewer 5IRZ 5IRX 5IS0	Gao et al. (2016). Gao Y, Cao E, Julius D, & Cheng Y (2016). TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action. Nature 534 :347-351. PubMed Id: 27281200. doi:10.1038/nature17964.
*TRPV1 transient receptor potential channel, T = 4ºC: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 2.63 Å** cryo-EM structure with capsaicin at 4ºC, 3.37 Å: 7LPA 48ºC, 3.06 Å: 7LPC with capsaicin at 25ºC, 3.54 Å: 7LPB with capsaicin at 48ºC (intermediate state, class 2), 3.55 Å: 7LPD with capsaicin at 48ºC (open state, class 1), 3.72 Å: 7LPE	7LP9	Data File Jmol Viewer 7LP9 7LPA 7LPD 7LPC 7LPE 7LPB	Kwon et al. (2021). Kwon DH, Zhang F, Suo Y, Bouvette J, Borgnia MJ, & Lee SY (2021). Heat-dependent opening of TRPV1 in the presence of capsaicin. Nat Struct Mol Biol 28 7:554-563. PubMed Id: 34239123. doi:10.1038/s41594-021-00616-3.
*TRPV1 transient receptor potential channel, unliganded minimal TRPV1: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 2.60 Å** cryo-EM structure DkTx-bound minimal TRPV1 at the pre-bound state, 2.71 Å 7L2S DkTx-bound minimal TRPV1 at the pre-open state, 3.30 Å 72LR DkTx-bound minimal TRPV1 in partial open state, 3.08 Å 7L2T DkTx-bound minimal TRPV1 in open state, 3.47 Å 7L2U RTX-bound minimal TRPV1 with NMDG at state a, 3.16 Å 7L2W RTX-bound minimal TRPV1 with NMDG at state b, 3.64 Å 7L2V RTX-bound minimal TRPV1 with NMDG at state c, 3.26 Å 7L2X minimal TRPV1 with 1 perturbed PI, 2.91 Å 7MZ6 minimal TRPV1 with 1 partially bound RTX, 3.18 Å 7MZ9 minimal TRPV1 with 4 partially bound RTX, 3.35 Å 7MZ7 minimal TRPV1 with 2 bound RTX in adjacent pockets, 3.46 Å 7MZA minimal TRPV1 with 2 bound RTX in opposite pockets, 3.42 Å 7MZE minimal TRPV1 with 3 bound RTX and 1 perturbed PI, 3.72 Å 7MZB minimal TRPV1 with RTX bound in C1 state, 3.03 Å 7MZC minimal TRPV1 with RTX bound in C2 state, 2.90 Å 7MZD unliganded full-length TRPV1 at neutral pH, 2.63 Å 7L2H DkTx/RTX-bound full-length TRPV1, 3.84 Å 7L2M RTX-bound full-length TRPV1 in C1 state, 3.09 Å 7L2N RTX-bound full-length TRPV1 in O1 state, 3.42 Å 7L2L RTX-bound full-length TRPV1 in C2 state, 2.76 Å 7MZ5 full-length TRPV1 at pH6a state, 3.70 Å 7L2I full-length TRPV1 at pH6b state, 3.89 Å 7L2K full-length TRPV1 at pH6c state, 3.66 Å 7L2J RTX-bound full-length TRPV1 at pH 5.5, 3.64 Å 7L2O	7L2P	Data File Jmol Viewer 7L2P 7MZ7 7L2M 7MZ9 7MZD 7L2T 7MZE 7L2N 7L2J 7L2S 7L2K 7L2W 7L2X 7L2H 7L2I 7L2V 7MZ6 7MZC 7L2O 7L2U 72LR 7MZB 7MZ5 7MZA 7L2L	Zhang et al. (2021). Zhang K, Julius D, & Cheng Y (2021). Structural snapshots of TRPV1 reveal mechanism of polymodal functionality. Cell 184 20:5138-5150.e12. PubMed Id: 34496225. doi:10.1016/j.cell.2021.08.012.
*full-length TRPV1 with RTx at 4°C, in a closed state, class I: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.05 Å** cryo-EM structure in an intermediate-closed state, class II, 3.45 Å: 7RQV in an open state, class III, 3.11 Å: 7RQW 25°C, in an intermediate-open state, class A, 3.36 Å: 7RQX 25°C, in an open state, class B, 3.04 Å: 7RQY 48°C in an open state, class alpha, 3.32 Å: 7RQZ	7RQU	Data File Jmol Viewer 7RQU 7RQZ 7RQV 7RQY 7RQX 7RQW	Kwon et al. (2022). Kwon DH, Zhang F, Fedor JG, Suo Y, & Lee SY (2022). Vanilloid-dependent TRPV1 opening trajectory from cryoEM ensemble analysis. Nat Commun 13 1:2874. PubMed Id: 35610228. doi:10.1038/s41467-022-30602-2.
*TRPV1 transient receptor potential channel, apo state: Ictidomys tridecemlineatus* E Eukaryota (expressed in HEK293 cells), 3.19 Å** cryo-EM structure in complex with RTX, 3.41 Å: 7LQZ in complex with capsaicin, 3.81 Å: 7LR0	7LQY	Data File Jmol Viewer 7LQY 7LR0 7LQZ	Nadezhdin et al. (2021). Nadezhdin KD, Neuberger A, Nikolaev YA, Murphy LA, Gracheva EO, Bagriantsev SN, & Sobolevsky AI (2021). Extracellular cap domain is an essential component of the TRPV1 gating mechanism. Nat Commun 12 1:2154. PubMed Id: 33846324. doi:10.1038/s41467-021-22507-3.
*TRPV1 transient receptor potential channel, in cNW11 nanodisc and soybean lipids: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure POPC:POPE:POPG lipid nanodisc, 2.58 Å: 8GF9 in complex with the analgesic drug SB-366791, 2.29 Å: 8GFA	8GF8	Data File Jmol Viewer 8GF8 8GF9 8GFA	Neuberger et al. (2023). Neuberger A, Oda M, Nikolaev YA, Nadezhdin KD, Gracheva EO, Bagriantsev SN, & Sobolevsky AI (2023). Human TRPV1 structure and inhibition by the analgesic SB-366791. Nat Commun 14 1:2451. PubMed Id: 37117175. doi:10.1038/s41467-023-38162-9.
*TRPV2 transient receptor potential channel: Oryctolagus cuniculus* E Eukaryota (expressed in S. frugiperda), 4 Å** cryo-EM structure	5AN8	Data File Jmol Viewer 5AN8	Zubcevic et al. (2016). Zubcevic L, Herzik MA Jr, Chung BC, Liu Z, Lander GC, & Lee SY (2016). Cryo-electron microscopy structure of the TRPV2 ion channel. Nat Struct Mol Biol 23 :180-186. PubMed Id: 26779611. doi:10.1038/nsmb.3159.
*TRPV2 transient receptor potential channel, Ca²⁺ bound: Oryctolagus cuniculus* E Eukaryota (expressed in S. frugiperda), 3.9 Å** in complex with RTx, 3.1 Å: 6BWJ	6BWM	Data File Jmol Viewer 6BWM 6BWJ	Zubcevic et al. (2018). Zubcevic L, Le S, Yang H, & Lee SY (2018). Conformational plasticity in the selectivity filter of the TRPV2 ion channel. Nat Struct Mol Biol 25 5:405-415. PubMed Id: 29728656. doi:10.1038/s41594-018-0059-z.
*TRPV2 transient receptor potential channel: C4-symmetric TRPV2/RTx complex in amphipol: Oryctolagus cuniculus* E Eukaryota (expressed in S. frugiperda), 2.9 Å** cryo-EM structure C2-symmetric TRPV2/RTx complex, 3.3 Å: 6OO4 C2-symmetric TRPV2/RTx complex, 4.2 Å: 6OO5 C2-symmetric TRPV2/RTx complex in nanodiscs, 3.8 Å: 6OO7	6OO3	Data File Jmol Viewer 6OO3 6OO4 6OO5 6OO7	Zubcevic et al. (2019). Zubcevic L, Hsu AL, Borgnia MJ, & Lee SY (2019). Symmetry transitions during gating of the TRPV2 ion channel in lipid membranes. Elife 8 :e45779. PubMed Id: 31090543. doi:10.7554/eLife.45779.
*TRPV2 channel, full-length: Rattus norvegicus* E Eukaryota (expressed in S. cerevisiae), 4.4 Å** cryo-EM structure	5HI9	Data File Jmol Viewer 5HI9	Huynh et al. (2016). Huynh KW, Cohen MR, Jiang J, Samanta A, Lodowski DT, Zhou ZH, & Moiseenkova-Bell VY (2016). Structure of the full-length TRPV2 channel by cryo-EM. Nat Commun 7 :11130. PubMed Id: 27021073. doi:10.1038/ncomms11130.
*TRPV2 channel, full-length with resolved pore turret domain: Rattus norvegicus* E Eukaryota (expressed in S. cerevisiae), 4.0 Å** cryo-EM structure channel in partially closed state, 3.6 Å: 6BO5	6BO4	Data File Jmol Viewer 6BO4 6BO5	Dosey et al. (2019). Dosey TL, Wang Z, Fan G, Zhang Z, Serysheva II, Chiu W, & Wensel TG (2019). Structures of TRPV2 in distinct conformations provide insight into role of the pore turret. Nat Struct Mol Biol 26 1:40-49. PubMed Id: 30598551. doi:10.1038/s41594-018-0168-8.
*TRPV2 channel full length in nanodiscs, apo state 1: Rattus norvegicus* E Eukaryota (expressed in S. cerevisiae), 3.7 Å** cryo-EM structure apo state 2, 4 Å: 6U86 CBD-bound, state 1, 3.4 Å: 6U8A CBD-bound, state 2, 3.2 Å: 6U88	6U84	Data File Jmol Viewer 6U84 6U86 6U88 6U8A	Pumroy et al. (2019). Pumroy RA, Samanta A, Liu Y, Hughes TE, Zhao S, Yudin Y, Rohacs T, Han S, & Moiseenkova-Bell VY (2019). Molecular mechanism of TRPV2 channel modulation by cannabidiol. Elife 8 :e48792. PubMed Id: 31566564. doi:10.7554/eLife.48792.
*TRPV2 channel in nanodiscs with bound piperlongumine: Rattus norvegicus* E Eukaryota (expressed in Saccharomyces cerevisiae), 3.46 Å** cryo-EM structure	6WKN	Data File Jmol Viewer 6WKN	Conde et al. (2021). Conde J, Pumroy RA, Baker C, Rodrigues T, Guerreiro A, Sousa BB, Marques MC, de Almeida BP, Lee S, Leites EP, Picard D, Samanta A, Vaz SH, Sieglitz F, Langini M, Remke M, Roque R, Weiss T, Weller M, Liu Y, Han S, Corzana F, Morais VA, Faria CC, Carvalho T, Filippakopoulos P, Snijder B, Barbosa-Morais NL, Moiseenkova-Bell VY, & Bernardes GJL (2021). Allosteric Antagonist Modulation of TRPV2 by Piperlongumine Impairs Glioblastoma Progression. ACS Cent Sci 7 5:868-881. PubMed Id: 34079902. doi:10.1021/acscentsci.1c00070.
*TRPV2 channel in nanodiscs with bound 1 CBD (conformation A): Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.23 Å** cryo-EM structure with bound 2 CBDs (conformation B), 3.32 Å: 8SLY	8SLX	Data File Jmol Viewer 8SLX 8SLY	Gochman et al. (2023). Gochman A, Tan XF, Bae C, Chen H, Swartz KJ, & Jara-Oseguera A (2023). Cannabidiol sensitizes TRPV2 channels to activation by 2-APB. Elife 12 :e86166. PubMed Id: 37199723. doi:10.7554/eLife.86166.
*TRPV2 channel in nanodiscs with bound ruthenium red: Rattus norvegicus* E Eukaryota (expressed in S. cerevisiae), 3.47 Å** cryo-EM structure with bound ruthenium red and 2-APB, 2.90 Å: 8FFM	8FFL	Data File Jmol Viewer 8FFL 8FFM	Pumroy et al. (2024). Pumroy RA, De Jesús-Pérez JJ, Protopopova AD, Rocereta JA, Fluck EC, Fricke T, Lee BH, Rohacs T, Leffler A, & Moiseenkova-Bell V (2024). Molecular details of ruthenium red pore block in TRPV channels. EMBO Rep 25 2:506-523. PubMed Id: 38225355. doi:10.1038/s44319-023-00050-0.
*TRPV2 transient receptor potential channel, cholesterol-bound state: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.17 Å** cryo-EM structure MbetaCD treated state, 2.89 Å: 7XEO Q525F mutant, 2.59 Å: 7XEW TRPV2_E2, 2.77 Å: 7XEU TRPV2_2-APB, 3.27 Å: 7XEV 2-APB bound state, 2.83 Å: 7YEP	7XEM	Data File Jmol Viewer 7XEM 7XEW 7YEP 7XEO 7XEV 7XEU	Su et al. (2023). Su N, Zhen W, Zhang H, Xu L, Jin Y, Chen X, Zhao C, Wang Q, Wang X, Li S, Wen H, Yang W, Guo J, & Yang F (2023). Structural mechanisms of TRPV2 modulation by endogenous and exogenous ligands. Nat Chem Biol 19 1:72-80. PubMed Id: 36163384. doi:10.1038/s41589-022-01139-8.
*TRPV3 transient receptor potential channel: Mus musculus* E Eukaryota (expressed in sf9 cells), 4.3 Å** cryo-EM structure in complex with 2-APB, 4 Å: 6DVY Y564A mutant in complex with 2-APB, 4.24 Å: 6DVZ	6DVW	Data File Jmol Viewer 6DVW 6DVZ 6DVY	Singh et al. (2018). Singh AK, McGoldrick LL, & Sobolevsky AI (2018). Structure and gating mechanism of the transient receptor potential channel TRPV3. Nat Struct Mol Biol 25 9:805-813. PubMed Id: 30127359. doi:10.1038/s41594-018-0108-7.
*TRPV3 transient receptor potential channel, closed state at 42°C: Mus musculus* E Eukaryota (expressed in HEK293 cells), 4.4 Å** cryo-EM structure putative sensitized state at 42°C, 4.5 Å: 6PVM Y564A mutant in putative sensitized state at 4°C, 4.07 Å: 6PVN Y564A mutant in putative sensitized state at 37°C, 5.18 Å: 6PVO Y564A mutant in open state at 37°C, 4.48 Å: 6PVP Y564A mutant in intermediate state at 37°C, 4.75 Å: 6PVQ	6PVL	Data File Jmol Viewer 6PVL 6PVQ 6PVM 6PVN 6PVO 6PVP	Singh et al. (2019). Singh AK, McGoldrick LL, Demirkhanyan L, Leslie M, Zakharian E, & Sobolevsky AI (2019). Structural basis of temperature sensation by the TRP channel TRPV3. Nat Struct Mol Biol 26 :994-998. PubMed Id: 31636415. doi:10.1038/s41594-019-0318-7.
*TRPV3 transient receptor potential channel in a lipid nanodisc: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	6LGP	Data File Jmol Viewer 6LGP	Shimada et al. (2020). Shimada H, Kusakizako T, Dung Nguyen TH, Nishizawa T, Hino T, Tominaga M, & Nureki O (2020). The structure of lipid nanodisc-reconstituted TRPV3 reveals the gating mechanism. Nat Struct Mol Biol 27 7:645-652. PubMed Id: 32572254. doi:10.1038/s41594-020-0439-z.
*TRPV3 transient receptor potential channel in MSP2N2 nanodiscs, closed state at 4C: Mus musculus* E Eukaryota (expressed in HEK293 cells), 1.98 Å** cryo-EM structure closed state at 42C, 3.12 Å: 7MIK sensitized state at 42C, 3.86 Å: 7MIL in cNW11 nanodiscs, closed state at 4C, 3.42 Å: 7MIM in cNW11 nanodiscs, closed state at 42C, 3.09 Å: 7MIN in cNW11 nanodiscs, open state at 42C, 3.48 Å: 7MIO	7MIJ	Data File Jmol Viewer 7MIJ 7MIM 7MIN 7MIK 7MIO 7MIL	Nadezhdin et al. (2021). Nadezhdin KD, Neuberger A, Trofimov YA, Krylov NA, Sinica V, Kupko N, Vlachova V, Zakharian E, Efremov RG, & Sobolevsky AI (2021). Structural mechanism of heat-induced opening of a temperature-sensitive TRP channel. Nat Struct Mol Biol 28 7:564-572. PubMed Id: 34239124. doi:10.1038/s41594-021-00615-4.
*TRPV3 transient receptor potential channel. Y564A mutant in complex with osthole: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.64 Å** cryo-EM structure in presence of 2APB, 3.99 Å 7RAU	7RAS	Data File Jmol Viewer 7RAS 7RAU	Neuberger et al. (2021). Neuberger A, Nadezhdin KD, Zakharian E, & Sobolevsky AI (2021). Structural mechanism of TRPV3 channel inhibition by the plant-derived coumarin osthole. EMBO Rep 22 11:e53233. PubMed Id: 34472684. doi:10.15252/embr.202153233.
*TRPV3 transient receptor potential channel in complex with anesthetic dyclonine: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.16 Å** cryo-EM structure	7UGG	Data File Jmol Viewer 7UGG	Neuberger et al. (2022). Neuberger A, Nadezhdin KD, & Sobolevsky AI (2022). Structural mechanism of TRPV3 channel inhibition by the anesthetic dyclonine. Nat Commun 13 1:2795. PubMed Id: 35589741. doi:10.1038/s41467-022-30537-8.
*TRPV3 transient receptor potential channel in apo conformation: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.4 Å** cryo-EM structure in putative sensitized conformation, 3.2 Å: 6MHS in the presence of 2-APB in C4 symmetry, 3.5 Å: 6MHV in the presence of 2-APB in C2 symmetry (1), 4 Å: 6MHW in the presence of 2-APB in C2 symmetry (2), 4 Å: 6MHX	6MHO	Data File Jmol Viewer 6MHO 6MHV 6MHX 6MHW 6MHS	Zubcevic et al. (2018). Zubcevic L, Herzik MA Jr, Wu M, Borschel WF, Hirschi M, Song AS, Lander GC, & Lee SY (2018). Conformational ensemble of the human TRPV3 ion channel. Nat Commun 9 1. PubMed Id: 30429472. doi:10.1038/s41467-018-07117-w.
*TRPV3 transient receptor potential channel, K169A sensitized mutant: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 4.1 Å** cryo-EM structure K169A sensitized mutant in the presence of 2-APB, 3.6 Å: 6OT5	6OT2	Data File Jmol Viewer 6OT2 6OT5	Zubcevic et al. (2019). Zubcevic L, Borschel WF, Hsu AL, Borgnia MJ, & Lee SY (2019). Regulatory switch at the cytoplasmic interface controls TRPV channel gating. Elife 8 :e47746. PubMed Id: 31070581. doi:10.7554/eLife.47746.
*TRPV3 transient receptor potential channel in lipid nanodisc: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 3.10 Å** cryo-EM structure K169A mutant, 3.66 Å: 6UW6 K169A mutant exposed to 2-APB for 3 mins., 4.02 Å: 6UW8 K169A mutant in the presence of 2-APB, 4.33 Å: 6UW9	6UW4	Data File Jmol Viewer 6UW4 6UW6 6UW9 6UW8	Deng et al. (2020). Deng Z, Maksaev G, Rau M, Xie Z, Hu H, Fitzpatrick JAJ, & Yuan P (2020). Gating of human TRPV3 in a lipid bilayer. Nat Struct Mol Biol 27 7:635-644. PubMed Id: 32572252. doi:10.1038/s41594-020-0428-2.
*TRPV3 transient receptor potential channel, apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.54 Å** cryo-EM structure in complex with Trpvicin, 2.53 Å: 7XJ0 G573S in complex with Trpvicin in C4 symmetry, 3.64 Å: 7XJ2 TRPV3_G573S in complex with Trpvicin in C2 symmetry, 2.93 Å: 7XJ1	7XJ3	Data File Jmol Viewer 7XJ3 7XJ0 7XJ2 7XJ1	Fan et al. (2023). Fan J, Hu L, Yue Z, Liao D, Guo F, Ke H, Jiang D, Yang Y, & Lei X (2023). Structural basis of TRPV3 inhibition by an antagonist. Nat Chem Biol 19 1:81-90. PubMed Id: 36302896. doi:10.1038/s41589-022-01166-5.
*TRPV3 transient receptor potential channel, pentamer: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.38 Å** cryo-EM structure tetramer, 2.55 Å: 8GKA	8GKG	Data File Jmol Viewer 8GKG 8GKA	Lansky et al. (2023). Lansky S, Betancourt JM, Zhang J, Jiang Y, Kim ED, Paknejad N, Nimigean CM, Yuan P, & Scheuring S (2023). A pentameric TRPV3 channel with a dilated pore. Nature 621 7977:206-214. PubMed Id: 37648856. doi:10.1038/s41586-023-06470-1.
*TRPV4 transient receptor potential channel: Xenopus tropicalis* E Eukaryota (expressed in Pichia pastoris), 3.8 Å** cryo-EM structure. The structures below are by x-ray crystallography: in the presence of cesium, 6.5 Å: 6C8F in the presence of barium, 6.31 Å: 6C8G in the presence of gadolinium, 6.5 Å: 6C8H	6BBJ	Data File Jmol Viewer 6BBJ 6C8G 6C8H 6C8F	Deng et al. (2018). Deng Z, Paknejad N, Maksaev G, Sala-Rabanal M, Nichols CG, Hite RK, & Yuan P (2018). Cryo-EM and X-ray structures of TRPV4 reveal insight into ion permeation and gating mechanisms. Nat Struct Mol Biol 25 :252-260. PubMed Id: 29483651. doi:10.1038/s41594-018-0037-5.
*TRPV4 transient receptor potential channel - RhoA complex, apo: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.75 Å** cryo-EM structure with bound GSK2798745, 3.30 Å: 8FC7 with bound 4alpha-Phorbol 12,13-didecanoate, 3.41 Å: 8FCA with bound GSK1016790A, 3.30 Å: 8FCB TRPV4-only, with bound GSK1016790A, 3.47 Å: 8FC8	8FC9	Data File Jmol Viewer 8FC9 8FCA 8FC7 8FC8 8FCB	Kwon et al. (2023). Kwon DH, Zhang F, McCray BA, Feng S, Kumar M, Sullivan JM, Im W, Sumner CJ, & Lee SY (2023). TRPV4-Rho GTPase complex structures reveal mechanisms of gating and disease. Nat Commun 14 1:3732. PubMed Id: 37353484. doi:10.1038/s41467-023-39345-0.
*TRPV4 transient receptor potential channel - RhoA complex, apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure in complex with agonist 4a-PDD, 3.35 Å: 8T1D closed state in the presence of 4a-PPD, 2.77 Å: 8T1E in complex with antagonist HC-067047, 3.49 Å: 8T1F ankyrin repeat domain in complex with GTPase RhoA, 3.49 Å: 8T1C	8T1B	Data File Jmol Viewer 8T1B 8T1F 8T1E 8T1C 8T1D	Nadezhdin et al. (2023). Nadezhdin KD, Talyzina IA, Parthasarathy A, Neuberger A, Zhang DX, & Sobolevsky AI (2023). Structure of human TRPV4 in complex with GTPase RhoA. Nat Commun 14 1:3733. PubMed Id: 37353478. doi:10.1038/s41467-023-39346-z.
*TRPV4 transient receptor potential channel, apo: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.59 Å** cryo-EM structure with bound GSK101, 3.62 Å: 8J1F with bound GSK101 and Ruthenium Red, 3.72 Å: 8J1B with bound Agonist1 and Ruthenium Red, 3.88 Å: 8J1H	8J1D	Data File Jmol Viewer 8J1D 8J1F 8J1B 8J1H	Zhen et al. (2023). Zhen W, Zhao Z, Chang S, Chen X, Wan Y, & Yang F (2023). Structural basis of ligand activation and inhibition in a mammalian TRPV4 ion channel. Cell Discov 9 1:70. PubMed Id: 37429860. doi:10.1038/s41421-023-00579-3.
*TRPV5 Ca²⁺-selective ion channel with econazole inhibitor: Oryctolagus cuniculus* E Eukaryota (expressed in S. cerevisiae), 4.8 Å** cryo-EM structure. Transmembrane region has 3.5-4.0 Å resolution	6B5V	Data File Jmol Viewer 6B5V	Hughes et al. (2018). Hughes TET, Lodowski DT, Huynh KW, Yazici A, Del Rosario J, Kapoor A, Basak S, Samanta A, Han X, Chakrapani S, Zhou ZH, Filizola M, Rohacs T, Han S, & Moiseenkova-Bell VY (2018). Structural basis of TRPV5 channel inhibition by econazole revealed by cryo-EM. Nat Struct Mol Biol 25 :53-60. PubMed Id: 29323279. doi:10.1038/s41594-017-0009-1.
*TRPV5 Ca²⁺-selective ion channel (residues 1-660) in nanodisc: Oryctolagus cuniculus* E Eukaryota (expressed in HEK293 cells), 2.9 Å** cryo-EM structure full-length protein, 3 Å: 6O1P W583A mutant, 2.8 Å: 6O1U with bound calmodulin, 3.3 Å: 6O20	6O1N	Data File Jmol Viewer 6O1N 6O1U 6O20 6O1P	Dang et al. (2019). Dang S, van Goor MK, Asarnow D, Wang Y, Julius D, Cheng Y, & van der Wijst J (2019). Structural insight into TRPV5 channel function and modulation. Proc Natl Acad Sci USA 116 18:8869-8878. PubMed Id: 30975749. doi:10.1073/pnas.1820323116.
*TRPV5 Ca²⁺-selective ion channel in nanodiscs, with bound ZINC9155420 inhibitor: Oryctolagus cuniculus* E Eukaryota (expressed in S. cerevisiae), 4.2 Å** cryo-EM structure with bound ZINC17988990 inhibitor, 3.78 Å: 6PBE	6PBF	Data File Jmol Viewer 6PBF 6PBE	Hughes et al. (2019). Hughes TE, Del Rosario JS, Kapoor A, Yazici AT, Yudin Y, Fluck EC 3rd, Filizola M, Rohacs T, & Moiseenkova-Bell VY (2019). Structure-based characterization of novel TRPV5 inhibitors. Elife 8 . PubMed Id: 31647410. doi:10.7554/eLife.49572.
*TRPV5 Ca²⁺-selective ion channel in nanodiscs: Oryctolagus cuniculus* E Eukaryota (expressed in Saccharomyces cerevisiae), 3.20 Å** cryo-EM structure at pH6, 3.00 Å: 7T6K at pH5, 3.70 Å: 7T6L with PI(4,5)P2 at pH6 state 1, 2.80 Å: 7T6M at pH6 state 2, 2.90 Å: 7T6N at pH6 state 3, 2.60 Å: 7T6O T709D mutant in nanodiscs, 2.80 Å: 7T6P T709D with PI(4,5)P2, 3.40 Å: 7T6Q T709D in the presence of Calmodulin, 3.00 Å: 7T6R	7T6J	Data File Jmol Viewer 7T6J 7T6K 7T6L 7T6M 7T6O 7T6N 7T6Q 7T6P 7T6R	Fluck et al. (2022). Fluck EC, Yazici AT, Rohacs T, & Moiseenkova-Bell VY (2022). Structural basis of TRPV5 regulation by physiological and pathophysiological modulators. Cell Rep 39 4:110737. PubMed Id: 35476976. doi:10.1016/j.celrep.2022.110737.
*TRPV5 Ca²⁺-selective ion channel in nanodiscs, with bound PI(4,5)P₂: Oryctolagus cuniculus* E Eukaryota (expressed in S. cerevisiae), 3.50 Å** cryo-EM structure with bound oleoyl coenzyme A, closed state, 3.09 Å: 8FHH with bound oleoyl coenzyme A, open state, 3.25 Å: 8FHI	8FFO	Data File Jmol Viewer 8FFO 8FHH 8FHI	Lee et al. (2023). Lee BH, De Jesús Pérez JJ, Moiseenkova-Bell V, & Rohacs T (2023). Structural basis of the activation of TRPV5 channels by long-chain acyl-Coenzyme-A. Nat Commun 14 1:5883. PubMed Id: 37735536. doi:10.1038/s41467-023-41577-z.
*TRPV5 Ca²⁺-selective ion channel in nanodiscs with bound ruthenium red: Oryctolagus cuniculus* E Eukaryota (expressed in S. cerevisiae), 2.96 Å** cryo-EM structure with bound ruthenium red and PI(4,5)P2, 2.65 Å: 8FFQ	8FFN	Data File Jmol Viewer 8FFN 8FFQ	Pumroy et al. (2024). Pumroy RA, De Jesús-Pérez JJ, Protopopova AD, Rocereta JA, Fluck EC, Fricke T, Lee BH, Rohacs T, Leffler A, & Moiseenkova-Bell V (2024). Molecular details of ruthenium red pore block in TRPV channels. EMBO Rep 25 2:506-523. PubMed Id: 38225355. doi:10.1038/s44319-023-00050-0.
*TRPV6 transient receptor potential calcium channel: Rattus norvegicus* E Eukaryota (expressed in HEK 293S cells), 3.25 Å** with bound Ca²⁺, 3.65 Å: 5IWP with bound Ba²⁺, 3.85 Å: 5IWR with bound Gd³⁺, 3.8 Å: 5IWT	5IWK	Data File Jmol Viewer 5IWK 5IWP 5IWT 5IWR	Saotome et al. (2016). Saotome K, Singh AK, Yelshanskaya MV, & Sobolevsky AI (2016). Crystal structure of the epithelial calcium channel TRPV6. Nature 534 :506-511. PubMed Id: 27296226. doi:10.1038/nature17975.
*TRPV6 transient receptor potential calcium channel, no domain swapping: TRPV6_cryst: Rattus norvegicus* E Eukaryota (expressed in HEK 293 cells), 3.31 Å** TRPV6* (domain swapped), 3.25 Å: 5WO7 TRPV6-Del1 (4 deletions in S4-S5 linker), 3.4 Å: 5WO8 TRPV6 in the presence of Ca²⁺, 3.7 Å: 5WO9 TRPV6* in presence of Gd³⁺, 3.9 Å: 5WOA	5WO6	Data File Jmol Viewer 5WO6 5WO7 5WO8 5WO9 5WOA	Singh et al. (2017). Singh AK, Saotome K, & Sobolevsky AI (2017). Swapping of transmembrane domains in the epithelial calcium channel TRPV6. Sci Rep 7 1:10669. PubMed Id: 28878326. doi:10.1038/s41598-017-10993-9.
*TRPV6 transient receptor potential calcium channel with bound 2-APB: Rattus norvegicus E Eukaryota (expressed in HEK293 cells), 3.45 Å** with bound brominated 2-APB, 4.3 Å: 6D7V Y466A mutant without 2-APB, 3.37 Å: 6D7P Y466A mutant with bound 2-APB, 3.50 Å: 6D7Q Y466A mutant with bound brominated 2-APB, 3.6 Å: 6D7X	6DO7	Data File Jmol Viewer 6DO7 6D7X 6D7P 6D7V 6D7Q	Singh et al. (2018). Singh AK, Saotome K, McGoldrick LL, & Sobolevsky AI (2018). Structural bases of TRP channel TRPV6 allosteric modulation by 2-APB. Nat Commun 9 1. PubMed Id: 29941865. doi:10.1038/s41467-018-04828-y.
*TRPV6 transient receptor in complex with (4- phenylcyclohexyl)piperazine inhibitor Br-cis-22a: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.70 Å**	7D2K	Data File Jmol Viewer 7D2K	Bhardwaj et al. (2020). Bhardwaj R, Lindinger S, Neuberger A, Nadezhdin KD, Singh AK, Cunha MR, Derler I, Gyimesi G, Reymond JL, Hediger MA, Romanin C, & Sobolevsky AI (2020). Inactivation-mimicking block of the epithelial calcium channel TRPV6. Sci Adv 6 48:eabe1508. PubMed Id: 33246965. doi:10.1126/sciadv.abe1508.
*TRPV6 transient receptor potential calcium channel in nanodiscs: Homo sapiens* E Eukaryota (expressed in HEK 293S cells), 3.6 Å** cryo-EM structure in amphipols, 4 Å: 6BO9 R470E mutant in amphipols, 4.2 Å: 6BOA TRPV6* (see 5WO6 above) in nanodiscs, 3.9 Å: 6BOB	6BO8	Data File Jmol Viewer 6BO8 6BOA 6BOB 6BO9	McGoldrick et al. (2018). McGoldrick LL, Singh AK, Saotome K, Yelshanskaya MV, Twomey EC, Grassucci RA, & Sobolevsky AI (2018). Opening of the human epithelial calcium channel TRPV6. Nature 553 :233-237. PubMed Id: 29258289. doi:10.1038/nature25182.
*TRPV6 transient receptor potential calcium channel in amphipols, Y467A mutant: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.34 Å** cryo-EM structure with bound 2-APB, 4.44 Å: 6D7T	6D7S	Data File Jmol Viewer 6D7S 6D7T	Singh et al. (2018). Singh AK, Saotome K, McGoldrick LL, & Sobolevsky AI (2018). Structural bases of TRP channel TRPV6 allosteric modulation by 2-APB. Nat Commun 9 1. PubMed Id: 29941865. doi:10.1038/s41467-018-04828-y.
*TRPV6 transient receptor potential calcium channel, apo-state, in glyco-diosgenin detergent: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.69 Å** cryo-EM structure in cNW11 nanodiscs, 2.54 Å 7S89 in complex with channel blocker ruthenium red, 2.43 Å 7S8B in complex with inhibitor econazole, 2.85 Å 7S8C	7S88	Data File Jmol Viewer 7S88 7S8C 7S89 7S8B	Neuberger et al. (2021). Neuberger A, Nadezhdin KD, & Sobolevsky AI (2021). Structural mechanisms of TRPV6 inhibition by ruthenium red and econazole. Nat Commun 12 1:6284. PubMed Id: 34725357. doi:10.1038/s41467-021-26608-x.
*TRPV6 transient receptor potential calcium channel, open state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.26 Å** cryo-EM structure in complex with (4- phenylcyclohexyl)piperazine inhibitor cis-22a, 3.10 Å 7K4B in complex with (4- phenylcyclohexyl)piperazine inhibitor Br-cis-22a, 3.78 Å 7K4C in complex with (4- phenylcyclohexyl)piperazine inhibitor 3OG, 3.66 Å 7K4D in complex with (4- phenylcyclohexyl)piperazine inhibitor Br-cis-22a, 3.70 Å 7D2K	7K4A	Data File Jmol Viewer 7K4A 7K4D 7K4C 7K4B 7D2K	Bhardwaj et al. (2020). Bhardwaj R, Lindinger S, Neuberger A, Nadezhdin KD, Singh AK, Cunha MR, Derler I, Gyimesi G, Reymond JL, Hediger MA, Romanin C, & Sobolevsky AI (2020). Inactivation-mimicking block of the epithelial calcium channel TRPV6. Sci Adv 6 48:eabe1508. PubMed Id: 33246965. doi:10.1126/sciadv.abe1508.
*TRPV6 transient receptor potential calcium channel, open state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.71 Å** cryo-EM structure in complex with natural phytoestrogen genistein, 2.66 Å: 8FOA	8FOB	Data File Jmol Viewer 8FOB 8FOA	Neuberger et al. (2023). Neuberger A, Trofimov YA, Yelshanskaya MV, Nadezhdin KD, Krylov NA, Efremov RG, & Sobolevsky AI (2023). Structural mechanism of human oncochannel TRPV6 inhibition by the natural phytoestrogen genistein. Nat Commun 14 1:2659. PubMed Id: 37160865. doi:10.1038/s41467-023-38352-5.
*TRPV6 transient receptor potential calcium channel in cNW30 nanodisc with bound tetrahydrocannabivarin (THCV): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.79 Å** cryo-EM structure	8SP8	Data File Jmol Viewer 8SP8	Neuberger et al. (2023). Neuberger A, Trofimov YA, Yelshanskaya MV, Khau J, Nadezhdin KD, Khosrof LS, Krylov NA, Efremov RG, & Sobolevsky AI (2023). Molecular pathway and structural mechanism of human oncochannel TRPV6 inhibition by the phytocannabinoid tetrahydrocannabivarin. Nat Commun 14 1:4630. PubMed Id: 37532722. doi:10.1038/s41467-023-40362-2.
*PKD2 polycystic kidney disease channel in lipid nanodiscs: Homo sapiens* E Eukaryota (expressed in HEK293S cells), 3.0 Å** cryo-EM structure	5T4D	Data File Jmol Viewer 5T4D	Shen et al. (2016). Shen PS, Yang X, DeCaen PG, Liu X, Bulkley D, Clapham DE, & Cao E (2016). The Structure of the Polycystic Kidney Disease Channel PKD2 in Lipid Nanodiscs. Cell 167 :763-773.e11. PubMed Id: 27768895. doi:10.1016/j.cell.2016.09.048.
*PKD2 polycystic kidney disease channel in detergent: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 4.22 Å** cryo-EM structure	5K47	Data File Jmol Viewer 5K47	Grieben et al. (2017). Grieben M, Pike AC, Shintre CA, Venturi E, El-Ajouz S, Tessitore A, Shrestha L, Mukhopadhyay S, Mahajan P, Chalk R, Burgess-Brown NA, Sitsapesan R, Huiskonen JT, & Carpenter EP (2017). Structure of the polycystic kidney disease TRP channel Polycystin-2 (PC2). Nat Struct Mol Biol 24 :114-122. PubMed Id: 27991905. doi:10.1038/nsmb.3343.
*PKD2 polycystic kidney disease channel in complex with cations and lipids: Homo sapiens* E Eukaryota (expressed in HEK293S cells), 4.3 Å** cryo-EM structure in complex with Ca²⁺ and lipids, 4.2 Å: 5MKF	5MKE	Data File Jmol Viewer 5MKE 5MKF	Wilkes et al. (2017). Wilkes M, Madej MG, Kreuter L, Rhinow D, Heinz V, De Sanctis S, Ruppel S, Richter RM, Joos F, Grieben M, Pike AC, Huiskonen JT, Carpenter EP, Kühlbrandt W, Witzgall R, & Ziegler C (2017). Molecular insights into lipid-assisted Ca²⁺ regulation of the TRP channel Polycystin-2. Nat Struct Mol Biol 24 :123-130. PubMed Id: 28092368. doi:10.1038/nsmb.3357.
*PKD2 polycystic kidney disease channel in complex with PKD1 receptor: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.6 Å** cryo-EM structure. PKD1 comprised of residues 3049 to 4169 and PKD2 residues 185-723.	6A70	Data File Jmol Viewer 6A70	Su et al. (2018). Su Q, Hu F, Ge X, Lei J, Yu S, Wang T, Zhou Q, Mei C, & Shi Y (2018). Structure of the human PKD1-PKD2 complex. Science 361 6406. PubMed Id: 30093605. doi:10.1126/science.aat9819.
*Human Polycsytin 2-l1 TRP channel: Homo sapiens* E Eukaryota (expressed in sf9 cells), 3.11 Å** cryo-EM structure	6DU8	Data File Jmol Viewer 6DU8	Hulse et al. (2018). Hulse RE, Li Z, Huang RK, Zhang J, & Clapham DE (2018). Cryo-EM structure of the polycystin 2-l1 ion channel. Elife 7 :e36931. PubMed Id: 30004384. doi:10.7554/eLife.36931.
*PKD2 polycystic kidney disease channel in UDM supplemented with PI(4,5)P₂: Homo sapiens* E Eukaryota (expressed in sf9 cells), 2.96 Å** cryo-EM structure in UDM supplemented with PI(3,5)P₂, 3.39 Å: 6T9O	6T9N	Data File Jmol Viewer 6T9N 6T9O	Wang et al. (2020). Wang Q, Corey RA, Hedger G, Aryal P, Grieben M, Nasrallah C, Baronina A, Pike ACW, Shi J, Carpenter EP, & Sansom MSP (2020). Lipid Interactions of a Ciliary Membrane TRP Channel: Simulation and Structural Studies of Polycystin-2. Structure 28 2:169-184.e5. PubMed Id: 31806353. doi:10.1016/j.str.2019.11.005.
*PKD2 polycystic kidney disease channel, C331S disease variant: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.24 Å** cryo-EM structure	6WB8	Data File Jmol Viewer 6WB8	Vien et al. (2020). Vien TN, Wang J, Ng LCT, Cao E, & DeCaen PG (2020). Molecular dysregulation of ciliary polycystin-2 channels caused by variants in the TOP domain. Proc Natl Acad Sci USA 117 19:10329-10338. PubMed Id: 32332171. doi:10.1073/pnas.1920777117.
*PKD2L1 polycystic kidney disease channel (residues 64-629): Mus musculus* E Eukaryota (expressed in HEK 293 cells), 3.38 Å** cryo-EM structure.	5Z1W	Data File Jmol Viewer 5Z1W	Su et al. (2018). Su Q, Hu F, Liu Y, Ge X, Mei C, Yu S, Shen A, Zhou Q, Yan C, Lei J, Zhang Y, Liu X, & Wang T (2018). Cryo-EM structure of the polycystic kidney disease-like channel PKD2L1. Nat Commun 9 1. PubMed Id: 29567962. doi:10.1038/s41467-018-03606-0.
*PKD2L1/ PKD1L3-CTD polycystic kidney disease channel, apo state: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure calcium-bound state, 3.10 Å 7D7F	7D7E	Data File Jmol Viewer 7D7E 7D7F	Su et al. (2021). Su Q, Chen M, Wang Y, Li B, Jing D, Zhan X, Yu Y, & Shi Y (2021). Structural basis for Ca²⁺ activation of the heteromeric PKD1L3/PKD2L1 channel. Nat Commun 12 1:4871. PubMed Id: 34381056. doi:10.1038/s41467-021-25216-z.
*NOMPC mechanotransduction channel: Drosophila melanogaster* E Eukaryota (expressed in HEK293 cells), 3.55 Å** cryo-EM structure	5VKQ	Data File Jmol Viewer 5VKQ	Jin et al. (2017). Jin P, Bulkley D, Guo Y, Zhang W, Guo Z, Huynh W, Wu S, Meltzer S, Cheng T, Jan LY, Jan YN, & Cheng Y (2017). Electron cryo-microscopy structure of the mechanotransduction channel NOMPC. Nature 7661:118-122. PubMed Id: 28658211. doi:10.1038/nature22981.
*Endolysosomal TRPML1 channel luminal domain, pH 6: Homo sapiens* E Eukaryota (expressed in E. coli), 2.3 Å** at pH 7.5, 2.4 Å: 5TJC at pH 4.5, 2.4 Å: 5TJB	5TJA	Data File Jmol Viewer 5TJA 5TJB 5TJC	Li et al. (2017). Li M, Zhang WK, Benvin NM, Zhou X, Su D, Li H, Wang S, Michailidis IE, Tong L, Li X & Yang J (2017). Structural basis of dual Ca²⁺/pH regulation of the endolysosomal TRPML1 channel Nature Struct Mol Biol 24 :205-213. PubMed Id: 28112729. doi:10.1038/nsmb.3362.
*Endolysosomal TRPML1 channel with bound synthetic inhibitor ML-SI3: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure	7MGL	Data File Jmol Viewer 7MGL	Schmiege et al. (2021). Schmiege P, Fine M, & Li X (2021). Atomic insights into ML-SI3 mediated human TRPML1 inhibition. Structure 29 11:1295-1302.e3. PubMed Id: 34171299. doi:10.1016/j.str.2021.06.003.
*TRPY1 yeast vacuolar receptor conductance 1 (YVC1) channel: Saccharomyces cerevisiae* E Eukaryota, 3.10 Å** cryo-EM structure	6WHG	Data File Jmol Viewer 6WHG	Ahmed et al. (2022). Ahmed T, Nisler CR, Fluck EC 3rd, Walujkar S, Sotomayor M, & Moiseenkova-Bell VY (2022). Structure of the ancient TRPY1 channel from Saccharomyces cerevisiae reveals mechanisms of modulation by lipids and calcium. Structure 30 1:139-155.e5. PubMed Id: 34453887. doi:10.1016/j.str.2021.08.003.
Channels: Gap Junctions and Related Channels
*Connexin 26 (Cx26; GJB2) gap junction: Homo sapiens* E Eukaryota (expressed in Sf9 cells), 3.5 Å**	2ZW3	Data File Jmol Viewer 2ZW3	Maeda et al. (2009). Maeda S, Nakagawa S, Suga M, Yamashita E, Oshima A, Fujiyoshi Y, & Tsukihara T (2009). Structure of the connexin 26 gap junction channel at 3.5 Å resolution. Nature 458 :597-602. PubMed Id: 19340074.
*Connexin 26, dodecamer at pH7.4, 20mmHg PCO₂: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.10 Å** cryo-EM structure 55mm Hg PCO₂, 2.20 Å: 7QER 90mmHg PCO₂, 1.90 Å: 7QEQ class 1 hexamer at 90mmHg PCO₂, 2.00 Å: 7QEY class 2 hexamer at 90mmHg PCO₂, 2.10 Å: 7QEW	7QET	Data File Jmol Viewer 7QET 7QER 7QEW 7QEY 7QEQ	Brotherton et al. (2022). Brotherton DH, Savva CG, Ragan TJ, Dale N, & Cameron AD (2022). Conformational changes and CO₂-induced channel gating in connexin26. Structure 30 5:697-706.e4. PubMed Id: 35276081. doi:10.1016/j.str.2022.02.010.
*Connexin 36 (Cx36; GJD2) gap junction channel in detergents: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.20 Å** cryo-EM structure C6 symmetry, 3.60 Å: 8HKP with pore-lining N-terminal helices, in soybean lipids, 3.10 Å: 7XNH in soybean lipids, C6 symmetry, 3.40 Å: 7XNV BRIL-fused mutant, 2.20 Å: 7XKT N-terminal deletion mutant, in soybean lipids, D6 symmetry, 3.00 Å: 7XL8 N-terminal deletion BRIL-fused mutant, in soybean lipids, D6 symmetry, 3.40 Å: 7XKI	7XKK	Data File Jmol Viewer 7XKK 8HKP 7XNV 7XKI 7XKT 7XNH 7XL8	Lee et al. (2023). Lee SN, Cho HJ, Jeong H, Ryu B, Lee HJ, Kim M, Yoo J, Woo JS, & Lee HH (2023). Cryo-EM structures of human Cx36/GJD2 neuronal gap junction channel. Nat Commun 14 1:1347. PubMed Id: 36906653. doi:10.1038/s41467-023-37040-8.
*Connexin 36 (Cx36; GJD2) gap junction channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.69 Å** cryo-EM structure	8IYG	Data File Jmol Viewer 8IYG	Mao & Chen (2024). Mao W, & Chen S (2024). Assembly mechanisms of the neuronal gap junction channel connexin 36 elucidated by Cryo-EM. Arch Biochem Biophys 754 :109959. PubMed Id: 38490311. doi:10.1016/j.abb.2024.109959.
*Cx31.3/GJC3 connexin hemichannel, in the absence of calcium: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.34 Å** cryo-EM structure in the presence of calcium, 2.53 Å: 6L3U R15G mutant, 2.63 Å: 6L3V	6L3T	Data File Jmol Viewer 6L3T 6L3U 6L3V	Lee et al. (2020). Lee HJ, Jeong H, Hyun J, Ryu B, Park K, Lim HH, Yoo J, & Woo JS (2020). Cryo-EM structure of human Cx31.3/GJC3 connexin hemichannel. Sci Adv 6 35. PubMed Id: 32923625. doi:10.1126/sciadv.aba4996.
*Innexin-6 gap junction channel: Caenorhabditis elegans* E Eukaryota (expressed in Spodoptera frugiperda), 3.6 Å** cryo-EM structure hemichannel, 3.3 Å: 5H1Q	5H1R	Data File Jmol Viewer 5H1R 5H1Q	Oshima et al. (2016). Oshima A, Tani K, & Fujiyoshi Y (2016). Atomic structure of the innexin-6 gap junction channel determined by cryo-EM. Nat Commun 7 :13681. PubMed Id: 27905396. doi:10.1038/ncomms13681.
*Innexin-6 (INX-6) gap junction hemichannel in a nanodisc: Caenorhabditis elegans* E Eukaryota (expressed in S. frugiperda), 3.80 Å** cryo-EM hemichannel in detergent, 3.80 Å: 6KFG N-terminal deletion mutant of INX-6 in a nanodisc, 3.60 Å: 6KFH	6KFF	Data File Jmol Viewer 6KFF 6KFG 6KFH	Burendei et al. (2020). Burendei B, Shinozaki R, Watanabe M, Terada T, Tani K, Fujiyoshi Y, & Oshima A (2020). Cryo-EM structures of undocked innexin-6 hemichannels in phospholipids. Sci Adv 6 7. PubMed Id: 32095518. doi:10.1126/sciadv.aax3157.
*connexin (Cx)-46/50 intercellular gap junction channels. Cx46 channel: Ovis aries* E Eukaryota, 3.4 Å** cryo-EM structure Cx50 channel, 3.4 Å: 6MHY	6MHQ	Data File Jmol Viewer 6MHQ 6MHY	Myers et al. (2018). Myers JB, Haddad BG, O'Neill SE, Chorev DS, Yoshioka CC, Robinson CV, Zuckerman DM, & Reichow SL (2018). Structure of native lens connexin 46/50 intercellular channels by cryo-EM. Nature 564 7736:372-377. PubMed Id: 30542154. doi:10.1038/s41586-018-0786-7.
*connexin (Cx)-46/50 intercellular gap junction channels in nanodiscs. Cx-50: Ovis aries* E Eukaryota, 1.94 Å** cryo-EM structure Cx-46, 1.90 Å: 7JKC Cx-50, lipid class 1, 2.50 Å: 7JLW Cx-46, lipid class 1, 2.50 Å: 7JMD Cx-50, lipid class 2, 2.50 Å: 7JM9 Cx-46, lipid class 2, 2.50 Å: 7JN0 Cx-50, lipid class 3, 2.50 Å: 7JMC Cx-46, lipid class 3, 2.50Å: 7JN1	7JJP	Data File Jmol Viewer 7JJP 7JN0 7JMC 7JN1 7JMD 7JKC 7JM9 7JLW	Flores et al. (2020). Flores JA, Haddad BG, Dolan KA, Myers JB, Yoshioka CC, Copperman J, Zuckerman DM, & Reichow SL (2020). Connexin-46/50 in a dynamic lipid environment resolved by CryoEM at 1.9?Å. Nat Commun 11 1. PubMed Id: 32859914. doi:10.1038/s41467-020-18120-5.
*Calcium homeostasis modulator (CALHM1) voltage-gated ATP release channel: Gallus gallus* E Eukaryota (expressed in S. frugiperda), 3.63 Å** cryo-EM structure undecameric chicken CALHM1 and human CALHM2 chimera, 3.87 Å: 6VAL	6VAM	Data File Jmol Viewer 6VAM 6VAL	Syrjanen et al. (2020). Syrjanen JL, Michalski K, Chou TH, Grant T, Rao S, Simorowski N, Tucker SJ, Grigorieff N, & Furukawa H (2020). Structure and assembly of calcium homeostasis modulator proteins. Nat Struct Mol Biol 27 2:150-159. PubMed Id: 31988524. doi:10.1038/s41594-019-0369-9.
*Calcium homeostasis modulator (CLHM-1) voltage-gated ATP release channel:: Caenorhabditis elegans* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure	6LMV	Data File Jmol Viewer 6LMV	Demura et al. (2020). Demura K, Kusakizako T, Shihoya W, Hiraizumi M, Nomura K, Shimada H, Yamashita K, Nishizawa T, Taruno A, & Nureki O (2020). Cryo-EM structures of calcium homeostasis modulator channels in diverse oligomeric assemblies. Sci Adv 6 29. PubMed Id: 32832629. doi:10.1126/sciadv.aba8105.
*Calcium homeostasis modulator (CLHM-1) voltage-gated ATP release channel: Caenorhabditis elegans* E Eukaryota (expressed in HEK293 cells), 3.73 Å** cryo-EM structure	6LOM	Data File Jmol Viewer 6LOM	Yang et al. (2020). Yang W, Wang Y, Guo J, He L, Zhou Y, Zheng H, Liu Z, Zhu P, & Zhang XC (2020). Cryo-electron microscopy structure of CLHM1 ion channel from Caenorhabditis elegans. Protein Sci 29 8:1803-1815. PubMed Id: 32557855. doi:10.1002/pro.3904.
*Calcium homeostasis modulator (CALHM1) voltage-gated ATP release channel: Oryzias latipes* E Eukaryota (expressed in HEK293 cells), 2.66 Å** cryo-EM structure chimeric construct with human CALHM1, 8-mer. 3.40Å: 6LMW chimeric construct with human CALHM1, 9-mer. 3.40 Å: 6LMX	6LMT	Data File Jmol Viewer 6LMT 6LMW 6LMX	Demura et al. (2020). Demura K, Kusakizako T, Shihoya W, Hiraizumi M, Nomura K, Shimada H, Yamashita K, Nishizawa T, Taruno A, & Nureki O (2020). Cryo-EM structures of calcium homeostasis modulator channels in diverse oligomeric assemblies. Sci Adv 6 29. PubMed Id: 32832629. doi:10.1126/sciadv.aba8105.
*Calcium homeostasis modulator (CALHM1) voltage-gated ATP release channel: Danio rerio* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure	6LYG	Data File Jmol Viewer 6LYG	Ren et al. (2020). Ren Y, Wen T, Xi Z, Li S, Lu J, Zhang X, Yang X, & Shen Y (2020). Cryo-EM structure of the calcium homeostasis modulator 1 channel. Sci Adv 6 29. PubMed Id: 32832630. doi:10.1126/sciadv.aba8161.
*Calcium homeostasis modulator (CALHM2) voltage-gated ATP release channel, open state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.3 Å** cryo-EM structure CALHM2 gap junction, 3.5 Å: 6UIX ruthenium red-bound inhibited state, 2.7 Å: 6UIW	6UIV	Data File Jmol Viewer 6UIV 6UIW 6UIX	Choi et al. (2019). Choi W, Clemente N, Sun W, Du J, & Lü W (2019). The structures and gating mechanism of human calcium homeostasis modulator 2. Nature 576 7785:163-167. PubMed Id: 31776515. doi:10.1038/s41586-019-1781-3.
*Calcium homeostasis modulator (CALHM2) voltage-gated ATP release channel: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.48 Å** cryo-EM structure dimer of undecameric CALHM2, 3.68 Å: 6VAI	6VAK	Data File Jmol Viewer 6VAK 6VAI	Syrjanen et al. (2020). Syrjanen JL, Michalski K, Chou TH, Grant T, Rao S, Simorowski N, Tucker SJ, Grigorieff N, & Furukawa H (2020). Structure and assembly of calcium homeostasis modulator proteins. Nat Struct Mol Biol 27 2:150-159. PubMed Id: 31988524. doi:10.1038/s41594-019-0369-9.
*Calcium homeostasis modulator (CALHM4), decameric in absence of Ca²⁺: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.07 Å** cryo-EM structure dimer of undecameric CALHM4 in the absence of Ca²⁺, 3.82 Å: 6YTL dimer of decameric CALHM4 in the presence of Ca²⁺, 4.24 Å: 6YTO dimer of undecameric CALHM4 in the presence of Ca²⁺, 4.02 Å: 6YTQ	6YTK	Data File Jmol Viewer 6YTK 6YTL 6YTO 6YTQ	Drożdżyk et al. (2020). Drożdżyk K, Sawicka M, Bahamonde-Santos MI, Jonas Z, Deneka D, Albrecht C, & Dutzler R (2020). Cryo-EM structures and functional properties of CALHM channels of the human placenta. Elife 9 . PubMed Id: 32374262. doi:10.7554/eLife.55853.
*Calcium homeostasis modulator (CALHM5) in the presence of EDTA: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.80 Å** cryo-EM structure in the presence of rubidium red, 2.61 Å: 7D60 in the presence of Ca²⁺, 2.94 Å: 7D65	7D61	Data File Jmol Viewer 7D61 7D60 7D65	Liu et al. (2020). Liu J, Wan F, Jin Q, Li X, Bhat EA, Guo J, Lei M, Guan F, Wu J, & Ye S (2020). Cryo-EM structures of human calcium homeostasis modulator 5. Cell Discov 6 1:81. PubMed Id: 33298887. doi:10.1038/s41421-020-00228-z.
*Calcium homeostasis modulator (CALHM6), decameric in presence of Ca²⁺: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.39 Å** cryo-EM structure undecameric form in presence of Ca²⁺, 6.23 Å: 6YTX	6YTV	Data File Jmol Viewer 6YTV 6YTX	Drożdżyk et al. (2020). Drożdżyk K, Sawicka M, Bahamonde-Santos MI, Jonas Z, Deneka D, Albrecht C, & Dutzler R (2020). Cryo-EM structures and functional properties of CALHM channels of the human placenta. Elife 9 . PubMed Id: 32374262. doi:10.7554/eLife.55853.
Channels: Other Ion Channels
*GluA2 Glutamate receptor (AMPA-subtype): Rattus norvegicus* E Eukaryota (expressed in sf9 cells), 3.60 Å** 3KG2 is in complex with the competitive antagonist ZK 200775 GluA2 ligand-binding core complex with bound glutamate, 1.55 Å: 3KGC	3KG2	Data File Jmol Viewer 3KG2 3KGC	Sobolevsky et al. (2009). Sobolevsky AI, Rosconi MP, & Gouaux E (2009). X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 462 :745-756. PubMed Id: 19946266.
*GluA2 Glutamate receptor (AMPA-subtype) with competitive antagonist ZK 200775: Rattus norvegicus* E Eukaryota (expressed in S. frugiperda), 4.49 Å** In complex with partial agonist (S)-5-nitrowillardiine (NOW), 4.79 Å: 4U4F	4U4G	Data File Jmol Viewer 4U4G 4U4F	Yelshanskaya et al. (2014). Yelshanskaya MV, Li M, & Sobolevsky AI (2014). Structure of an agonist-bound ionotropic glutamate receptor. Science 345 :1070-1074. PubMed Id: 25103407.
*GluA2 Glutamate receptor (AMPA-subtype) in complex with ZK200775: Rattus norvegicus* E Eukaryota (expressed in S. frugiperda), 10.4 Å** in complex with LY451646 and Glu, 12.8 Å: 4UQ6 in complex with quisqualate and LY451646, 16.4 Å: 4UQK	4UQJ	Data File Jmol Viewer 4UQJ 4UQK 4UQ6	Meyerson et al. (2014). Meyerson JR, Kumar J, Chittori S, Rao P, Pierson J, Bartesaghi A, Mayer ML, & Subramaniam S (2014). Structural mechanism of glutamate receptor activation and desensitization. Nature 514 :328-334. PubMed Id: 25119039. doi:10.1038/nature13603.
*GluA2 Glutamate receptor (AMPA-subtype), apo formA: Rattus norvegicus* E Eukaryota (expressed in HEK293S cells), 3.24 Å** GluA2-kainate-(R,R)-2b complex crystal form A, 3.25 Å: 4U1W GluA2-kainate-(R,R)-2b complex crystal form B, 3.30 Å: 4U1X GluA2-FW-(R,R)-2b complex, 3.90 Å: 4U1Y GluA2 in complex with partial agonist kainate, 3.52 Å: 4U2Q	4U2P	Data File Jmol Viewer 4U2P 4U1Y 4U1X 4U2Q 4U1W	Dürr et al. (2014). Dürr KL, Chen L, Stein RA, De Zorzi R, Folea IM, Walz T, Mchaourab HS, & Gouaux E (2014). Structure and Dynamics of AMPA Receptor GluA2 in Resting, Pre-Open, and Desensitized States. Cell 158 :778-792. PubMed Id: 25109876. doi:10.1016/j.cell.2014.07.023.
GluA2 Glutamate receptor (AMPA-subtype) A622T in complex with cone snail toxin, partial agonist KA, and postitive modulator (R,R)-2b: Rattus norvegicus E Eukaryota (expressed in HEK293 cells), 3.50 Å T625G with cone snail toxin, partial agonist KA, and positive modulator (R,R)-2b, 3.51 Å: 4U5E With snail toxin, partial agonist KA and positive modulator (R,R)-2b, 3.58 Å: 4U5D With snail toxin, partial agonist FW and positive modulator (R,R)-2b complex, 3.69 Å: 4U5C With snail toxin, partial agonist KA and postitive modulator (R,R)-2b complex ( crystal form 2), 3.70 Å: 4U5F	4U5B	Data File Jmol Viewer 4U5B 4U5F 4U5D 4U5C 4U5E	Chen et al. (2014). Chen L, Dür KL, & Gouaux E (2014). X-ray structures of AMPA receptor-cone snail toxin complexes illuminate activation mechanism. Science 345 :1021-1026. PubMed Id: 25103405. doi:10.1126/science.1258409.
*Glutamate receptor (AMPA-subtype), GluA2/GluA4 heterodimer: Rattus norvegicus* B Bacteria (expressed in HEK293S), 2.5 Å** GluA2/A3 heterodimer, 2.12 Å: 5FWY cryo-EM map for GluA2/A3 model I, 8.25 Å: 5IDE cryo-EM map for GluA2/A3 model II, 10.31 Å: 5IDF	5FWX	Data File Jmol Viewer 5FWX 5IDE 5IDF 5FWY	Herguedas et al. (2016). Herguedas B, García-Nafría J, Cais O, Fernández-Leiro R, Krieger J, Ho H, & Greger IH (2016). Structure and organization of heteromeric AMPA-type glutamate receptors. Science 352 . PubMed Id: 26966189. doi:10.1126/science.aad3873.
*GluA2 Glutamate receptor (AMPA-subtype) without bound stargazin (0-xSTZ) regulatory protein: Rattus norvegicus (GluA2) & Mus musculus (STZ)* E Eukaryota (expressed in HEK293 cells), 8.7 Å** cryo-EM structures with 1 bound STZ (1xSTZ), 6.4 Å: 5KBT with 2 bound STZ (2xSTZ), 7.8 Å: 5KBU GluA2 with bound ZK200775, 6.8 Å: 5KBV	5KBS	Data File Jmol Viewer 5KBS 5KBV 5KBU 5KBT	Twomey et al. (2016). Twomey EC, Yelshanskaya MV, Grassucci RA, Frank J, & Sobolevsky AI (2016). Elucidation of AMPA receptor-stargazin complexes by cryo-electron microscopy. Science 353 :83-86. PubMed Id: 27365450. doi:10.1126/science.aaf8411.
*GluA2 Glutamate receptor (AMPA-subtype) saturated with TARPγ2 subunits: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 7.3 Å** cryo-EM structure TARPγ2 is stargazin	5KK2	Data File Jmol Viewer 5KK2	Zhao et al. (2016). Zhao Y, Chen S, Yoshioka C, Baconguis I, & Gouaux E (2016). Architecture of fully occupied GluA2 AMPA receptor-TARP complex elucidated by cryo-EM. Nature 536 :108-111. PubMed Id: 27368053. doi:10.1038/nature18961.
*GluA2 Glutamate receptor (AMPA-subtype) bound to antagonist ZK and GSG1L in digitonin, state 1: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 4.6 Å** cryo-EM structure bound to antagonist ZK and GSG1L in digitonin, state 2; 4.4 Å: 5WEL bound to GSG1L in digitonin, state; 6.1 Å: 5WEM bound to GSG1L in digitonin, state 2; 6.8 Å: 5WEN bound to glutamate, cyclothiazide, and STZ in digitonin, 4.2 Å: 5WEO	5WEK	Data File Jmol Viewer 5WEK 5WEL 5WEN 5WEM 5WEO	Twomey et al. (2017). Twomey EC, Yelshanskaya MV, Grassucci RA, Frank J, & Sobolevsky AI (2017). Channel opening and gating mechanism in AMPA-subtype glutamate receptors. Nature 549 :60-65. PubMed Id: 28737760. doi:10.1038/nature23479.
*Glutamate receptor (AMPA-subtype), GluA1/GluA2/GluA1/GluA2 tetramer: Rattus norvegicus* E Eukaryota (expressed in S. frugiperda), 6.7 Å** cryo-EM structure GluA3/GluA2/GluA3/GluA2 tetramer, 6.5 Å: 6NJM GluA1/GluA2/GluA3/GluA2 tetramer, 6.5 Å: 6NJN	6NJL	Data File Jmol Viewer 6NJL 6NJM 6NJN	Zhao et al. (2019). Zhao Y, Chen S, Swensen AC, Qian WJ, & Gouaux E (2019). Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM. Science 364 6438:355-362. PubMed Id: 30975770. doi:10.1126/science.aaw8250.
*Glutamate receptor (AMPA-subtype), GluA1/GluA2/GluA1/GluA2 tetramer in complex with TARP γ8: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 6.3 Å** cryo-EM structure Full length GluA1/2-γ8 complex, 4.4 Å: 6QKC	6QKZ	Data File Jmol Viewer 6QKZ 6QKC	Herguedas et al. (2019). Herguedas B, Watson JF, Ho H, Cais O, García-Nafría J, & Greger IH (2019). Architecture of the heteromeric GluA1/2 AMPA receptor in complex with the auxiliary subunit TARP γ8. Science 364 6438. PubMed Id: 30872532. doi:10.1126/science.aav9011.
*GluA2 Glutamate receptor (AMPA-subtype) in complex with cornichon homolog and antagonist ZK200775: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 2.97 Å** cryo-EM structure in pseudo-symmetric global conformation, 3.07 Å: 6U5S in asymmetric global conformation, 3.12 Å: 6U6I with antagonist ZK200775, LBD, TMD, CNIH3, and lipids; 3.28 Å: 6UCB in AS map II - (LBD-TMD-C3(AS) II)- with antagonist ZK200775, without NTD; 3.3 Å: 6UD4 with antagonist ZK200775, 3.2 Å: 6UD8	6PEQ	Data File Jmol Viewer 6PEQ 6UCB 6U6I 6U5S 6UD4 6UD8	Nakagawa (2019). Nakagawa T (2019). Structures of the AMPA receptor in complex with its auxiliary subunit cornichon. Science 366 6470:1259-1263. PubMed Id: 31806817. doi:10.1126/science.aay2783.
*GluA2 Glutamate receptor (AMPA-subtype) in complex with trans-4-butylcyclohexane carboxylic acid (4-BCCA) inhibitor: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 4.25 Å**	6XSR	Data File Jmol Viewer 6XSR	Yelshanskaya et al. (2022). Yelshanskaya MV, Singh AK, Narangoda C, Williams RSB, Kurnikova MG, & Sobolevsky AI (2022). Structural basis of AMPA receptor inhibition by trans-4-butylcyclohexane carboxylic acid. Br J Pharmacol 179 14:3628-3644. PubMed Id: 32959886. doi:10.1111/bph.15254.
*GluA2 Glutamate receptor (AMPA-subtype) in complex the antagonist ZK200775 and the negative allosteric modulator GYKI53655: Rattus norvegicus* E Eukaryota (expressed in Sf9 cells), 4.65 Å**	6RUQ	Data File Jmol Viewer 6RUQ	Krintel et al. (2021). Krintel C, Dorosz J, Larsen AH, Thorsen TS, Venskutonyté R, Mirza O, Gajhede M, Boesen T, & Kastrup JS (2021). Binding of a negative allosteric modulator and competitive antagonist can occur simultaneously at the ionotropic glutamate receptor GluA2. FEBS J 288 3:995-1007. PubMed Id: 32543078. doi:10.1111/febs.15455.
*GluA1/A2 Glutamate receptor (AMPA-subtype) in complex with TARP-γ8 and CNIH2 (LBD-TMD), resting state: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure NTD of resting state GluA1/A2 heterotetramer, 3.40 Å: 7OCC Resting state GluA1/A2 heterotetramer in complex with auxiliary subunit TARP γ8 (LBD-TMD), 3.50 Å: 7OCD Active state GluA1/A2 heterotetramer in complex with auxiliary subunit TARP γ8 (LBD-TMD), 3.60 Å: 7OCF	7OCE	Data File Jmol Viewer 7OCE 7OCF 7OCD 7OCC	Zhang et al. (2021). Zhang D, Watson JF, Matthews PM, Cais O, & Greger IH (2021). Gating and modulation of a hetero-octameric AMPA glutamate receptor. Nature 594 7863:454-458. PubMed Id: 34079129. doi:10.1038/s41586-021-03613-0.
*AMPA receptor GluA2 with auxiliary subunit TARP gamma-5, bound to competitive antagonist ZK 200775: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure LBD-TMD part bound to competitive antagonist ZK 200775, 3.30 Å 7RZ5 with auxiliary subunit TARP gamma-5 bound to agonist glutamate, 4.40 Å 7RZ6 with auxiliary subunit TARP gamma-5 bound to agonist Quisqualate, 4.20 Å 7RZ7 LBD-TMD part subunit TARP gamma-5 bound to agonist quisqualate, 4.10 Å 7RZ8 receptor GluA2 with auxiliary subunit GSG1L in the apo state, 4.15 Å 7RZ9 GluA2 with auxiliary subunit GSG1L bound to agonist quisqualate, 4.26 Å 7RZA LBD-TMD part of AMPA receptor GluA2 with auxiliary subunit GSG1L bound to agonist quisqualate, 4.15 Å 7RYZ	7RZ4	Data File Jmol Viewer 7RZ4 7RZ7 7RYZ 7RZ5 7RZ9 7RZ6 7RZ8 7RZA	Klykov et al. (2021). Klykov O, Gangwar SP, Yelshanskaya MV, Yen L, & Sobolevsky AI (2021). Structure and desensitization of AMPA receptor complexes with type II TARP γ5 and GSG1L. Mol Cell 81 23:4771-4783.e7. PubMed Id: 34678168. doi:10.1016/j.molcel.2021.09.030.
*GluA1/A2 Glutamate receptor (AMPA-subtype) in complex with TARP-γ8, with L-glutamate and CTZ: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure in complex with TARP-γ 8 (TMD-LBD), 3.60 Å 7QHH	7QHB	Data File Jmol Viewer 7QHB 7QHH	Herguedas et al. (2022). Herguedas B, Kohegyi BK, Dohrke JN, Watson JF, Zhang D, Ho H, Shaikh SA, Lape R, Krieger JM, & Greger IH (2022). Mechanisms underlying TARP modulation of the GluA1/2-γ8 AMPA receptor. Nat Commun 13 1:734. PubMed Id: 35136046. doi:10.1038/s41467-022-28404-7.
GluA2 Glutamate receptor (NNNN of AMPA-subtype)/γ2 (stargazin) complex in the presence of glutamate (20μM) & cyclothiazide (100μM): Rattus norvegicus E Eukaryota (expressed in HEK293 cells), 4.02 Å cryo-EM structure GNNN of AMPA-subtype, 4.50 Å 7TNK GNGN1 of AMPA-subtype, 3.59 Å 7TNL GNGN2 of AMPA-subtype, 4.74 Å 7TNM GGNN of AMPA-subtype, 3.91 Å 7TNN GGGN of AMPA-subtype, 4.02 Å 7TNO GGGG of AMPA-subtype, 3.96 Å 7TNP	7TNJ	Data File Jmol Viewer 7TNJ 7TNN 7TNO 7TNM 7TNL 7TNP 7TNK	Yelshanskaya et al. (2022). Yelshanskaya MV, Patel DS, Kottke CM, Kurnikova MG, & Sobolevsky AI (2022). Opening of glutamate receptor channel to subconductance levels. Nature 605 7908:172-178. PubMed Id: 35444281. doi:10.1038/s41586-022-04637-w.
GluA2 Glutamate receptor (AMPA-subtype) L504Y, N775S mutant (LBD) in complex with L-glutamate and positive allosteric modulator BPAM395: Rattus norvegicus E Eukaryota (expressed in E. coli), 1.55 Å x-ray structure	8QEZ	Data File Jmol Viewer 8QEZ	Francotte et al. (2023). Francotte P, Bay Y, Goffin E, Colson T, Lesenfants C, Dorosz J, Laulumaa S, Fraikin P, de Tullio P, Beaufour C, Botez I, Pickering DS, Frydenvang K, Danober L, Kristensen AS, Kastrup JS, & Pirotte B (2023). Exploring thienothiadiazine dioxides as isosteric analogues of benzo- and pyridothiadiazine dioxides in the search of new AMPA and kainate receptor positive allosteric modulators. Eur J Med Chem 264 :116036. PubMed Id: 38101041. doi:10.1016/j.ejmech.2023.116036.
*GluA2 Glutamate receptor (AMPA-subtype), F231A mutant, in complex with TARP-γ2, resting state: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure transmembrane domain, 3.00 Å: 8C1S flip isoform (R/G-edited; Q/R-edited), desensitized conformation 1, 3.36 Å: 8P3X flip isoform (R/G-edited; Q/R-edited), desensitized conformation 2, 3.46 Å: 8P3Z flip isoform (R/G-edited; Q/R-edited), desensitized conformation 3, 3.55 Å: 8P3Y flip isoform (R/G-unedited; Q/R-edited), desensitized conformation 1, 3.46 Å: 8PIV flip isoform (R/G-unedited; Q/R-edited), desensitized conformation 2, 2.95 Å: 8P3S flip isoform (R/G-unedited; Q/R-edited), desensitized conformation 3, 2.95 Å: 8P3Q	8C1R	Data File Jmol Viewer 8C1R 8P3X 8P3Y 8P3Q 8P3S 8C1S 8PIV 8P3Z	Zhang et al. (2023). Zhang D, Ivica J, Krieger JM, Ho H, Yamashita K, Stockwell I, Baradaran R, Cais O, & Greger IH (2023). Structural mobility tunes signalling of the GluA1 AMPA glutamate receptor. Nature 621 7980:877-882. PubMed Id: 37704721. doi:10.1038/s41586-023-06528-0.
*Glutamate receptor (AMPA-subtype), composite LBD-TMD structure combined from all hippocampal AMPAR subtypes: Mus musculus* E Eukaryota (expressed in S. frugiperda), 3.25 Å** cryo-EM structure native AMPA receptor, 3.40 Å: 7LDD native AMPA receptor, 3.90 Å: 7LDE	7LEP	Data File Jmol Viewer 7LEP 7LDD 7LDE	Yu et al. (2021). Yu J, Rao P, Clark S, Mitra J, Ha T, & Gouaux E (2021). Hippocampal AMPA receptor assemblies and mechanism of allosteric inhibition. Nature 594 7863:448-453. PubMed Id: 33981040. doi:10.1038/s41586-021-03540-0.
*GluD1 ionotropic glutamate receptor in complex with 7-CKA and Calcium, compact state: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 8.1 Å** cryo-EM structure in complex with 7-CKA and Calcium, splayed state, 8.1 Å: 6KSP	6KSS	Data File Jmol Viewer 6KSS 6KSP	Burada et al. (2020). Burada AP, Vinnakota R, & Kumar J (2020). Cryo-EM structures of the ionotropic glutamate receptor GluD1 reveal a non-swapped architecture. Nat Struct Mol Biol 27 1:84-91. PubMed Id: 31925409. doi:10.1038/s41594-019-0359-y.
*GluD2 ionotropic glutamate receptor in complex with 7-CKA and Calcium: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 8.80 Å** cryo-EM structure	6LU9	Data File Jmol Viewer 6LU9	Burada et al. (2020). Burada AP, Vinnakota R, & Kumar J (2020). The architecture of GluD2 ionotropic delta glutamate receptor elucidated by cryo-EM. J Struct Biol 211 2:107546. PubMed Id: 32512155. doi:10.1016/j.jsb.2020.107546.
*GluN1a/GluN2B NMDA receptor: Rattus norvegicus* E Eukaryota (expressed in S. frugiperda), 3.96 Å** NMDA = N-methyl-D-aspartate	4PE5	Data File Jmol Viewer 4PE5	Karakas et al. (2014). Karakas E, & Furukawa H (2014). Crystal structure of a heterotetrameric NMDA receptor ion channel. Science 344 :992-997. PubMed Id: 24876489. doi:10.1126/science.1251915.
*GluN1a/GluN2B NMDA receptor, apo-form crystal structure: Rattus norvegicus* E Eukaryota (expressed in Trichoplusia ni), 2.9 Å** cryo-EM structures (S. frugiperda expression system): receptor in active conformation, 6.8 Å: 5FXG receptor in non-active-1 conformation, 5.0 Å: 5FXH receptor in non-active-2 conformation, 6.4 Å: 5FXI receptor structure-Class X, 6.25 Å: 5FXJ receptor structure-Class Y, 6.4 Å: 5YXK	5B3J	Data File Jmol Viewer 5B3J 5FXJ 5FXG 5FXH 5YXK 5FXI	Tajima et al. (2016). Tajima N, Karakas E, Grant T, Simorowski N, Diaz-Avalos R, Grigorieff N, & Furukawa H (2016). Activation of NMDA receptors and the mechanism of inhibition by ifenprodil. Nature 534 :63-68. PubMed Id: 27135925. doi:10.1038/nature17679.
*GluN1a/GluN2B NMDA receptor, glycine/glutamate-bound conformation: Rattus norvegicus* E Eukaryota (expressed in Spodoptera frugiperda), 2.97 Å** cryo-EM structure phencyclidine-bound conformation, 4.30 Å 7SAB S-(+)-ketamine-bound conformation, 3.69 Å 7SAC memantine-bound conformation, 3.96 Å 7SAD	7SAA	Data File Jmol Viewer 7SAA 7SAC 7SAD 7SAB	Chou et al. (2022). Chou TH, Epstein M, Michalski K, Fine E, Biggin PC, & Furukawa H (2022). Structural insights into binding of therapeutic channel blockers in NMDA receptors. Nat Struct Mol Biol 29 6:507-518. PubMed Id: 35637422. doi:10.1038/s41594-022-00772-0.
*GluN1a/GluN2B NMDA receptor: Xenopus laevis* E Eukaryota (expressed in HEK293S GnTI^-), 3.59 Å** The protein is the K216C mutant. Structure at 3.77 Å: 4TLM	4TLL	Data File Jmol Viewer 4TLL 4TLM	Lee et al. (2014). Lee CH, Lü W, Michel JC, Goehring A, Du J, Song X, & Gouaux E (2014). NMDA receptor structures reveal subunit arrangement and pore architecture. Nature 511 :191-197. PubMed Id: 25008524. doi:10.1038/nature13548.
*GluN1a/GluN2B NMDA receptor: Xenopus laevis* E Eukaryota (expressed in HEK293S), 7.0 Å** Cryo-EM structures. 5IOU is glutamate/glycine-bound. glutamate/glycine/Ro25-6981-bound conformation, 7.5 Å: 5IOV DCKA/D-APV-bound conformation, state 2, 13.5 Å: 5IPQ DCKA/D-APV-bound conformation, state 3, 14.1 Å: 5IPR DCKA/D-APV-bound conformation, state 4, 13.5 Å: 5IPS DCKA/D-APV-bound conformation, state 5, 14.1 Å: 5IPT DCKA/D-APV-bound conformation, state 6, 15.4 Å: 5IPU DCKA/D-APV-bound conformation, state 1, 9.25 Å: 5IPV	5IOU	Data File Jmol Viewer 5IOU 5IPR 5IPQ 5IPT 5IPS 5IPV 5IPU 5IOV	Zhu et al. (2016). Zhu S, Stein RA, Yoshioka C, Lee CH, Goehring A, Mchaourab HS, & Gouaux E (2016). Mechanism of NMDA Receptor Inhibition and Activation. Cell 165 :704-714. PubMed Id: 27062927. doi:10.1016/j.cell.2016.03.028.
*GluN1/GluN2A/GluN1/GluN2B heterotrimeric NMDA receptor in complex with Gly, Glu, & MK-801: Xenopus laevis* E Eukaryota (expressed in HEK293S cells), 4.5 Å** cryo-EM structure additionally in complex with Ro 25-6981, 4.5 Å: 5UP2	5UOW	Data File Jmol Viewer 5UOW 5UP2	Lü et al. (2017). Lü W, Du J, Goehring A, & Gouaux E (2017). Cryo-EM structures of the triheteromeric NMDA receptor and its allosteric modulation. Science 355 6331. PubMed Id: 28232581. doi:10.1126/science.aal3729.
*GluN1a/GluN2B NMDA receptor lacking N-terminal domain (ΔATD): Xenopus laevis* E Eukaryota (expressed in S. frugiperda), 3.6 Å**	5UN1	Data File Jmol Viewer 5UN1	Song et al. (2018). Song X, Jensen MØ, Jogini V, Stein RA, Lee CH, Mchaourab HS, Shaw DE, & Gouaux E (2018). Mechanism of NMDA receptor channel block by MK-801 and memantine. Nature 556 7702:515-519. PubMed Id: 29670280. doi:10.1038/s41586-018-0039-9.
*GluN1a/GluN2C NMDA receptor with bound D-cycloserine and glutamate, intact conformation: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.96 Å** cryo-EM structure splayed conformation, 3.71 Å: 8E93 with bound PYD-106, intact conformation, 3.72 Å: 8E94 with bound PYD-106, splayed conformation, 4.19 Å: 8E97 in nanodisc with bound D-cycloserine and glutamate, intact conformation, 3.75 Å: 8E98	8E92	Data File Jmol Viewer 8E92 8E94 8E98 8E93 8E97	Chou et al. (2022). Chou TH, Kang H, Simorowski N, Traynelis SF, & Furukawa H (2022). Structural insights into assembly and function of GluN1-2C, GluN1-2A-2C, and GluN1-2D NMDARs. Mol Cell 82 23:4548-4563.e4. PubMed Id: 36309015. doi:10.1016/j.molcel.2022.10.008.
*GluN1a/GluN2D NMDA receptor with bound Glycine and glutamate: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.38 Å** cryo-EM structure	8E96	Data File Jmol Viewer 8E96	Chou et al. (2022). Chou TH, Kang H, Simorowski N, Traynelis SF, & Furukawa H (2022). Structural insights into assembly and function of GluN1-2C, GluN1-2A-2C, and GluN1-2D NMDARs. Mol Cell 82 23:4548-4563.e4. PubMed Id: 36309015. doi:10.1016/j.molcel.2022.10.008.
*GluN1a/GluN2D NMDA receptor with bound glycine and glutamate: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.90 Å** cryo-EM structure with bound glycine and CPP, 3.60 Å: 7YFF GluN1a mutant (E698C)/GluN2D, in cystines crosslinked state, 6.40 Å: 7YFO GluN1a mutant (E698C)/GluN2D, in cystines non-crosslinked state, 5.10 Å: 7YFR	7YFL	Data File Jmol Viewer 7YFL 7YFF 7YFO 7YFR	Zhang et al. (2023). Zhang J, Zhang M, Wang Q, Wen H, Liu Z, Wang F, Wang Y, Yao F, Song N, Kou Z, Li Y, Guo F, & Zhu S (2023). Distinct structure and gating mechanism in diverse NMDA receptors with GluN2C and GluN2D subunits. Nat Struct Mol Biol 30 5:629-639. PubMed Id: 36959261. doi:10.1038/s41594-023-00959-z.
*GluN1a/GluN2A/GluN2C NMDA receptor in complex with Nb-4: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 4.24 Å** cryo-EM structure	8E99	Data File Jmol Viewer 8E99	Chou et al. (2022). Chou TH, Kang H, Simorowski N, Traynelis SF, & Furukawa H (2022). Structural insights into assembly and function of GluN1-2C, GluN1-2A-2C, and GluN1-2D NMDARs. Mol Cell 82 23:4548-4563.e4. PubMed Id: 36309015. doi:10.1016/j.molcel.2022.10.008.
*GluN1b-GluN2B NMDA receptor heterodimer, amino-terminal domains bound to allosteric inhibitor 93-4: Xenopus laevis/Rattus norvegicus* E Eukaryota (expressed in Trichoplusia ni), 2.1 Å** bound to allosteric inhibitor 93-5, 2.72 Å: 6E7S bound to allosteric inhibitor 93-6, 2.31 Å: 6E7T bound to allosteric inhibitor 93-31, 2.27 Å: 6E7U bound to allosteric inhibitor 93-88, 2.6 Å: 6E7V bound to allosteric inhibitor 93-115, 2.67 Å: 6E7W bound to allosteric inhibitor 93-97, 2.58 Å: 6E7X	6E7R	Data File Jmol Viewer 6E7R 6E7V 6E7T 6E7S 6E7W 6E7X 6E7U	Regan et al. (2019). Regan MC, Zhu Z, Yuan H, Myers SJ, Menaldino DS, Tahirovic YA, Liotta DC, Traynelis SF, & Furukawa H (2019). Structural elements of a pH-sensitive inhibitor binding site in NMDA receptors. Nat Commun 10 1:321. PubMed Id: 30659174. doi:10.1038/s41467-019-08291-1.
*GluN1b-GluN2B NMDA receptor heterodimer, non-active state 1: Rattus norvegicus* E Eukaryota (expressed in Spodoptera frugiperda), 4.00 Å** cryo-EM structure non-active state 2, 3.99 Å: 6WHR active conformation, 4.39 Å: 6WHT in complex with SDZ 220-040 and L689,560, class 1. 3.93 Å: 6WHU in complex with SDZ 220-040 and L689,560, class 2. 4.05 Å: 6WHV in complex with GluN2B antagonist SDZ 220-040, class 1. 4.09 Å: 6WHW in complex with GluN2B antagonist SDZ 220-040, class 2, 4.09 Å: 6WHX in complex with GluN1 antagonist L689,560, class 1. 4.03 Å: 6WHY complex with GluN1 antagonist L689,560, class 2. 4.27 Å: 6WI0 GluN1/GluN2A ligand-binding domain in complex with L689,560 and glutamate (x-ray) 2.09 Å: 6USU GluN1/GluN2A ligand-binding domain in complex with glycine and SDZ 220-040 (x-ray) 2.30 Å: 6USV	6WHS	Data File Jmol Viewer 6WHS 6USV 6USU 6WI0 6WHW 6WHT 6WHY 6WHX 6WHU 6WHV 6WHR	Chou et al. (2020). Chou TH, Tajima N, Romero-Hernandez A, & Furukawa H (2020). Structural Basis of Functional Transitions in Mammalian NMDA Receptors. Cell 182 2:357-371.e13. PubMed Id: 32610085. doi:10.1016/j.cell.2020.05.052.
*GluN1b-GluN2B NMDA receptor heterodimer, complexed to Fab2 class1: Rattus norvegicus* E Eukaryota (expressed in Spodoptera frugiperda), 3.92 Å** cryo-EM structure complexed to Fab2 non-active1-like, 4.23 Å 7TEB complexed to Fab2 Non-active2-like, 6.59 Å 7TEE complexed with Fab5 active conformation, 7.51 Å 7TEQ complexed with Fab5 non-active2 conformation, 5.23 Å 7TER complexed with Fab5 in Non-active1 conformation, 4.70 Å 7TES complexed with Fab5 in non-active2-like conformation, 4.45 Å 7TET	7TE9	Data File Jmol Viewer 7TE9 7TEE 7TEQ 7TEB 7TER 7TET 7TES	Tajima et al. (2022). Tajima N, Simorowski N, Yovanno RA, Regan MC, Michalski K, Gómez R, Lau AY, & Furukawa H (2022). Development and characterization of functional antibodies targeting NMDA receptors. Nat Commun 13 1:923. PubMed Id: 35177668. doi:10.1038/s41467-022-28559-3.
*GluN1b-GluN2B NMDA receptor heterodimer, amino-terminal domains bound to allosteric inhibitor 93-108: Xenopus laevis/Rattus norvegicus* E Eukaryota (expressed in Trichoplusia ni), 2.85 Å**	8G18	Data File Jmol Viewer 8G18	Harris et al. (2023). Harris LD, Regan MC, Myers SJ, Nocilla KA, Akins NS, Tahirovic YA, Wilson LJ, Dingledine R, Furukawa H, Traynelis SF, & Liotta DC (2023). Novel GluN2B-Selective NMDA Receptor Negative Allosteric Modulator Possesses Intrinsic Analgesic Properties and Enhances Analgesia of Morphine in a Rodent Tail Flick Pain Model. ACS Chem Neurosci 14 5:917-935. PubMed Id: 36779874. doi:10.1021/acschemneuro.2c00779.
*GluN1b/GluN2D NMDA receptor with bound glycine and glutamate: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 5.10 Å** cryo-EM structure	7YFM	Data File Jmol Viewer 7YFM	Zhang et al. (2023). Zhang J, Zhang M, Wang Q, Wen H, Liu Z, Wang F, Wang Y, Yao F, Song N, Kou Z, Li Y, Guo F, & Zhu S (2023). Distinct structure and gating mechanism in diverse NMDA receptors with GluN2C and GluN2D subunits. Nat Struct Mol Biol 30 5:629-639. PubMed Id: 36959261. doi:10.1038/s41594-023-00959-z.
*GluN1/GluN2A NMDA receptor in the glutamate/glycine-bound state at pH 7.8: Homo sapiens* E Eukaryota (expressed in HEK293S cells), 4.5 Å** cryo-EM structure Class I at pH 6.3, 5.1 Å: 6IRF Class II at pH 6.3, 5.5 Å: 6IRG Class III, at pH 6.3, 7.8 Å: 6IRH	6IRA	Data File Jmol Viewer 6IRA 6IRF 6IRH 6IRG	Zhang et al. (2018). Zhang JB, Chang S, Xu P, Miao M, Wu H, Zhang Y, Zhang T, Wang H, Zhang J, Xie C, Song N, Luo C, Zhang X, & Zhu S (2018). Structural Basis of the Proton Sensitivity of Human GluN1-GluN2A NMDA Receptors. Cell Rep 25 13:3582-3590.e4. PubMed Id: 30590034. doi:10.1016/j.celrep.2018.11.071.
*GluN1/GluN2A NMDA receptor in complex with S-ketamine, glycine, and glutamate: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure GluN1-GluN2B NMDA receptor in complex with S-ketamine, glycine, and glutamate, 4.07 Å 7EU8	7EU7	Data File Jmol Viewer 7EU7 7EU8	Zhang et al. (2021). Zhang Y, Ye F, Zhang T, Lv S, Zhou L, Du D, Lin H, Guo F, Luo C, & Zhu S (2021). Structural basis of ketamine action on human NMDA receptors. Nature 596 7871:301-305. PubMed Id: 34321660. doi:10.1038/s41586-021-03769-9.
*GluN1/GluN2A NMDA receptor, glycine/glutamate bound state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.90 Å** cryo-EM structure in the glycine/CPP bound state, 4.10 Å 7EOQ in the CGP-78608/glutamate bound state, 3.80 Å 7EOT in the glycine/glutamate/GNE-6901 bound state, 4.00 Å 7EOR in the glycine/glutamate/GNE-6901/9-AA bound state, 4.30 Å 7EOU	7EOS	Data File Jmol Viewer 7EOS 7EOT 7EOQ 7EOU 7EOR	Wang et al. (2021). Wang H, Lv S, Stroebel D, Zhang J, Pan Y, Huang X, Zhang X, Paoletti P, & Zhu S (2021). Gating mechanism and a modulatory niche of human GluN1-GluN2A NMDA receptors. Neuron 109 15:2443-2456.e5. PubMed Id: 34186027. doi:10.1016/j.neuron.2021.05.031.
*GluN1/GluN2C NMDA receptor with bound glycine and glutamate, asymmetric conformation: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure symmetric conformation, 4.30 Å: 8HDK with bound glycine, glutamate, and R-PYD-106, 3.00 Å: 7YFH	7YFG	Data File Jmol Viewer 7YFG 7YFH 8HDK	Zhang et al. (2023). Zhang J, Zhang M, Wang Q, Wen H, Liu Z, Wang F, Wang Y, Yao F, Song N, Kou Z, Li Y, Guo F, & Zhu S (2023). Distinct structure and gating mechanism in diverse NMDA receptors with GluN2C and GluN2D subunits. Nat Struct Mol Biol 30 5:629-639. PubMed Id: 36959261. doi:10.1038/s41594-023-00959-z.
*GluN1/GluN2A/GluN2C NMDA receptor with bound glycine and glutamate: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	7YFI	Data File Jmol Viewer 7YFI	Zhang et al. (2023). Zhang J, Zhang M, Wang Q, Wen H, Liu Z, Wang F, Wang Y, Yao F, Song N, Kou Z, Li Y, Guo F, & Zhu S (2023). Distinct structure and gating mechanism in diverse NMDA receptors with GluN2C and GluN2D subunits. Nat Struct Mol Biol 30 5:629-639. PubMed Id: 36959261. doi:10.1038/s41594-023-00959-z.
*GluR1 Glutamate receptor ligand binding domain with bound Glu: Adineta vaga* E Eukaryota (expressed in E. coli), 1.37 Å** The structure does not include transmembrane domain. with bound Asp, 1.66 Å: 4IO3 with bound Ser, 1.94 Å: 4IO4 with bound Ala, 1.72 Å: 4IO5 with bound Met, 1.60 Å: 4IO6 with bound Phe, 1.92 Å: 4IO7	4IO2	Data File Jmol Viewer 4IO2 4IO4 4IO5 4IO3 4IO7 4IO6	Lomash et al. (2013). Lomash S, Chittori S, Brown P, & Mayer ML (2013). Anions Mediate Ligand Binding in Adineta vaga Glutamate Receptor Ion Channels. Structure 21 :414-425. PubMed Id: 23434404. doi:10.1016/j.str.2013.01.006.
*GluK1 Glutamate receptor (Kainate-subtype; full length) with L-Glu: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 4.60 Å** cryo-EM structure	7LVT	Data File Jmol Viewer 7LVT	Selvakumar et al. (2021). Selvakumar P, Lee J, Khanra N, He C, Munguba H, Kiese L, Broichhagen J, Reiner A, Levitz J, & Meyerson JR (2021). Structural and compositional diversity in the kainate receptor family. Cell Rep 37 4:109891. PubMed Id: 34706237. doi:10.1016/j.celrep.2021.109891.
*GluK2 Glutamate receptor (Kainate-subtype) in desensitized state with bound 2S,4R-4-methylglutamate: Rattus norvegicus* E Eukaryota (expressed in S. frugiperda), 7.6 Å**	4UQQ	Data File Jmol Viewer 4UQQ	Meyerson et al. (2014). Meyerson JR, Kumar J, Chittori S, Rao P, Pierson J, Bartesaghi A, Mayer ML, & Subramaniam S (2014). Structural mechanism of glutamate receptor activation and desensitization. Nature 514 :328-334. PubMed Id: 25119039. doi:10.1038/nature13603.
*GluK2_EM Glutamate receptor (Kainate-subtype) with bound 2S,4R-4-methylglutamate: Rattus norvegicus* E Eukaryota (expressed in S. frugiperda), 3.8 Å** cryo-EM structure GluK2_EM with LY66195, 11.6 Å: 5KUH GluK2_EM dimer assembly complex with with bound 2S,4R-4-methylglutamate, x-ray 1.27 Å: 5CMM GluK2_EM dimer assembly complex with LY66195, x-ray 1.8 Å: 5CMK	5KUF	Data File Jmol Viewer 5KUF 5CMM 5CMK 5KUH	Meyerson et al. (2016). Meyerson JR, Chittori S, Merk A, Rao P, Han TH, Serpe M, Mayer ML, & Subramaniam S (2016). Structural basis of kainate subtype glutamate receptor desensitization. Nature 537 :567-571. PubMed Id: 27580033. doi:10.1038/nature19352.
*GluK2 Glutamate receptor in complex with NETO2, desensitized state: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.80 Å** cryo-EM structure DNQX-bound GluK2-2xNeto2 complex, 6.40 Å 7F5A DNQX-bound GluK2-1xNeto2 complex, 4.20 Å 7F59 LBD-TMD focused reconstruction of DNQX-bound GluK2-1xNeto2 complex, 3.90 Å 7F5B DNQX-bound GluK2-1xNeto2 complex, with asymmetric LBD 4.10 Å 7F56	7F57	Data File Jmol Viewer 7F57 7F5A 7F59 7F5B 7F56	He et al. (2021). He L, Sun J, Gao Y, Li B, Wang Y, Dong Y, An W, Li H, Yang B, Ge Y, Zhang XC, Shi YS, & Zhao Y (2021). Kainate receptor modulation by NETO2. Nature 599 7884:325-329. PubMed Id: 34552241. doi:10.1038/s41586-021-03936-y.
*GluK2 Glutamate receptor (Kainate-subtype), full-length, with bound positive allosteric modulator BPAM344: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.96 Å** cryo-EM structure amino-terminal domain, with bound BPAM344, 3.10 Å: 8FWR ligand-binding and transmembrane domains, with bound BPAM344, 3.23 Å: 8FWS amino-terminal domain, with bound BPAM344 and competitive antagonist DNQX, 3.09 Å: 8FWT ligand-binding and transmembrane domains, with bound BPAM344 and DNQX, 3.18 Å: 8FWU amino-terminal domain, with bound BPAM344 and noncompetitive inhibitor perampanel , 3.10 Å: 8FWV ligand-binding and transmembrane domains, with bound BPAM344 and perampanel, 3.10 Å: 8FWW	8FWQ	Data File Jmol Viewer 8FWQ 8FWT 8FWV 8FWR 8FWS 8FWW 8FWU	Gangwar et al. (2023). Gangwar SP, Yen LY, Yelshanskaya MV, & Sobolevsky AI (2023). Positive and negative allosteric modulation of GluK2 kainate receptors by BPAM344 and antiepileptic perampanel. Cell Rep 42 2:112124. PubMed Id: 36857176. doi:10.1016/j.celrep.2023.112124.
*GluK2/K5 heteromeric Glutamate receptor (Kainate-subtype) in complex with with 6-Cyano-7-nitroquinoxaline-2,3-dione (CNQX): Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 5.30 Å** cryo-EM structure in complex with L-Glu, 5.80 Å: 7KS3	7KS0	Data File Jmol Viewer 7KS0 7KS3	Khanra et al. (2021). Khanra N, Brown PMGE, Perozzo AM, Bowie D, & Meyerson JR (2021). Architecture and structural dynamics of the heteromeric GluK2/K5 kainate receptor. Elife 10 :e66097. PubMed Id: 33724189. doi:10.7554/eLife.66097.
*GluK3 Glutamate receptor (Kainate-subtype), desensitized state: Rattus norvegicus* E Eukaryota, 7.4 Å** cryo-EM structure in complex with UBP310, 7.6 Å: 6JFZ by x-ray:ligand binding domain complex with SYM and zinc, 1.83 Å: 6JMV	6JFY	Data File Jmol Viewer 6JFY 6JMV 6JFZ	Kumari et al. (2019). Kumari J, Vinnakota R, & Kumar J (2019). Structural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery. Sci Rep 9 1:10254. PubMed Id: 31311973. doi:10.1038/s41598-019-46770-z.
*GluK3 Glutamate receptor (Kainate-subtype) in complex with kainate: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 9.6 Å** cryo-EM structure in complex with UBP301, 10.6 Å: 6L6F	6KZM	Data File Jmol Viewer 6KZM 6L6F	Kumari et al. (2020). Kumari J, Bendre AD, Bhosale S, Vinnakota R, Burada AP, Tria G, Ravelli RBG, Peters PJ, Joshi M, & Kumar J (2020). Structural dynamics of the GluK3-kainate receptor neurotransmitter binding domains revealed by cryo-EM. Int J Biol Macromol 149 :1051-1058. PubMed Id: 32006583. doi:10.1016/j.ijbiomac.2020.01.282.
*M2 proton channel (AM2): Influenza A (synthesized)* V Viruses, 2.05 Å** with amantadine inhibitor, 3.50 Å: 3C9J	3BKD	Data File Jmol Viewer 3BKD 3C9J	Stouffer et al. (2008). Stouffer AL, Acharya R, Salom D, Levine AS, Di Costanzo L, Soto CS, Tereshko V, Nanda V, Stayrook S, & DeGrado WF. (2008). Structural basis for the function and inhibition of an influenza virus proton channel. Nature 451 :596-599. PubMed Id: 18235504.
*M2 proton channel (AM2): Influenza A* V Viruses (expressed in E. coli), NMR structure** with rimantadine inhibitor	2RLF	Data File Jmol Viewer 2RLF	Schnell & Chou. (2008). Schnell JR & Chou JJ (2008). Structure and mechanism of the M2 proton channel of influenza A virus. Nature 451 :591-595. PubMed Id: 18235503.
*M2 proton channel (AM2) H5N1 S31N drug-resistant mutant: Influenza A* V Viruses (expressed in E. coli), NMR structure**	2KIH	Data File Jmol Viewer 2KIH	Pielak et al. (2009). Pielak RM, Schnell JR, & Chou JJ (2009). Mechanism of drug inhibition and drug resistance of influenza A M2 channel. Proc Natl Acad Sci USA 106 :7379-7384. PubMed Id: 19383794. doi:10.1073/pnas.0902548106.
*M2 proton channel (AM2) in a hydrated lipid bilayer: Influenza A* V Viruses (expressed in E. coli), NMR structure**	2L0J	Data File Jmol Viewer 2L0J	Sharma et al. (2010). Sharma M, Yi M, Dong H, Qin H, Peterson E, Busath DD, Zhou HX, & Cross TA (2010). Insight into the mechanism of the influenza A proton channel from a structure in a lipid bilayer. Science 330 :509-512. PubMed Id: 20966252.
*M2 proton channel (AM2), S31N mutant in complex with M2WJ332: Influenza A* V Viruses (expressed in E. coli), NMR Structure**	2LY0	Data File Jmol Viewer 2LY0	Wang et al. (2013). Wang J, Wu Y, Ma C, Fiorin G, Wang J, Pinto LH, Lamb RA, Klein ML, & DeGrado WF (2013). Structure and inhibition of the drug-resistant S31N mutant of the M2 ion channel of influenza A virus. Proc Natl Acad Sci USA 110 :1315-1320. PubMed Id: 23302696. doi:10.1073/pnas.1216526110.
*M2 proton channel (AM2): Influenza A* V Viruses (expressed in Synthesized), 1.65 Å**	3LBW	Data File Jmol Viewer 3LBW	Acharya et al. (2010). Acharya R, Carnevale V, Fiorin G, Levine BG, Polishchuk AL, Balannik V, Samish I, Lamb RA, Pinto LH, DeGrado WF, & Klein ML (2010). Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus. Proc Natl Acad Sci USA 107 :15075-15080. PubMed Id: 20689043. doi:10.1073/pnas.1007071107.
*M2 proton channel (AM2) at low pH: Influenza A* V Viruses (expressed in Synthesized), 1.10 Å** at high pH, 1.10 Å: 4QK7	4QKC	Data File Jmol Viewer 4QKC 4QK7	Thomaston et al. (2015). Thomaston JL, Alfonso-Prieto M, Woldeyes RA, Fraser JS, Klein ML, Fiorin G, & DeGrado WF (2015). High-resolution structures of the M2 channel from influenza A virus reveal dynamic pathways for proton stabilization and transduction. Proc Natl Acad Sci USA 112 :14260-14265. PubMed Id: 26578770. doi:10.1073/pnas.1518493112.
*M2 proton channel (AM2), low-pH state (pH 5.5): Influenza A* V Viruses (expressed in Synthesized), 1.41 Å** XFEL structure. Cubic-phase crystallization. intermediate-pH state (pH 6.5), 1.45 Å: 5UM1 high-pH state (pH 8.0), 1.4 Å: 5TTC	5JOO	Data File Jmol Viewer 5JOO 5UM1 5TTC	Thomaston et al. (2017). Thomaston JL, Woldeyes RA, Nakane T, Yamashita A, Tanaka T, Koiwai K, Brewster AS, Barad BA, Chen Y, Lemmin T, Uervirojnangkoorn M, Arima T, Kobayashi J, Masuda T, Suzuki M, Sugahara M, Sauter NK, Tanaka R, Nureki O, Tono K, Joti Y, Nango E, Iwata S, Yumoto F, Fraser JS, & DeGrado WF (2017). XFEL structures of the influenza M2 proton channel: Room temperature water networks and insights into proton conduction. Proc Natl Acad Sci USA 114 51:13357-13362. PubMed Id: 28835537. doi:10.1073/pnas.1705624114.
*M2 proton channel (AM2) with bound amantadine: Influenza A* V Viruses (expressed in synthesized), 2.00 Å** with bound rimantadine, 2.00 Å: 6BKL with bound rimantadine (inward-open state), 2.25 Å: 6BOC bound to a spiroadamantane inhibitor, 2.64 Å: 6BMZ	6BKK	Data File Jmol Viewer 6BKK 6BOC 6BMZ 6BKL	Thomaston et al. (2018). Thomaston JL, Polizzi NF, Konstantinidi A, Wang J, Kolocouris A, & DeGrado WF (2018). Inhibitors of the M2 Proton Channel Engage and Disrupt Transmembrane Networks of Hydrogen-Bonded Waters. J Am Chem Soc 140 45:15219-15226. PubMed Id: 30165017. doi:10.1021/jacs.8b06741.
*M2 proton channel (AM2), S31N mutant: Influenza A virus* V Viruses, 2.06 Å**	6MJH	Data File Jmol Viewer 6MJH	Thomaston et al. (2019). Thomaston JL, Wu Y, Polizzi N, Liu L, Wang J, & DeGrado WF (2019). X-ray Crystal Structure of the Influenza A M2 Proton Channel S31N Mutant in Two Conformational States: An Open and Shut Case. J Am Chem Soc 141 29:11481-11488. PubMed Id: 31184871. doi:10.1021/jacs.9b02196.
*M2 proton channel (AM2) V27A mutant bound to spiroadamantyl amine inhibitor: Influenza A virus* V Viruses (expressed in synthesized), 2.5 Å** TM + cytosolic helix construct, 3.01 Å: 6OUG	6NV1	Data File Jmol Viewer 6NV1 6OUG	Thomaston et al. (2020). Thomaston JL, Konstantinidi A, Liu L, Lambrinidis G, Tan J, Caffrey M, Wang J, Degrado WF, & Kolocouris A (2020). X-ray Crystal Structures of the Influenza M2 Proton Channel Drug-Resistant V27A Mutant Bound to a Spiro-Adamantyl Amine Inhibitor Reveal the Mechanism of Adamantane Resistance. Biochemistry 59 4:627-634. PubMed Id: 31894969. doi:10.1021/acs.biochem.9b00971.
*M2 proton channel (BM2): Influenza B* V Viruses (expressed in Escherichia coli), NMR Structure** Cytoplasmic domain, NMR Structure: 2KJ1	2KIX	Data File Jmol Viewer 2KIX 2KJ1	Wang et al. (2009). Wang J, Pielak RM, McClintock MA, & Chou JJ (2009). Solution structure and functional analysis of the influenza B proton channel. Nat Struct Mol Biol 16 :1267-1271. PubMed Id: 19898475.
*M2 proton channel (BM2): closed state, pH 7.5: influenza B* V Viruses (expressed in E. coli), NMR structure** open state pH 4.5, 6PVT	6PVR	Data File Jmol Viewer 6PVR 6PVT	Mandala et al. (2020). Mandala VS, Loftis AR, Shcherbakov AA, Pentelute BL, & Hong M (2020). Atomic structures of closed and open influenza B M2 proton channel reveal the conduction mechanism. Nat Struct Mol Biol 27 2:160-167. PubMed Id: 32015551. doi:10.1038/s41594-019-0371-2.
*M2A-M2B chimeric proton channel (AM2-BM2): Influenza A/Influenza B* V Viruses (expressed in E. coli), NMR Structure** With rimantadine inhibitor, NMR structure: 2LJC	2LJB	Data File Jmol Viewer 2LJB 2LJC	Pielak et al. (2011). Pielak RM, Oxenoid K, & Chou JJ (2011). Structural Investigation of Rimantadine Inhibition of the AM2-BM2 Chimera Channel of Influenza Viruses. Structure 19 :1655-1663. PubMed Id: 22078564. doi:10.1016/j.str.2011.09.003.
*SARS-CoV-2 Envelope Protein Transmembrane Domain: Pentameric: Severe acute respiratory syndrome coronavirus 2* V Viruses (expressed in E. coli), NMR structure**	7K3G	Data File Jmol Viewer 7K3G	Mandala et al. (2020). Mandala VS, McKay MJ, Shcherbakov AA, Dregni AJ, Kolocouris A, & Hong M (2020). Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers. Nat Struct Mol Biol 27 12:1202-1208. PubMed Id: 33177698. doi:10.1038/s41594-020-00536-8.
*p7 hexamer channel: Hepatitis C virus (isolate EUH1480)* V Viruses (expressed in E. coli), NMR Structure**	2M6X	Data File Jmol Viewer 2M6X	OuYang et al. (2013). OuYang B, Xie S, Berardi MJ, Zhao X, Dev J, Yu W, Sun B, & Chou JJ (2013). Unusual architecture of the p7 channel from hepatitis C virus. Nature 498 :521-525. PubMed Id: 23739335. doi:10.1038/nature12283.
*ASIC1 Acid-Sensing Ion Channel (ΔASIC1; N- and C-term deletions): Gallus gallus* E Eukaryota (expressed in S. frugiperda), 1.9 Å** Construct does not exhibit proton-dependent gating	2QTS	Data File Jmol Viewer 2QTS	Jasti et al. (2007). Jasti J, Furukawa H, Gonzales EB, & Gouaux E (2007). Structure of acid-sensing ion channel 1 at 1.9 Å resolution and low pH. Nature 449 :316-323. PubMed Id: 17882215.
*ASIC1 Acid-Sensing Ion Channel (ASIC1mfc; minimal functional channel): Gallus gallus* E Eukaryota (expressed in S. frugiperda), 3.0 Å** Desensitized State	3HGC	Data File Jmol Viewer 3HGC	Gonzales et al. (2009). Gonzales EB, Kawate T, & Gouaux E (2009). Pore architecture and ion sites in acid-sensing ion channels and P2X receptors. Nature 460 :599-604. PubMed Id: 19641589.
*ASIC1 Acid-Sensing Ion Channel in complex with psalmotoxin 1 (PcTx1): Gallus gallus* E Eukaryota (expressed in S. frugiperda), 2.99 Å** Apo protein, 2.60 Å: 3S3W	3S3X	Data File Jmol Viewer 3S3X 3S3W	Dawson et al. (2012). Dawson RJ, Benz J, Stohler P, Tetaz T, Joseph C, Huber S, Schmid G, Hügin D, Pflimlin P, Trube G, Rudolph MG, Hennig M, & Ruf A (2012). Structure of the Acid-sensing ion channel 1 in complex with the gating modifier Psalmotoxin 1. Nature Commun 3 :936. PubMed Id: 22760635. doi:10.1038/ncomms1917.
*ASIC1 Acid-Sensing Ion Channel in complex with psalmotoxin 1 (PcTx1), pH 5.5: Gallus gallus* E Eukaryota (expressed in S. frugiperda), 2.80 Å** 13 AA removed from N-terminus, 63 AA removed from C-terminus (referred to as Δ13) at pH 7.25, 3.36 Å: 4FZ1	4FZ0	Data File Jmol Viewer 4FZ0 4FZ1	Baconguis & Gouaux (2012). Baconguis I & Gouaux E (2012). Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes. Nature 489 :400-405. PubMed Id: 22842900. doi:10.1038/nature11375.
*ASIC1 Acid-Sensing Ion Channel in complex with MitTx toxin: Gallus gallus* E Eukaryota (expressed in S. frugiperda), 2.07 Å** Δ13 construct (4FZ0 above). in complex with MitTx toxin and amiloride, 2.27 Å: 4NTX in complex with MitTx toxin and Cesium, 2.65 Å: 4NTY	4NTW	Data File Jmol Viewer 4NTW 4NTY 4NTX	Baconguis et al. (2014). Baconguis I, Bohlen CJ, Goehring A, Julius D, & Gouaux E (2014). X-Ray Structure of Acid-Sensing Ion Channel 1-Snake Toxin Complex Reveals Open State of a Na(+)-Selective Channel. Cell 156 :717-729. PubMed Id: 24507937. doi:10.1016/j.cell.2014.01.011.
*ASIC1a Acid-Sensing Ion Channel (residues 25-463) in resting state with barium.: Gallus gallus* E Eukaryota (expressed in HEK293S cells), 2.95 Å** resting state with calcium, 3.2 Å: 5WKV cryo-EM structure, 3.7 Å: 6AVE	5WKU	Data File Jmol Viewer 5WKU 6AVE 5WKV	Yoder et al. (2018). Yoder N, Yoshioka C, & Gouaux E (2018). Gating mechanisms of acid-sensing ion channels. Nature 555 7696:397-401. PubMed Id: 29513651. doi:10.1038/nature25782.
*ASIC1 Acid-Sensing Ion Channel (full length) solubilized by styrene maleic acid copolymer; desensitized state at low pH: Gallus gallus* E Eukaryota (expressed in HEK293 cells), 2.82 Å** cryo-EM structure resting state at high pH, 3.65 Å: 6VTL	6VTK	Data File Jmol Viewer 6VTK 6VTL	Yoder & Gouaux (2020). Yoder N, & Gouaux E (2020). The His-Gly motif of acid-sensing ion channels resides in a reentrant 'loop' implicated in gating and ion selectivity. Elife 9 . PubMed Id: 32496192. doi:10.7554/eLife.56527.
*ASIC1a Acid-Sensing Ion Channel, pH 8: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.56 Å** cryo-EM structure in complex with snake toxin Mambalgin1 at pH 8.0, 3.90 Å: 7CFT	7CFS	Data File Jmol Viewer 7CFS 7CFT	Sun et al. (2020). Sun D, Liu S, Li S, Zhang M, Yang F, Wen M, Shi P, Wang T, Pan M, Chang S, Zhang X, Zhang L, Tian C, & Liu L (2020). Structural insights into human acid-sensing ion channel 1a inhibition by snake toxin mambalgin1. Elife 9 :e57096. PubMed Id: 32915133. doi:10.7554/eLife.57096.
*ASIC1a Acid-Sensing Ion Channel in complex with Nb.C1 nanobody: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.86 Å** cryo-EM structure	7RNN	Data File Jmol Viewer 7RNN	Wu et al. (2021). Wu Y, Chen Z, Sigworth FJ, & Canessa CM (2021). Structure and analysis of nanobody binding to the human ASIC1a ion channel. Elife 10 :e67115. PubMed Id: 34319232. doi:10.7554/eLife.67115.
*proton-activated chloride (PAC/ASOR) channel, pH 8: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure at pH 4, 3.73 Å: 7JNC	7JNA	Data File Jmol Viewer 7JNA 7JNC	Ruan et al. (2020). Ruan Z, Osei-Owusu J, Du J, Qiu Z, & Lü W (2020). Structures and pH-sensing mechanism of the proton-activated chloride channel. Nature 588 7837:350-354. PubMed Id: 33149300. doi:10.1038/s41586-020-2875-7.
*proton-activated chloride (PAC/ASOR) channel, resting conformation: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.60 Å** cryo-EM structure activated conformation, 3.10 Å 7SQF desensitized conformation, 2.50 Å 7SQH	7SQG	Data File Jmol Viewer 7SQG 7SQH 7SQF	Wang et al. (2022). Wang C, Polovitskaya MM, Delgado BD, Jentsch TJ, & Long SB (2022). Gating choreography and mechanism of the human proton-activated chloride channel ASOR. Sci Adv 8 5:eabm3942. PubMed Id: 35108041. doi:10.1126/sciadv.abm3942.
*proton-activated chloride (PAC/ASOR) channel, pH 4.0 with diC₈-PI(4,5)P₂ using full map: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.71 Å** cryo-EM structure using focused map on the ECD and part of the TMD (residues 78-316), 2.70 Å: 8FBL	8EQ4	Data File Jmol Viewer 8EQ4 8FBL	Mihaljević et al. (2023). Mihaljević L, Ruan Z, Osei-Owusu J, Lü W, & Qiu Z (2023). Inhibition of the proton-activated chloride channel PAC by PIP2. Elife 12 :83935. PubMed Id: 36633397. doi:10.7554/eLife.83935.
*epithelial sodium channel ENaC: Homo sapiens* E Eukaryota (expressed in HEK293S cells), 3.9 Å** cryo-EM structure	6BQN	Data File Jmol Viewer 6BQN	Noreng et al. (2018). Noreng S, Bharadwaj A, Posert R, Yoshioka C, & Baconguis I (2018). Structure of the human epithelial sodium channel by cryo-electron microscopy. Elife 7 :e39340. PubMed Id: 30251954. doi:10.7554/eLife.39340.
*epithelial sodium channel ENaC, reveals molecular source of assembly: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.06 Å** cryo-EM structure	6WTH	Data File Jmol Viewer 6WTH	Noreng et al. (2020). Noreng S, Posert R, Bharadwaj A, Houser A, & Baconguis I (2020). Molecular principles of assembly, activation, and inhibition in epithelial sodium channel. Elife 9 :e59038. PubMed Id: 32729833. doi:10.7554/eLife.59038.
*MgtE Mg²⁺ Transporter: Thermus thermophilus* B Bacteria (expressed in E. coli), 3.5 Å** Cytoplasmic domains w. bound Mg²⁺, 2.30 Å: 2YVY Cytoplasmic domains without Mg²⁺, 3.90 Å: 2YVZ	2YVX	Data File Jmol Viewer 2YVX 2YVY 2YVZ	Hattori et al. (2007). Hattori M, Tanaka Y, Fukai S, Ishitani R, & Nureki O (2007). Crystal structure of the MgtE Mg₂⁺transporter. Nature 448 :1072-1075. PubMed Id: 17700703.
*MgtE Mg²⁺ Transporter: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.9 Å**	2ZY9	Data File Jmol Viewer 2ZY9	Hattori et al. (2009). Hattori M, Iwase N, Furuya N, Tanaka Y, Tsukazaki T, Ishitani R, Maguire ME, Ito K, Maturana A, & Nureki O (2009). Mg(²⁺)-dependent gating of bacterial MgtE channel underlies Mg(²⁺) homeostasis. EMBO J 28 :3602-3612. PubMed Id: 19798051.
*MgtE Mg²⁺ Transporter with bound Mg²⁺: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.30 Å** with bound Mn²⁺, 2.2 Å:4U9N with bound Ca²⁺, 3.2 Å: 4WIB	4U9L	Data File Jmol Viewer 4U9L 4U9N 4WIB	Takeda et al. (2014). Takeda H, Hattori M, Nishizawa T, Yamashita K, Shah ST, Caffrey M, Maturana AD, Ishitani R, & Nureki O (2014). Structural basis for ion selectivity revealed by high-resolution crystal structure of Mg²⁺ channel MgtE. Nat Commun 5 :5374. PubMed Id: 25367295. doi:10.1038/ncomms6374.
*MgtE Mg²⁺ Transporter in complex with ATP: Thermus thermophilus* B Bacteria (expressed in E. coli), 3.60 Å** cytosolic domain, 3.00 Å: 5X9G	5X9H	Data File Jmol Viewer 5X9H 5X9G	Tomita et al. (2017). Tomita A, Zhang M, Jin F, Zhuang W, Takeda H, Maruyama T, Osawa M, Hashimoto KI, Kawasaki H, Ito K, Dohmae N, Ishitani R, Shimada I, Yan Z, Hattori M, & Nureki O (2017). ATP-dependent modulation of MgtE in Mg²⁺ homeostasis. Nat Commun 8 1. PubMed Id: 28747715. doi:10.1038/s41467-017-00082-w.
*MgtE Mg²⁺ Transporter, Mg²⁺ free: Thermus thermophilus* B Bacteria (expressed in E. coli), 3.70 Å** cryo-EM structure	6LBH	Data File Jmol Viewer 6LBH	Jin et al. (2021). Jin F, Sun M, Fujii T, Yamada Y, Wang J, Maturana AD, Wada M, Su S, Ma J, Takeda H, Kusakizako T, Tomita A, Nakada-Nakura Y, Liu K, Uemura T, Nomura Y, Nomura N, Ito K, Nureki O, Namba K, Iwata S, Yu Y, & Hattori M (2021). The structure of MgtE in the absence of magnesium provides new insights into channel gating. PLoS Biol 19 4. PubMed Id: 33905418. doi:10.1371/journal.pbio.3001231.
*SLAC1 anion channel, TehA homolog (wild-type): Haemophilus influenzae* B Bacteria (expressed in E. coli), 1.2 Å** F262A mutant, 1.15 Å: 3M73 F262L mutant, 1.65 Å: 3M74 F262V mutant, 1.60 Å: 3M75 G15D mutant, 1.50 Å: 3M76	3M71	Data File Jmol Viewer 3M71 3M76 3M73 3M75 3M74	Chen et al. (2010). Chen YH, Hu L, Punta M, Bruni R, Hillerich B, Kloss B, Rost B, Love J, Siegelbaum SA, & Hendrickson WA (2010). Homologue structure of the SLAC1 anion channel for closing stomata in leaves. Nature 467 :1074-1080. PubMed Id: 20981093.
*SLAC1 anion channel, TehA homolog (wild-type) at room temperature.: Haemophilus influenzae* B Bacteria (expressed in E. coli), 2.30 Å**	4YCR	Data File Jmol Viewer 4YCR	Axford et al. (2015). Axford D, Foadi J, Hu NJ, Choudhury HG, Iwata S, Beis K, Evans G, & Alguel Y (2015). Structure determination of an integral membrane protein at room temperature from crystals in situ. Acta Crystallogr D Biol Crystallogr 71 :1228-1237. PubMed Id: 26057664. doi:10.1107/S139900471500423X.
*SLAC1 anion channel, TehA homolog, native-SAD structure determined at 5 keV in helium: Haemophilus influenzae* B Bacteria (expressed in E. coli), 2.60 Å**	8EN9	Data File Jmol Viewer 8EN9	Karasawa et al. (2022). Karasawa A, Andi B, Fuchs MR, Shi W, McSweeney S, Hendrickson WA, & Liu Q (2022). Multi-crystal native-SAD phasing at 5 keV with a helium environment. IUCrJ 9 6:768-777. PubMed Id: 36381147. doi:10.1107/S205225252200971X.
*SLAC1 anion channel: Brachypodium distachyon* E Eukaryota (expressed in Schizosaccharomyces pombe), 2.97 Å** cryo-EM structure	7EN0	Data File Jmol Viewer 7EN0	Deng et al. (2021). Deng YN, Kashtoh H, Wang Q, Zhen GX, Li QY, Tang LH, Gao HL, Zhang CR, Qin L, Su M, Li F, Huang XH, Wang YC, Xie Q, Clarke OB, Hendrickson WA, & Chen YH (2021). Structure and activity of SLAC1 channels for stomatal signaling in leaves. Proc Natl Acad Sci U S A 118 18:e2015151118. PubMed Id: 33926963. doi:10.1073/pnas.2015151118.
*SLAC1 anion channel, S59A mutant: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 2.70 Å** cryo-EM structure	7WNQ	Data File Jmol Viewer 7WNQ	Li et al. (2022). Li Y, Ding Y, Qu L, Li X, Lai Q, Zhao P, Gao Y, Xiang C, Cang C, Liu X, & Sun L (2022). Structure of the Arabidopsis guard cell anion channel SLAC1 suggests activation mechanism by phosphorylation. Nat Commun 13 1:2511. PubMed Id: 35523967. doi:10.1038/s41467-022-30253-3.
*ATP-gated P2X₂ ion channel in the presence of ATP and Zn²⁺: Amblyomma maculatum* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å**	5F1C	Data File Jmol Viewer 5F1C	Kasuya et al. (2016). Kasuya G, Fujiwara Y, Takemoto M, Dohmae N, Nakada-Nakura Y, Ishitani R, Hattori M, & Nureki O (2016). Structural Insights into Divalent Cation Modulations of ATP-Gated P2X Receptor Channels. Cell Rep 14 4:932-944. PubMed Id: 26804916. doi:10.1016/j.celrep.2015.12.087.
*ATP-gated P2X₃ ion channel, closed apo state: Homo sapiens* E Eukaryota (expressed in HEK293S), 2.98 Å** ATP-bound, open state, 2.77 Å: 5SVK ATP-bound, closed(desensitized) state, 2.9 Å: 5SVL bound to agonist 2-methylthio-ATP in the desensitized state, 3.09 Å: 5SVM agonist 2-methylthio-ATP bound in desensitized state, 3.3 Å: 5SVP bound to competitive antagonist TNP-ATP, 3.25 Å: 5SVQ bound to competitive antagonist A-317491, 3.13 Å: 5SVR Mn²⁺ divalent cation-binding site, 4.03 Å: 5SVS Cs⁺ at Na⁺ entry site, 3.79 Å: 5SVT	5SVJ	Data File Jmol Viewer 5SVJ 5SVK 5SVQ 5SVR 5SVM 5SVT 5SVS 5SVL 5SVP	Mansoor et al. (2016). Mansoor SE, Lü W, Oosterheert W, Shekhar M, Tajkhorshid E, & Gouaux E (2016). X-ray structures define human P2X₃ receptor gating cycle and antagonist action. Nature 538 :66-71. PubMed Id: 27626375. doi:10.1038/nature19367.
*ATP-gated P2X₃ ion channel in complex with AF-219 negative allosteric modulator: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.4 Å**	5YVE	Data File Jmol Viewer 5YVE	Wang et al. (2018). Wang J, Wang Y, Cui WW, Huang Y, Yang Y, Liu Y, Zhao WS, Cheng XY, Sun WS, Cao P, Zhu MX, Wang R, Hattori M, & Yu Y (2018). Druggable negative allosteric site of P2X3 receptors. Proc Natl Acad Sci USA 115 19:4939-4944. PubMed Id: 29674445. doi:10.1073/pnas.1800907115.
*ATP-gated P2X₃ ion channel in complex with ATP and Ca²⁺: Homo sapiens* E Eukaryota (expressed in HEK293), 3.30 Å** in complex with ATP and Mg²⁺, 3.82 Å:6AH5	6AH4	Data File Jmol Viewer 6AH4 6AH5	Li et al. (2019). Li M, Wang Y, Banerjee R, Marinelli F, Silberberg S, Faraldo-Gómez JD, Hattori M, & Swartz KJ (2019). Molecular mechanisms of human P2X₃ receptor channel activation and modulation by divalent cation bound ATP. Elife 8 :e47060. PubMed Id: 31232692. doi:10.7554/eLife.47060.
*ATP-gated P2X₄ ion channel (apo protein; ΔP2X₄-B construct): Danio rerio (zebra fish)* E Eukaryota (expressed in S. frugiperda), 3.1 Å** Closed state. ΔP2X₄-A construct, 3.5 Å: 3I5D	3H9V	Data File Jmol Viewer 3H9V 3I5D	Kawate et al. (2009). Kawate T, Michel JC, Birdsong WT, & Gouaux E (2009). Crystal structure of the ATP-gated P2X₄ion channel in the closed state. Nature 460 :592-598. PubMed Id: 19641588.
*ATP-gated P2X₄ ion channel with bound ATP in open-pore conformation: Danio rerio (zebra fish)* E Eukaryota (expressed in S. frugiperda ), 2.80 Å** Structure without bound ATP, 2.90 Å: 4DW0	4DW1	Data File Jmol Viewer 4DW1 4DW0	Hattori & Gouaux (2012). Hattori M & Gouaux E (2012). Molecular mechanism of ATP binding and ion channel activation in P2X receptors. Nature 485 :207-2112. PubMed Id: 22535247. doi:10.1038/nature11010.
*ATP-gated P2X₄ ion channel with bound BX430: Danio rerio* E Eukaryota (expressed in S. frugiperda), 3.23 Å** cryo-EM structure with bound BAY-1797, 3.43 Å: 8JV6	8JV5	Data File Jmol Viewer 8JV5 8JV6	Shen et al. (2023). Shen C, Zhang Y, Cui W, Zhao Y, Sheng D, Teng X, Shao M, Ichikawa M, Wang J, & Hattori M (2023). Structural insights into the allosteric inhibition of P2X4 receptors. Nat Commun 14 1:6437. PubMed Id: 37833294. doi:10.1038/s41467-023-42164-y.
*ATP-gated P2X₇ ion channel: Gallus gallus* E Eukaryota (expressed in HEK293S cells), 3.1 Å**	5XW6	Data File Jmol Viewer 5XW6	Kasuya et al. (2017). Kasuya G, Yamaura T, Ma XB, Nakamura R, Takemoto M, Nagumo H, Tanaka E, Dohmae N, Nakane T, Yu Y, Ishitani R, Matsuzaki O, Hattori M, & Nureki O (2017). Structural insights into the competitive inhibition of the ATP-gated P2X receptor channel. Nat Commun 8 1:876. PubMed Id: 29026074. doi:10.1038/s41467-017-00887-9.
*ATP-gated P2X₇ ion channel, apo protein in closed state: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 2.9 Å** cryo-EM structure ATP-bound open state, 3.3 Å: 6U9W	6U9V	Data File Jmol Viewer 6U9V 6U9W	McCarthy et al. (2019). McCarthy AE, Yoshioka C, & Mansoor SE (2019). Full-Length P2X₇ Structures Reveal How Palmitoylation Prevents Channel Desensitization. Cell 179 3:659-670.e13. PubMed Id: 31587896. doi:10.1016/j.cell.2019.09.017.
*Bestrophin-1 (BEST1) Ca²⁺-activated Cl^- channel: Gallus gallus* E Eukaryota (expressed in Pichia pastoris), 2.85 Å**	4RDQ	Data File Jmol Viewer 4RDQ	Kane Dickson et al. (2014). Kane Dickson V, Pedi L, & Long SB (2014). Structure and insights into the function of a Ca²⁺-activated Cl^- channel. Nature 516 7530:213-218. PubMed Id: 25337878. doi:10.1038/nature13913.
*Bestrophin-1 (BEST1) Ca²⁺-activated Cl^- channel I76A, F80A, F84A mutant: Gallus gallus* E Eukaryota (expressed in Pichia pastoris), 3.1 Å**	5T5N	Data File Jmol Viewer 5T5N	Vaisey et al. (2016). Vaisey G, Miller AN, & Long SB (2016). Distinct regions that control ion selectivity and calcium-dependent activation in the bestrophin ion channel. Proc Natl Acad Sci USA 113 :E7399–E7408. PubMed Id: 27821745. doi:10.1073/pnas.1614688113.
*Bestrophin-1 (BEST1) Ca²⁺-activated Cl^- channel, calcium-bound inactivated state: Gallus gallus* E Eukaryota (expressed in Komagataella pastoris), 3.1 Å** cryo-EM structure W287F mutant in open calcium-free state, 3.0 Å: 6N24 W287F mutant in open calcium-bound state, 2.7 Å: 6N25 calcium-free closed state, 3.0 Å: 2N26 calcium-bound closed state, 3.0 Å: 6N27 calcium-bound open state, 2.9 Å: 2N28	6N23	Data File Jmol Viewer 6N23 6N25 2N28 6N24 6N27 2N26	Miller et al. (2019). Miller AN, Vaisey G, & Long SB (2019). Molecular mechanisms of gating in the calcium-activated chloride channel bestrophin. Elife 8 :e43231. PubMed Id: 30628889. doi:10.7554/eLife.43231.
*Bestrophin-2 (BEST2) Ca²⁺-activated Cl^-1 channel, Ca²⁺-unbound state: Bos taurus* E Eukaryota (expressed in HEK293 cells), 3.03 Å** cryo-EM structure Ca²⁺-bound state, 3.00 Å: 6VX6 Ca²⁺-bound state (5 mM Ca²⁺), 2.36 Å: 6VX7 Ca²⁺-unbound state 2 (EGTA), 2.33 Å: 6VX8 Ca²⁺-unbound state 1 (EGTA), 2.17 Å: 6VX9	6VX5	Data File Jmol Viewer 6VX5 6VX9 6VX6 6VX7 6VX8	Owji et al. (2020). Owji AP, Zhao Q, Ji C, Kittredge A, Hopiavuori A, Fu Z, Ward N, Clarke OB, Shen Y, Zhang Y, Hendrickson WA, & Yang T (2020). Structural and functional characterization of the bestrophin-2 anion channel. Nat Struct Mol Biol 27 4:382-391. PubMed Id: 32251414. doi:10.1038/s41594-020-0402-z.
*KpBest Bestrophin homolog of the BEST1 Ca²⁺-activated Cl^- channel (ΔC7): Klebsiella pneumoniae* B Bacteria (expressed in E. coli), 2.90 Å** This homolog is not Ca²⁺ activated and conducts cations rather than anions. ΔC11, 2.30 Å: 4WD8	4WD7	Data File Jmol Viewer 4WD7 4WD8	Yang et al. (2014). Yang T, Liu Q, Kloss B, Bruni R, Kalathur RC, Guo Y, Kloppmann E, Rost B, Colecraft HM, & Hendrickson WA (2014). Structure and selectivity in bestrophin ion channels. Science 346 :355-359. PubMed Id: 25324390. doi:10.1126/science.1259723.
*Bestrophin-1 (BEST1) Ca²⁺-activated Cl⁻ channel, 1uM Ca2⁺ closed state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 1.82 Å** cryo-EM structure closed state, 5mM Ca²⁺, 2.05 Å: 8D1J Ca²⁺-bound partially open neck state, 2.28 Å: 8D1K Ca²⁺-bound partially open aperture state, 2.12 Å:8D1L Ca²⁺-unbound closed state, 3.11 Å: 8D1M truncated at residue 345, Ca²⁺-bound open state, 2.44 Å: 8D1O	8D1I	Data File Jmol Viewer 8D1I 8D1O 8D1J 8D1M 8D1K 8D1L	Owji et al. (2022). Owji AP, Wang J, Kittredge A, Clark Z, Zhang Y, Hendrickson WA, & Yang T (2022). Structures and gating mechanisms of human bestrophin anion channels. Nat Commun 13 1:3836. PubMed Id: 35789156. doi:10.1038/s41467-022-31437-7.
*Bestrophin-2 (BEST2) Ca²⁺-activated Cl− channel, 1uM Ca²⁺, closed state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 1.78 Å** cryo-EM structure 5mM Ca2⁺, closed state, 1.82 Å: 8D1F Ca²⁺-bound open state, 2.07 Å: 8D1G Ca²⁺-unbound closed state, 1.94 Å: 8D1H truncated at residue 345, Ca²⁺-bound open state, 8D1N	8D1E	Data File Jmol Viewer 8D1E 8D1G 8D1N 8D1H 8D1F	Owji et al. (2022). Owji AP, Wang J, Kittredge A, Clark Z, Zhang Y, Hendrickson WA, & Yang T (2022). Structures and gating mechanisms of human bestrophin anion channels. Nat Commun 13 1:3836. PubMed Id: 35789156. doi:10.1038/s41467-022-31437-7.
*ExbB/ExbD complex associated with TonB complex, pH 7.0: Escherichia coli* B Bacteria, 2.6 Å** ExbB/ExbD complex at pH 4.5, 3.5 Å: 5SV1	5SV0	Data File Jmol Viewer 5SV0 5SV1	Celia et al. (2016). Celia H, Noinaj N, Zakharov SD, Bordignon E, Botos I, Santamaria M, Barnard TJ, Cramer WA, Lloubes R, & Buchanan SK (2016). Structural insight into the role of the Ton complex in energy transduction. Nature 538 :60-65. PubMed Id: 27654919. doi:10.1038/nature19757.
*ExbB/ExbD complex associated with TonB complex in nanodiscs: Escherichia coli* B Bacteria, 3.3 Å** cryo-EM structure	6TYI	Data File Jmol Viewer 6TYI	Celia et al. (2019). Celia H, Botos I, Ni X, Fox T, De Val N, Lloubes R, Jiang J, & Buchanan SK (2019). Cryo-EM structure of the bacterial Ton motor subcomplex ExbB-ExbD provides information on structure and stoichiometry. Commun Biol 2 . PubMed Id: 31602407. doi:10.1038/s42003-019-0604-2.
*CLC-K chloride ion channel, class 1: Bos taurus* E Eukaryota (expressed in S. frugiperda), 3.76 Å** cryo-EM structure class 2, 3.95 Å: 5TR1	5TQQ	Data File Jmol Viewer 5TQQ 5TR1	Park et al. (2017). Park E, Campbell EB, & MacKinnon R (2017). Structure of a CLC chloride ion channel by cryo-electron microscopy. Nature 541 :500-505. PubMed Id: 28002411. doi:10.1038/nature20812.
*CLC-1 ion channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.36 Å** cryo-EM structure C-terminal cytosolic domain, 3.36 Å: 6COZ	6COY	Data File Jmol Viewer 6COY 6COZ	Park & MacKinnon (2018). Park E, & MacKinnon R (2018). Structure of the CLC-1 chloride channel from Homo sapiens. Elife 7 :e36629. PubMed Id: 29809153. doi:10.7554/eLife.36629.
*ClC-1 chloride channel membrane domain: Homo sapiens* E Eukaryota (expressed in S. cerevisiae), 3.63 Å** cryo-EM structure CBS state 1, 4 Å: 6QVC CBS state 2, 4.34 Å: 6QVD CBS state 3, 4.34 Å: 6QVB low pH structure, 4.2 Å: 6QVU	6QV6	Data File Jmol Viewer 6QV6 6QVB 6QVD 6QVU 6QVC	Wang et al. (2019). Wang K, Preisler SS, Zhang L, Cui Y, Missel JW, Grønberg C, Gotfryd K, Lindahl E, Andersson M, Calloe K, Egea PF, Klaerke DA, Pusch M, Pedersen PA, Zhou ZH, & Gourdon P (2019). Structure of the human ClC-1 chloride channel. PLoS Biol 17 4. PubMed Id: 31022181. doi:10.1371/journal.pbio.3000218.
*CLC-2 chloride ion channel membrane domain with bound AK-42 inhibitor: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure CLC-2 channel in apo state, 3.90 Å: 7XF5 TMD masked refine map, 3.50 Å: 7XJA	8GQU	Data File Jmol Viewer 8GQU 7XJA 7XF5	Ma et al. (2023). Ma T, Wang L, Chai A, Liu C, Cui W, Yuan S, Wing Ngor Au S, Sun L, Zhang X, Zhang Z, Lu J, Gao Y, Wang P, Li Z, Liang Y, Vogel H, Wang YT, Wang D, Yan K, & Zhang H (2023). Cryo-EM structures of ClC-2 chloride channel reveal the blocking mechanism of its specific inhibitor AK-42. Nat Commun 14 1:3424. PubMed Id: 37296152. doi:10.1038/s41467-023-39218-6.
*LRRC8A volume-regulated anion channel: Mus musculus* E Eukaryota (expressed in HEK293 cells), 4.25 Å** cryo-EM structure at 5.01 Å: 6G9L, pore domain, 3.66 Å: 6G8Z Leucine-rich repeat (LRR) by x-ray, 1.8 Å: 6FNW	6G9O	Data File Jmol Viewer 6G9O 6G9L 6G8Z 6FNW	Deneka et al. (2018). Deneka D, Sawicka M, Lam AKM, Paulino C, & Dutzler R (2018). Structure of a volume-regulated anion channel of the LRRC8 family. Nature . PubMed Id: 29769723. doi:10.1038/s41586-018-0134-y.
*LRRC8A-DCPIB in MSP1E3D1 nanodisc constricted state: Mus musculus* E Eukaryota (expressed in S. frugiperda), 3.21 Å** cryo-EM structure nanodisc expanded state, 3.32 Å: 6NZZ	6NZW	Data File Jmol Viewer 6NZW 6NZZ	Kern et al. (2019). Kern DM, Oh S, Hite RK, & Brohawn SG (2019). Cryo-EM structures of the DCPIB-inhibited volume-regulated anion channel LRRC8A in lipid nanodiscs. eLife 8 . PubMed Id: 30775971. doi:10.7554/eLife.42636.
*LRRC8A volume-regulated anion channel in complex with synthetic nanobody Sb1: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.06 Å** cryo-EM structure in complex with synthetic nanobody Sb2, 3.50 Å: 7P5W in complex with synthetic nanobody Sb3, 3.29 Å: 7P5Y in complex with synthetic nanobody Sb4 at 1:0.5 ratio, 3.80 Å: 7P60 in complex with synthetic nanobody Sb5, 3.80 Å: 7P6K	7P5V	Data File Jmol Viewer 7P5V 7P5W 7P5Y 7P60 7P6K	Deneka et al. (2021). Deneka D, Rutz S, Hutter CAJ, Seeger MA, Sawicka M, & Dutzler R (2021). Allosteric modulation of LRRC8 channels by targeting their cytoplasmic domains. Nat Commun 12 1:5435. PubMed Id: 34521847. doi:10.1038/s41467-021-25742-w.
*LRRC8A (SWELL1) volume-regulated anion channel in MSP1E3D1 lipid nanodiscs (Pose-1): Mus musculus* E Eukaryota (expressed in Spodoptera frugiperda), 3.65 Å** cryo-EM structure Pose-2, 3.69 Å	7M17	Data File Jmol Viewer 7M17	Gunasekar et al. (2022). Gunasekar SK, Xie L, Kumar A, Hong J, Chheda PR, Kang C, Kern DM, My-Ta C, Maurer J, Heebink J, Gerber EE, Grzesik WJ, Elliot-Hudson M, Zhang Y, Key P, Kulkarni CA, Beals JW, Smith GI, Samuel I, Smith JK, Nau P, Imai Y, Sheldon RD, Taylor EB, Lerner DJ, Norris AW, Klein S, Brohawn SG, Kerns R, & Sah R (2022). Small molecule SWELL1 complex induction improves glycemic control and nonalcoholic fatty liver disease in murine Type 2 diabetes. Nat Commun 13 1:784. PubMed Id: 35145074. doi:10.1038/s41467-022-28435-0.
*LRRC8A volume-regulated anion channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.25 Å** cryo-EM structure	5ZSU	Data File Jmol Viewer 5ZSU	Kasuya et al. (2018). Kasuya G, Nakane T, Yokoyama T, Jia Y, Inoue M, Watanabe K, Nakamura R, Nishizawa T, Kusakizako T, Tsutsumi A, Yanagisawa H, Dohmae N, Hattori M, Ichijo H, Yan Z, Kikkawa M, Shirouzu M, Ishitani R, & Nureki O (2018). Cryo-EM structures of the human volume-regulated anion channel LRRC8. Nat. Struct. Mol. Biol. 25 9:797-804. PubMed Id: 30127360. doi:10.1038/s41594-018-0109-6.
*LRRC8A (SWELL1) volume-regulated anion channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.4 Å** cryo-EM structure	6DJB	Data File Jmol Viewer 6DJB	Kefauver et al. (2018). Kefauver JM, Saotome K, Dubin AE, Pallesen J, Cottrell CA, Cahalan SM, Qiu Z, Hong G, Crowley CS, Whitwam T, Lee WH, Ward AB, & Patapoutian A (2018). Structure of the human volume regulated anion channel. Elife 7 :e38461. PubMed Id: 30095067. doi:10.7554/eLife.38461.
*LRRC8C-LRRC8A(IL1²⁵) Chimera, volume-regulated anion channel, Class 1: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.40 Å** cryo-EM structure Class 2, 3.60 Å: 8DXO Class 3, 3.70 Å: 8DXP Class 4, 3.80 Å: 8DXQ Class 5, 4.00 Å: 8DXR	8DXN	Data File Jmol Viewer 8DXN 8DXR 8DXQ 8DXO 8DXP	Takahashi et al. (2023). Takahashi H, Yamada T, Denton JS, Strange K, & Karakas E (2023). Cryo-EM structures of an LRRC8 chimera with native functional properties reveal heptameric assembly. Elife 12 :e82431. PubMed Id: 36897307. doi:10.7554/eLife.82431.
*LRRC8C Volume-Regulated Anion Channel, homomeric: Mus musculus* E Eukaryota (expressed in HEK293 cells), 4.60 Å** cryo-EM structure heteromeric, LRRC8C-LRRC8A, 6.60 Å: 8B42 heteromeric, LRRC8C-LRRC8A (1:1 co-transfected) in complex with nanobody Sb1, 3.80 Å: 8B41	8B40	Data File Jmol Viewer 8B40 8B42 8B41	Rutz et al. (2023). Rutz S, Deneka D, Dittmann A, Sawicka M, & Dutzler R (2023). Structure of a volume-regulated heteromeric LRRC8A/C channel. Nat Struct Mol Biol 30 1:52-61. PubMed Id: 36522427. doi:10.1038/s41594-022-00899-0.
*LRRC8D volume-regulated anion channel: Homo sapiens* E Eukaryota (expressed in sf9 cells), 4.36 Å** cryo-EM structure	6M04	Data File Jmol Viewer 6M04	Nakamura et al. (2020). Nakamura R, Numata T, Kasuya G, Yokoyama T, Nishizawa T, Kusakizako T, Kato T, Hagino T, Dohmae N, Inoue M, Watanabe K, Ichijo H, Kikkawa M, Shirouzu M, Jentsch TJ, Ishitani R, Okada Y, & Nureki O (2020). Cryo-EM structure of the volume-regulated anion channel LRRC8D isoform identifies features important for substrate permeation. Commun Biol 3 1:240. PubMed Id: 32415200. doi:10.1038/s42003-020-0951-z.
*SatP bacterial acetate channel: Escherichia coli* B Bacteria, 2.80 Å** Structurally similar to UreI-like channel 3UX4.	5ZUG	Data File Jmol Viewer 5ZUG	Sun et al. (2018). Sun P, Li J, Zhang X, Guan Z, Xiao Q, Zhao C, Song M, Zhou Y, Mou L, Ke M, Guo L, Geng J, & Deng D (2018). Crystal structure of the bacterial acetate transporter SatP reveals that it forms a hexameric channel. J Biol Chem 293 50:19492-19500. PubMed Id: 30333234. doi:10.1074/jbc.RA118.003876.
*Ctr1 high-affinity copper transporter, Cu⁺-free form: Salmo salar* E Eukaryota (expressed in Pichia pastoris), 3.03 Å** with bound Cu⁺, 3.21 Å: 6M98	6M97	Data File Jmol Viewer 6M97 6M98	Ren et al. (2019). Ren F, Logeman BL, Zhang X, Liu Y, Thiele DJ, & Yuan P (2019). X-ray structures of the high-affinity copper transporter Ctr1. Nat Commun 10 1. PubMed Id: 30918258. doi:10.1038/s41467-019-09376-7.
*OTOP1 otopetrin proton channel in nanodiscs: Danio rerio* E Eukaryota (expressed in HEK-293 cells), 2.98 Å** cryo-EM structure	6NF4	Data File Jmol Viewer 6NF4	Saotome et al. (2019). Saotome K, Teng B, Tsui CCA, Lee WH, Tu YH, Kaplan JP, Sansom MSP, Liman ER, & Ward AB (2019). Structures of the otopetrin proton channels Otop1 and Otop3. Nat Struct Mol Biol 26 6:518-525. PubMed Id: 31160780. doi:10.1038/s41594-019-0235-9.
*OTOP3 otopetrin proton channel: Xenopus tropicalis* E Eukaryota (expressed in HEK293 cells), 3.92 Å** cryo-EM structure	6O84	Data File Jmol Viewer 6O84	Chen et al. (2019). Chen Q, Zeng W, She J, Bai XC, & Jiang Y (2019). Structural and functional characterization of an otopetrin family proton channel. Elife 8 :e46710. PubMed Id: 30973323. doi:10.7554/eLife.46710.
*OTOP3 otopetrin proton channel in nanodiscs: Gallus gallus* E Eukaryota (expressed in HEK-293 cells), 3.32 Å** cryo-EM structure	6NF6	Data File Jmol Viewer 6NF6	Saotome et al. (2019). Saotome K, Teng B, Tsui CCA, Lee WH, Tu YH, Kaplan JP, Sansom MSP, Liman ER, & Ward AB (2019). Structures of the otopetrin proton channels Otop1 and Otop3. Nat Struct Mol Biol 26 6:518-525. PubMed Id: 31160780. doi:10.1038/s41594-019-0235-9.
*Pannexin 1 (Panx1) ATP release channel: Xenopus tropicalis* E Eukaryota (expressed in Komagataella pastoris), 3.38 Å** cryo-EM structure	6UZY	Data File Jmol Viewer 6UZY	Deng et al. (2020). Deng Z, He Z, Maksaev G, Bitter RM, Rau M, Fitzpatrick JAJ, & Yuan P (2020). Cryo-EM structures of the ATP release channel pannexin 1. Nat Struct Mol Biol 27 4:373-381. PubMed Id: 32231289. doi:10.1038/s41594-020-0401-0.
*Pannexin 1 (Panx1) ATP release channel: Xenopus tropicalis* E Eukaryota (expressed in Spodoptera frugiperda), 3.02 Å** cryo-EM structure	6VD7	Data File Jmol Viewer 6VD7	Michalski et al. (2020). Michalski K, Syrjanen JL, Henze E, Kumpf J, Furukawa H, & Kawate T (2020). The Cryo-EM structure of pannexin 1 reveals unique motifs for ion selection and inhibition. Elife 9 :e54670. PubMed Id: 32048993. doi:10.7554/eLife.54670.
*Pannexin 1 (Panx1) ATP release channel: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 3.77 Å** cryo-EM structure	6V6D	Data File Jmol Viewer 6V6D	Deng et al. (2020). Deng Z, He Z, Maksaev G, Bitter RM, Rau M, Fitzpatrick JAJ, & Yuan P (2020). Cryo-EM structures of the ATP release channel pannexin 1. Nat Struct Mol Biol 27 4:373-381. PubMed Id: 32231289. doi:10.1038/s41594-020-0401-0.
*Pannexin 1 (Panx1) ATP release channel: Homo sapiens* E Eukaryota (expressed in Sf9 cells), 4.10 Å** cryo-EM structure. In nanodiscs. D376E/D379E mutant, 3.60 Å: 6M67 in the presence of CBX, 4.60 Å: 6M68	6M66	Data File Jmol Viewer 6M66 6M68 6M67	Jin et al. (2020). Jin Q, Zhang B, Zheng X, Li N, Xu L, Xie Y, Song F, Bhat EA, Chen Y, Gao N, Guo J, Zhang X, & Ye S (2020). Cryo-EM structures of human pannexin 1 channel. Cell Res 30 5:449-451. PubMed Id: 32246089. doi:10.1038/s41422-020-0310-0.
*Pannexin 1 (Panx1) ATP release channel. Wild-type: Homo sapiens* E Eukaryota (expressed in HEK tsA201 cells), 2.83 Å** cryo-EM structure with C-terminal tail cleaved by caspase-7, 2.97 Å: 6WBG C-terminal tail cleaved by caspase-7, in complex with CBX, 4.39 Å: 6WBI with deletion of N-terminal helix and C-terminal tail, 6.01 Å: 6WBK with deletion of N-terminal helix and C-terminal tail, in complex with CBX, 5.13 Å: 6WBL N255A mutant, 2.86 Å: 6WBM N255A mutant, gap junction. 2.83 Å: 6WBN	6WBF	Data File Jmol Viewer 6WBF 6WBI 6WBM 6WBG 6WBL 6WBN 6WBK	Ruan et al. (2020). Ruan Z, Orozco IJ, Du J, & Lü W (2020). Structures of human pannexin 1 reveal ion pathways and mechanism of gating. Nature 584 7822:646-651. PubMed Id: 32494015. doi:10.1038/s41586-020-2357-y.
*Pannexin 1 (Panx1) ATP release channel, full length: Homo sapiens* E Eukaryota (expressed in insect cells), 3.10 Å** cryo-EM structure C-terminal truncated (Δ 380-426), 3.10 Å: 6LTN	6LTO	Data File Jmol Viewer 6LTO 6LTN	Mou et al. (2020). Mou L, Ke M, Song M, Shan Y, Xiao Q, Liu Q, Li J, Sun K, Pu L, Guo L, Geng J, Wu J, & Deng D (2020). Structural basis for gating mechanism of Pannexin 1 channel. Cell Res 30 5:452-454. PubMed Id: 32284561. doi:10.1038/s41422-020-0313-x.
*Pannexin 1 (Panx1) ATP release channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure	6M02	Data File Jmol Viewer 6M02	Qu et al. (2020). Qu R, Dong L, Zhang J, Yu X, Wang L, & Zhu S (2020). Cryo-EM structure of human heptameric Pannexin 1 channel. Cell Res 30 5:446-448. PubMed Id: 32203128. doi:10.1038/s41422-020-0298-5.
*Pannexin 1 (Panx1) ATP release channel, full-length: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.15 Å** cryo-EM structure	7DWB	Data File Jmol Viewer 7DWB	Zhang et al. (2021). Zhang S, Yuan B, Lam JH, Zhou J, Zhou X, Ramos-Mandujano G, Tian X, Liu Y, Han R, Li Y, Gao X, Li M, & Yang M (2021). Structure of the full-length human Pannexin1 channel and insights into its role in pyroptosis. Cell Discov 7 1:30. PubMed Id: 33947837. doi:10.1038/s41421-021-00259-0.
*Pannexin 1 (Panx1) ATP release channel in a nanodisc: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure C-terminal deletion mutant, 3.60 Å 7F8O N-terminal deletion mutant, 4.50 Å 7WSV showing a conformational change in the N-terminal domain and blocked pore, 3.40 Å 7F8N	7F8J	Data File Jmol Viewer 7F8J 7F8O 7WSV 7F8N	Kuzuya et al. (2022). Kuzuya M, Hirano H, Hayashida K, Watanabe M, Kobayashi K, Terada T, Mahmood MI, Tama F, Tani K, Fujiyoshi Y, & Oshima A (2022). Structures of human pannexin-1 in nanodiscs reveal gating mediated by dynamic movement of the N terminus and phospholipids. Sci Signal 15 720:eabg6941. PubMed Id: 35133866. doi:10.1126/scisignal.abg6941.
*Pannexin 1 (Panx1) ATP release channel, R217H mutant: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.87 Å** cryo-EM structure W74R/R75D mutant, 3.20 Å: 8GTT	8GTS	Data File Jmol Viewer 8GTS 8GTT	Hussain et al. (2024). Hussain N, Apotikar A, Pidathala S, Mukherjee S, Burada AP, Sikdar SK, Vinothkumar KR, & Penmatsa A (2024). Cryo-EM structures of pannexin 1 and 3 reveal differences among pannexin isoforms. Nat Commun 15 1:2942. PubMed Id: 38580658. doi:10.1038/s41467-024-47142-6.
*Pannexin 1 (Panx1) ATP release channel purified in Salipro nanoparticles: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure	8A3B	Data File Jmol Viewer 8A3B	Drulyte et al. (2023). Drulyte I, Gutgsell AR, Lloris-Garcerá P, Liss M, Geschwindner S, Radjainia M, Frauenfeld J, & Löving R (2023). Direct cell extraction of membrane proteins for structure-function analysis. Sci Rep 13 1:1420. PubMed Id: 36697499. doi:10.1038/s41598-023-28455-w.
*Pannexin 2 (Panx2) large pore ATP release channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.44 Å** cryo-EM structure	7XLB	Data File Jmol Viewer 7XLB	Zhang et al. (2023). Zhang H, Wang S, Zhang Z, Hou M, Du C, Zhao Z, Vogel H, Li Z, Yan K, Zhang X, Lu J, Liang Y, Yuan S, Wang D, & Zhang H (2023). Cryo-EM structure of human heptameric pannexin 2 channel. Nat Commun 14 1:1118. PubMed Id: 36869038. doi:10.1038/s41467-023-36861-x.
*Pannexin 2 (Panx2) large pore ATP release channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.92 Å** cryo-EM structure	8F7C	Data File Jmol Viewer 8F7C	He et al. (2023). He Z, Zhao Y, Rau MJ, Fitzpatrick JAJ, Sah R, Hu H, & Yuan P (2023). Structural and functional analysis of human pannexin 2 channel. Nat Commun 14 1:1712. PubMed Id: 36973289. doi:10.1038/s41467-023-37413-z.
*Pannexin 3 (Panx3) ATP release channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.91 Å** cryo-EM structure	8GTR	Data File Jmol Viewer 8GTR	Hussain et al. (2024). Hussain N, Apotikar A, Pidathala S, Mukherjee S, Burada AP, Sikdar SK, Vinothkumar KR, & Penmatsa A (2024). Cryo-EM structures of pannexin 1 and 3 reveal differences among pannexin isoforms. Nat Commun 15 1:2942. PubMed Id: 38580658. doi:10.1038/s41467-024-47142-6.
*TMEM206 proton-activated chloride channel: Takifugu bimaculatus* E Eukaryota (expressed in Komagataella pastoris), 3.46 Å** cryo-EM structure	7JI3	Data File Jmol Viewer 7JI3	Deng et al. (2021). Deng Z, Zhao Y, Feng J, Zhang J, Zhao H, Rau MJ, Fitzpatrick JAJ, Hu H, & Yuan P (2021). Cryo-EM structure of a proton-activated chloride channel TMEM206. Sci Adv 7 9:eabe5983. PubMed Id: 33627432. doi:10.1126/sciadv.abe5983.
*sperm cation channel complex (CatSper) β, γ, δ, ε, ζ, and EFCAB9 complex: Mus musculus* E Eukaryota, 2.90 Å** cryo-EM structure	7EEB	Data File Jmol Viewer 7EEB	Lin et al. (2021). Lin S, Ke M, Zhang Y, Yan Z, & Wu J (2021). Structure of a mammalian sperm cation channel complex. Nature 595 7869:746-750. PubMed Id: 34225353. doi:10.1038/s41586-021-03742-6.
*insect olfactory receptor OR5,: Machilis hrabei* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure in complex with eugenol, 2.90 Å 7LID in complex with DEET, 2.90 Å 7LIG	7LIC	Data File Jmol Viewer 7LIC 7LID 7LIG	Del Mármol et al. (2021). Del Mármol J, Yedlin MA, & Ruta V (2021). The structural basis of odorant recognition in insect olfactory receptors. Nature 597 7874:126-131. PubMed Id: 34349260. doi:10.1038/s41586-021-03794-8.
*glutamate receptor-like channel GLR3.4, full-length: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 3.57 Å** cryo-EM structure after ATD & micelle subtraction, 4.39 Å 7LZI x-ray structures: ligand-binding domain in complex with glutamate, 2.29 Å 7LZ0 ligand-binding domain in complex with serine, 1.51 Å 7LZ1 ligand-binding domain in complex with methionine, 1.50 Å 7LZ2	7LZH	Data File Jmol Viewer 7LZH 7LZ1 7LZ0 7LZI 7LZ2	Green et al. (2021). Green MN, Gangwar SP, Michard E, Simon AA, Portes MT, Barbosa-Caro J, Wudick MM, Lizzio MA, Klykov O, Yelshanskaya MV, Feijó JA, & Sobolevsky AI (2021). Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4. Mol Cell 81 15:3216-3226.e8. PubMed Id: 34161757. doi:10.1016/j.molcel.2021.05.025.
*GluA1 Glutamate receptor (AMPA-subtype) in complex with TARP-γ3, resting state: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 2.82 Å** cryo-EM structure transmembrane domain, 2.70 Å: 8C2I active state, 2.90 Å: 8C1P active state, transmembrane domain, 2.64 Å: 8C2H desensitized conformation 1, 3.39 Å: 8P3T desensitized conformation 2, 3.77 Å: 8P3U desensitized conformation 3, 3.53 Å: 8P3V desensitized conformation 4, 3.53 Å: 8P3W	8C1Q	Data File Jmol Viewer 8C1Q 8C1P 8P3U 8C2I 8P3W 8P3T 8C2H 8P3V	Zhang et al. (2023). Zhang D, Ivica J, Krieger JM, Ho H, Yamashita K, Stockwell I, Baradaran R, Cais O, & Greger IH (2023). Structural mobility tunes signalling of the GluA1 AMPA glutamate receptor. Nature 621 7980:877-882. PubMed Id: 37704721. doi:10.1038/s41586-023-06528-0.
Channels: Fluc Family These are F^--selective channels
*Fluc F^- ion channel homolog in complex with Bpe-S7 monobody: Bordetella pertussis* B Bacteria (expressed in E. coli), 3.60 Å** in complex with Bpe-L7 monobody, 2.17 Å: 5A41 in complex with Ec2-S9 monobody, 2.58 Å: 5A43	5A40	Data File Jmol Viewer 5A40 5A41 5A43	Stockbridge et al. (2015). Stockbridge RB, Kolmakova-Partensky L, Shane T, Koide A, Koide S, Miller C, & Newstead S (2015). Crystal structures of a double-barrelled fluoride ion channel. Nature 525 7570:548-551. PubMed Id: 26344196. doi:10.1038/nature14981.
*Fluc F^- ion channel homolog in complex with monobody S8: Bordetella pertussis* B Bacteria (expressed in E. coli), 2.8 Å**	6BQO	Data File Jmol Viewer 6BQO	McIlwain et al. (2018). McIlwain BC, Newstead S, & Stockbridge RB (2018). Cork-in-Bottle Occlusion of Fluoride Ion Channels by Crystallization Chaperones. Structure 26 4:635-639.e1. PubMed Id: 29526432. doi:10.1016/j.str.2018.02.004.
*Fluc F^- ion channel homolog in complex Ec2-S9 monobody F801 mutant: Escherichia coli* B Bacteria, 2.48 Å** F831 mutant, 2.69 Å: 5KOM	5KBN	Data File Jmol Viewer 5KBN 5KOM	Last et al. (2016). Last NB, Kolmakova-Partensky L, Shane T, & Miller C (2016). Mechanistic signs of double-barreled structure in a fluoride ion channel. Elife 5 :e18767. PubMed Id: 27449280. doi:10.7554/eLife.18767.
*Fluc F^- ion channel homolog in complex Ec2-S9 monobody, F80Y mutant: Escherichia coli* B Bacteria, 2.75 Å** F80M mutant, 2.65 Å: 6B2A F83M mutant, 2.6 Å: 6B2B T114S mutant, 3.01 Å: 6B2D	6B24	Data File Jmol Viewer 6B24 6B2A 6B2B 6B2D	Last et al. (2017). Last NB, Sun S, Pham MC, & Miller C (2017). Molecular determinants of permeation in a fluoride-specific ion channel. Elife 6 :e31259. PubMed Id: 28952925. doi:10.7554/eLife.31259.
*Fluc F^- ion channel homolog wild-type in complex with bromide: Escherichia coli* B Bacteria, 3.11 Å** S81A with bromide, 2.50 Å: 7KKA S81C with bromide, 2.90 Å: 7KKB S81T with bromide, 2.70 Å: 7KK8 S81A/T82A with bromide, 3.10 Å: 7KK9	7KKR	Data File Jmol Viewer 7KKR 7KKB 7KKA 7KK8 7KK9	McIlwain et al. (2021). McIlwain BC, Gundepudi R, Koff BB, & Stockbridge RB (2021). The fluoride permeation pathway and anion recognition in Fluc family fluoride channels. Elife 10 :e69482. PubMed Id: 34250906. doi:10.7554/eLife.69482.
Channels: Aquaporins and Glyceroporins
*AQP0 aquaporin water channel: Bos taurus (Bovine) lens* E Eukaryota, 2.24 Å**	1YMG	Data File Jmol Viewer 1YMG	Harries et al. (2004). Harries WE, Akhavan D, Miercke LJ, Khademi S, & Stroud RM (2004). The channel architecture of aquaporin 0 at a 2.2 Å resolution. Proc Natl Acad Sci U S A 101 :14045-14050. PubMed Id: 15377788.
*AQP0 aquaporin water channel from sheep lens.: Ovis aries* E Eukaryota, 3.0 Å** AQP0 reconstituted with dimyristoylphosphatidylcholine and organized as a membrane junction. Electron Diffraction. Resolution: 3 Å in membrane plane, 3.5 Å normal to membrane plane.	1SOR	Data File Jmol Viewer 1SOR	Gonen et al. (2004). Gonen T, Sliz P, Kistler J, Cheng Y, & Walz T (2004). Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature 429 :193-197. PubMed Id: 15141214.
*AQP0 aquaporin sheep lens junction: Ovis aries* E Eukaryota, 1.90 Å** Electron Diffraction Non-junctional form, 2.4 Å: 2B6P	2B6O	Data File Jmol Viewer 2B6O 2B6P	Gonen et al. (2005). Gonen T, Cheng Y, Sliz P, Hiroaki Y, Fujiyoshi Y, Harrison SC, & Walz T (2005). Lipid-protein interactions in double-layered two-dimensional AQP0 crystals. Nature 438 :633-638. PubMed Id: 16319884.
*AQP0 aquaporin sheep lens junction: Ovis aries* E Eukaryota, 2.5 Å** Electron Diffraction. AQP0 reconstituted with E. coli polar lipids and organized as a membrane junction	3M9I	Data File Jmol Viewer 3M9I	Hite et al. (2010). Hite RK, Li Z, & Walz T. (2010). Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals. EMBO J 29 :1652-1658. PubMed Id: 20389283.
*AQP1 red blood cell aquaporin water channel: Homo sapiens* E Eukaryota, 3.8 Å** Electron Diffraction. Resolution shown is in-plane.	1FQY	Data File Jmol Viewer 1FQY aquaporin 1	Murata et al. (2000). Murata K, Mitsuoka K, Hirai T, Walz T, Agre P, Heymann J B, Engel A, & Fujiyoshi Y (2000). Structural determinants of water permeation through aquaporin-1. Nature 407 :599-605. PubMed Id: 11034202.
*AQP1 red blood cell aquaporin water channel: Homo sapiens* E Eukaryota, 3.7 Å** Electron Diffraction. Protein in vitreous ice.	1IH5	Data File Jmol Viewer 1IH5	Ren et al. (2001). Ren G, Reddy VS, Cheng A, Melnyk P, & Mitra AK (2001). Visualization of a water-selective pore by electron crystallography in vitreous ice. Proc Natl Acad Sci USA 98 :1398-1403. PubMed Id: 11171962.
*AQP1 red blood cell aquaporin water channel: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.28 Å**	4CSK	Data File Jmol Viewer 4CSK	Ruiz Carrillo et al. (2014). Ruiz Carrillo D, To Yiu Ying J, Darwis D, Soon CH, Cornvik T, Torres J, & Lescar J (2014). Crystallization and preliminary crystallographic analysis of human aquaporin 1 at a resolution of 3.28 Å. Acta Crystallogr F Struct Biol Commun 70 :1657-1663. PubMed Id: 25484221. doi:10.1107/S2053230X14024558.
*AQP1 red blood cell aquaporin water channel: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), NMR structure** Solid-state NMR structure under nearly physiological conditions	6POJ	Data File Jmol Viewer 6POJ	Dingwell et al. (2019). Dingwell DA, Brown LS, & Ladizhansky V (2019). Structure of the Functionally Important Extracellular Loop C of Human Aquaporin 1 Obtained by Solid-State NMR under Nearly Physiological Conditions. J Phys Chem B 123 36:7700-7710. PubMed Id: 31411472. doi:10.1021/acs.jpcb.9b06430.
*AQP1 aquaporin red blood cell water channel: Bos taurus* E Eukaryota, 2.20 Å** X-ray Diffraction	1J4N	Data File Jmol Viewer 1J4N aquaporin 1	Sui et al. (2001). Sui H, Han BG, Lee JK, Walian P, & Jap BK (2001). Structural basis of water-specific transport through the AQP1 water channel. Nature 414 :872-8. PubMed Id: 11780053.
*AQP1aa aquaporin water channel, with unique conformation of loop C: Anabas testudineus* E Eukaryota (expressed in Komagataella pastoris), 1.90 Å** 3.46 Å: 7W7R	7W7S	Data File Jmol Viewer 7W7S 7W7R	Zeng et al. (2022). Zeng J, Schmitz F, Isaksson S, Glas J, Arbab O, Andersson M, Sundell K, Eriksson LA, Swaminathan K, Törnroth-Horsefield S, & Hedfalk K (2022). High-resolution structure of a fish aquaporin reveals a novel extracellular fold. Life Sci Alliance 5 12:e202201491. PubMed Id: 36229063. doi:10.26508/lsa.202201491.
*AQP2 Aquaporin from kidney: Homo sapiens* E Eukaryota (expressed in Pichia pastoris), 2.75 Å**	4NEF	Data File Jmol Viewer 4NEF	Frick et al. (2014). Frick A, Eriksson UK, de Mattia F, Oberg F, Hedfalk K, Neutze R, de Grip WJ, Deen PM, & Törnroth-Horsefield S (2014). X-ray structure of human aquaporin 2 and its implications for nephrogenic diabetes insipidus and trafficking. Proc Natl Acad Sci USA 111 :6305-6310. PubMed Id: 24733887. doi:10.1073/pnas.1321406111.
*AQP2 Aquaporin from kidney crystallized on a silicon chip: Homo sapiens* E Eukaryota (expressed in Komagataella phaffii), 3.7 Å**	6QF5	Data File Jmol Viewer 6QF5	Lieske et al. (2019). Lieske J, Cerv M, Kreida S, Komadina D, Fischer J, Barthelmess M, Fischer P, Pakendorf T, Yefanov O, Mariani V, Seine T, Ross BH, Crosas E, Lorbeer O, Burkhardt A, Lane TJ, Guenther S, Bergtholdt J, Schoen S, Törnroth-Horsefield S, Chapman HN, & Meents A (2019). On-chip crystallization for serial crystallography experiments and on-chip ligand-binding studies. IUCrJ 6 :714-728. PubMed Id: 31316815. doi:10.1107/S2052252519007395.
*AQP2 Aquaporin, T125M mutant: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 3.90 Å** T126M mutant, 3.15 Å: 8OEE	8GHJ	Data File Jmol Viewer 8GHJ 8OEE	Hagströmer et al. (2023). Hagströmer CJ, Hyld Steffen J, Kreida S, Al-Jubair T, Frick A, Gourdon P, & Törnroth-Horsefield S (2023). Structural and functional analysis of aquaporin-2 mutants involved in nephrogenic diabetes insipidus. Sci Rep 13 1:14674. PubMed Id: 37674034. doi:10.1038/s41598-023-41616-1.
*AQP4 aquaporin rat glial cell water channel: Rattus norvegicus* E Eukaryota (expressed in S. frugiperda), 3.2 Å** Electron Diffraction.	2D57	Data File Jmol Viewer 2D57	Hiroaki et al. (2005). Hiroaki Y, Tani K, Kamegawa A, Gyobu N, Nishikawa K, Suzuki H, Walz T, Sasaki S, Mitsuoka K, Kimura K, Mizoguchi A, & Fujiyoshi Y (2005). Implications of the Aquaporin-4 Structure on Array Formation and Cell Adhesion. J Mol Biol 355 :628-639. PubMed Id: 16325200.
*AQP4 aquaporin rat glial cell water channel: Rattus norvegicus* E Eukaryota (expressed in S. frugiperda), 2.80 Å** Electron Diffraction. S180D mutant. Structure reveals five lipids associated with AQP4.	2ZZ9	Data File Jmol Viewer 2ZZ9	Tani et al. (2009). Tani K, Mitsuma T, Hiroaki Y, Kamegawa A, Nishikawa K, Tanimura Y, & Fujiyoshi Y (2009). Mechanism of aquaporin-4's fast and highly selective water conduction and proton exclusion. J Mol Biol 389 :694-706. PubMed Id: 19406128.
*AQP4 aquaporin water channel: Homo sapiens* E Eukaryota (expressed in Pichia pastoris), 1.8 Å**	3GD8	Data File Jmol Viewer 3GD8	Ho et al. (2009). Ho JD, Yeh R, Sandstrom A, Chorny I, Harries WE, Robbins RA, Miercke LJ, & Stroud RM (2009). Crystal structure of human aquaporin 4 at 1.8 A and its mechanism of conductance. Proc Natl Acad Sci USA 106 :7437-74422. PubMed Id: 19383790.
*AQP5 aquaporin water channel (HsAQP5): Homo sapiens* E Eukaryota (expressed in Pichia pastoris), 2.0 Å**	3D9S	Data File Jmol Viewer 3D9S	Horsefield et al. (2008). Horsefield R, Nordén K, Fellert M, Backmark A, Törnroth-Horsefield S, Terwisscha van Scheltinga AC, Kvassman J, Kjellbom P, Johanson U, & Neutze R. (2008). High-resolution x-ray structure of human aquaporin 5. Proc Natl Acad Sci USA 105 :13327-13332. PubMed Id: 18768791.
*AQP7 aquaporin glycerol channel: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 1.9 Å** structure at 2.2 Å: 6QZJ	6QZI	Data File Jmol Viewer 6QZI 6QZJ	de Maré et al. (2020). de Maré SW, Venskutonyté R, Eltschkner S, de Groot BL, & Lindkvist-Petersson K (2020). Structural Basis for Glycerol Efflux and Selectivity of Human Aquaporin 7. Structure 28 2:215-222.e3. PubMed Id: 31831212. doi:10.1016/j.str.2019.11.011.
*AQP7 aquaporin glycerol channel, dimer of tetramers, D4 symmetry: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 2.55 Å** cryo-EM structure C1 symmetry, 3.00 Å: 8AMW	8AMX	Data File Jmol Viewer 8AMX 8AMW	Huang et al. (2023). Huang P, Venskutonytė R, Prasad RB, Ardalani H, de Maré SW, Fan X, Li P, Spégel P, Yan N, Gourdon P, Artner I, & Lindkvist-Petersson K (2023). Cryo-EM structure supports a role of AQP7 as a junction protein. Nat Commun 14 1:600. PubMed Id: 36737436. doi:10.1038/s41467-023-36272-y.
*AQP10 aquaglyceroporin: Homo sapiens* E Eukaryota (expressed in S. cerevisiae), 2.30 Å**	6F7H	Data File Jmol Viewer 6F7H	Gotfryd et al. (2018). Gotfryd K, Mósca AF, Missel JW, Truelsen SF, Wang K, Spulber M, Krabbe S, Hélix-Nielsen C, Laforenza U, Soveral G, Pedersen PA, & Gourdon P (2018). Human adipose glycerol flux is regulated by a pH gate in AQP10. Nat Commun 9 1. PubMed Id: 30420639. doi:10.1038/s41467-018-07176-z.
*AqpM aquaporin water channel: Methanothermobacter marburgensis* A Archaea (expressed in E. coli), 1.68 Å** Initial structure, 2.3 Å: 2EVU	2F2B	Data File Jmol Viewer 2F2B 2EVU	Lee et al. (2005). Lee JK, Kozono D, Remis J, Kitagawa Y, Agre P, & Stroud RM (2005). Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 Å. Proc Natl Acad Sci USA 102 :18932-18937. PubMed Id: 16361443.
*AqpZ aquaporin water channel: Escherichia coli* B Bacteria, 2.5 Å**	1RC2	Data File Jmol Viewer 1RC2 aquaporin Z	Savage et al. (2003). Savage DF, Egea PF, Robles-Colmenares Y, Iii JD, & Stroud RM (2003). Architecture and Selectivity in Aquaporins: 2.5 Å X-Ray Structure of Aquaporin Z. PLoS Biol 1 :334-340. PubMed Id: 14691544.
*AqpZ aquaporin showing two conformations of Arg-189: Escherichia coli* B Bacteria, 3.2 Å**	2ABM	Data File Jmol Viewer 2ABM	Jiang et al. (2006). Jiang J, Daniels BV, & Fu D (2006). Crystal structure of AqpZ tetramer reveals two distinct R189 conformations associated with water permeation through the narrowest constriction of the water-conducting channel. J Biol Chem 281 :454-460. PubMed Id: 16239219.
*AqpZ aquaporin (C9S/C20S), T183C mutant without Hg: Escherichia coli* B Bacteria, 2.30 Å** T183C with Hg, 2.20 Å: 2O9E. L170C without Hg, 2.55 Å: 2O9F. L170C with Hg, 1.90 Å: 2O9G.	2O9D	Data File Jmol Viewer 2O9D 2O9E 2O9G 2O9F	Savage & Stroud (2007). Savage DF & Stroud RM (2007). Structural basis of aquaporin inhibition by mercury. J Mol Biol 368 :607-617. PubMed Id: 17376483.
*AqpZ aquaporin mutant F43W: Escherichia coli* B Bacteria, 2.40 Å** H174G/T183F mutant, 2.50 Å: 3NKA. F43W/H174G/T183F mutant, 3.10 Å: 3NKC.	3NK5	Data File Jmol Viewer 3NK5 3NKA 3NKC	Savage et al. (2010). Savage DF, O'Connell JD 3rd, Miercke LJ, Finer-Moore J, & Stroud RM (2010). Structural context shapes the aquaporin selectivity filter. Proc Natl Acad Sci USA 107 :17164-17169. PubMed Id: 20855585.
*PIP2;1 plant aquaporin (closed conformation): Spinacia oleracea* E Eukaryota (expressed in Pichia pastoris), 2.10 Å** Open conformation, 3.90 Å: 2B5F	1Z98	Data File Jmol Viewer 1Z98 2B5F	Törnroth-Horsefield et al. (2006). Törnroth-Horsefield S, Wang Y, Hedfalk K, Johanson U, Karlsson M, Tajkhorshid E, Neutze R, & Kjellbom P (2006). Structural mechanism of plant aquaporin gating. Nature 439 :688-694. PubMed Id: 16340961.
*PIP2;1 plant aquaporin, S115E mutant: Spinacia oleracea* E Eukaryota (expressed in Pichia pastoris), 2.30 Å** S115E:S274E mutant, 2.05 Å: 3CN5 S274E mutant, 2.95 Å: 3CN6	3CLL	Data File Jmol Viewer 3CLL 3CN5 3CN6	Nyblom et al. (2009). Nyblom M, Frick A, Wang Y, Ekvall M, Hallgren K, Hedfalk K, Neutze R, Tajkhorshid E, & Törnroth-Horsefield S (2009). Structural and functional analysis of SoPIP2;1 mutants adds insight into plant aquaporin gating. J Mol Biol 387 :653-668. PubMed Id: 19302796. doi:10.1016/j.jmb.2009.01.065.
*PIP2;4 plant aquaporin: Arabidopsis thaliana* E Eukaryota (expressed in Komagataella pastoris), 3.7 Å** Structure provides insight into hydrogen peroxide (H₂O₂) transport by aquaporins.	6QIM	Data File Jmol Viewer 6QIM	Wang et al. (2019). Wang H, Schoebel S, Schmitz F, Dong H, & Hedfalk K (2019). Characterization of aquaporin-driven hydrogen peroxide transport. Biochim Biophys Acta Biomembr 1862 :183065. PubMed Id: 31521632. doi:10.1016/j.bbamem.2019.183065.
*TIP2;1 ammonia-permeable aquaporin: Arabidopsis thaliana* E Eukaryota (expressed in Komagataella pastoris), 1.18 Å**	5I32	Data File Jmol Viewer 5I32	Kirscht et al. (2016). Kirscht A, Kaptan SS, Bienert GP, Chaumont F, Nissen P, de Groot BL, Kjellbom P, Gourdon P, & Johanson U (2016). Crystal Structure of an Ammonia-Permeable Aquaporin. PLoS Biol 14 3. PubMed Id: 27028365. doi:10.1371/journal.pbio.1002411.
*GlpF glycerol facilitator channel: Escherichia coli* B Bacteria, 2.2 Å**	1FX8	Data File Jmol Viewer 1FX8 Glycerol Channel, GlpF	Fu et al. (2000). Fu D, Libson A, Miercke LJW, Weitzman C, Nollert P, Krucinski J, & Stroud RM (2000). Structure of a glycerol-conducting channel and the basis for its selectivity. Science 290 :481-486. PubMed Id: 11039922.
*GlpF glycerol facilitator channel, W84F/F200T-mutant: Escherichia coli* B Bacteria, 2.1 Å** GlpF with non-transported xylose replacing glycerol: (GlpF - G)_A, 2.7 Å: 1LDI GlpF with non-transported xylose replacing glycerol: (GlpF - G)_B, 2.8 Å: 1LDA	1LDF	Data File Jmol Viewer 1LDF 1LDI 1LDA	Tajkhorshid et al. (2002). Tajkhorshid E, Nollert P, Jensen MØ, Miercke LJ, O'Connell J, Stroud RM, & Schulten K (2002). Control of the selectivity of the aquaporin water channel family by global orientational tuning. Science 296 :525-530. PubMed Id: 11964478.
*AQP aquaglyceroporin: Plasmodium falciparum* E Eukaryota, 2.05 Å** Transports water and glycerol equally well.	3C02	Data File Jmol Viewer 3C02	Newby et al. (2008). Newby ZE, O'Connell J 3rd, Robles-Colmenares Y, Khademi S, Miercke LJ, & Stroud RM (2008). Crystal structure of the aquaglyceroporin PfAQP from the malarial parasite Plasmodium falciparum. Nature Struc Mol Biol 15 :619-625. PubMed Id: 18500352.
*Aqy1 yeast aquaporin (pH 3.5): Pischia pastoris* E Eukaryota, 1.15 Å** pH 8.0, 1.40 Å: 2W1P	2W2E	Data File Jmol Viewer 2W2E 2W1P	Fischer et al. (2009). Fischer G, Kosinska-Eriksson U, Aponte-Santamaría C, Palmgren M, Geijer C, Hedfalk K, Hohmann S, de Groot BL, Neutze R, & Lindkvist-Petersson K. (2009). Crystal structure of a yeast aquaporin at 1.15 Å reveals a novel gating mechanism. PLoS Bio 7 6:e1000130. PubMed Id: 19529756. doi:10.1371/journal.pbio.1000130.
*Aqy1 yeast aquaporin (pH 8.0): Pischia pastoris* E Eukaryota, 0.88 Å**	3ZOJ	Data File Jmol Viewer 3ZOJ	Kosinska Eriksson et al. (2013). Kosinska Eriksson U, Fischer G, Friemann R, Enkavi G, Tajkhorshid E, & Neutze R (2013). Subangstrom resolution X-ray structure details aquaporin-water interactions. Science 340 :1346-1349. PubMed Id: 23766328. doi:10.1126/science.1234306.
*NIP2;1 aquaporin (metalloid porin) silicon transporter.: Oryza sativa* E Eukaryota (expressed in Saccharomyces cerevisiae), 3.00 Å**	7NL4	Data File Jmol Viewer 7NL4	van den Berg et al. (2021). van den Berg B, Pedebos C, Bolla JR, Robinson CV, Baslé A, & Khalid S (2021). Structural Basis for Silicic Acid Uptake by Higher Plants. J Mol Biol 433 21:167226. PubMed Id: 34487790. doi:10.1016/j.jmb.2021.167226.
*Lsi1 aquaporin (metalloid porin) silicon transporter: Oryza sativa* E Eukaryota (expressed in Spodoptera frugiperda), 1.80 Å**	7CJS	Data File Jmol Viewer 7CJS	Saitoh et al. (2021). Saitoh Y, Mitani-Ueno N, Saito K, Matsuki K, Huang S, Yang L, Yamaji N, Ishikita H, Shen JR, Ma JF, & Suga M (2021). Structural basis for high selectivity of a rice silicon channel Lsi1. Nat Commun 12 1:6236. PubMed Id: 34716344. doi:10.1038/s41467-021-26535-x.
Channels : Formate/Nitrite Transporter (FNT) Family
*FocA, pentameric aquaporin-like formate transporter: Escherichia coli* B Bacteria, 2.20 Å** 3KCU structure is for P2₁2₁2₁ space group. P3₂ space group: 3KCV, 3.2 Å	3KCU	Data File Jmol Viewer 3KCU 3KCV	Wang et al. (2009). Wang Y, Huang Y, Wang J, Cheng C, Huang W, Lu P, Xu YN, Wang P, Yan N, & Shi Y (2009). Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel. Nature 462 :467-472. PubMed Id: 19940917.
*FocA formate transporter without formate: Vibrio cholerae* B Bacteria (expressed in E. coli), 2.10 Å** FocA with bound formate: 3KLZ, 2.50 Å	3KLY	Data File Jmol Viewer 3KLY 3KLZ	Waight et al. (2010). Waight AB, Love J, & Wang DN (2010). Structure and mechanism of a pentameric formate channel. Nat Struct Mol Biol 17 :31-37. PubMed Id: 20010838.
*FocA formate transporter at pH 4.0: Salmonella typhimurium* B Bacteria, 2.80 Å** Three different conformations are observed in the asymmetric unit: Open, Intermediate, & closed	3Q7K	Data File Jmol Viewer 3Q7K	Lü et al. (2011). Lü W, Du J, Wacker T, Gerbig-Smentek E, Andrade SL, & Einsle O (2011). pH-dependent gating in a FocA formate channel Science 332 :352-354. PubMed Id: 21493860. doi:10.1126/science.1199098.
*FNT3 Hydrosulphide Channel (HSC), pH 9.0: Clostridium difficile* B Bacteria (expressed in E. coli), 2.20 Å** pH 7.5, 3.20 Å: 3TDR pH 4.5, 2.99 Å: 3TDP K16S mutant, 2.30 Å: 3TE2 L82V mutant, 2.50 Å: 3TDX T84A mutant, 2.39 Å: 3TE1 K148E mutant, 2.09 Å: 3TE0 F194I mutant, 1.98 Å: 3TDS	3TDO	Data File Jmol Viewer 3TDO 3TDR 3TDP 3TDX 3TE1 3TE2 3TDS 3TE0	Czyzewski & Wang (2012). Czyzewski BK & Wang DN (2012). Identification and characterization of a bacterial hydrosulphide ion channel. Nature 483 :494-497. PubMed Id: 22407320. doi:10.1038/nature10881.
*Formate-nitrite transporter PfFNT: Plasmodium falciparum* E Eukaryota (expressed in HEK293 cells), 2.56 Å** cryo-EM structure PfFNT-inhibitor complex, 2.78 Å: 6VQR	6VQQ	Data File Jmol Viewer 6VQQ 6VQR	Lyu et al. (2021). Lyu M, Su CC, Kazura JW, & Yu EW (2021). Structural basis of transport and inhibition of the Plasmodium falciparum transporter PfFNT. EMBO Rep 22 3:e51628. PubMed Id: 33471955. doi:10.15252/embr.202051628.
Channels: Urea Transporters
*Urea transporter: Desulfovibrio vulgaris* B Bacteria (expressed in E. coli), 2.30 Å** Structure with bound dimethyl urea: 3K3G, 2.40 Å	3K3F	Data File Jmol Viewer 3K3F 3K3G	Levin et al. (2009). Levin EJ, Quick M, & Zhou MG (2009). Crystal structure of a bacterial homologue of the kidney urea transporter. Nature 462 :757-761. PubMed Id: 19865084.
*UT-B Urea Transporter: Bos taurus* E Eukaryota (expressed in S. frugiperda), 2.36 Å** First structure of a mammalian urea transporter. Bound to Selenourea, 2.50 Å: 4EZD	4EZC	Data File Jmol Viewer 4EZC 4EZD	Levin et al. (2012). Levin EJ, Cao Y, Enkavi G, Quick M, Pan Y, Tajkhorshid E, & Zhou M (2012). Structure and permeation mechanism of a mammalian urea transporter. Proc Natl Acad Sci USA 109 :11194-11199. PubMed Id: 22733730. doi:10.1073/pnas.1207362109.
*UreI proton-gated inner membrane urea channel: Helicobacter pylori* B Bacteria (expressed in E. coli), 3.26 Å** Formed from six protomers with a two-helix hairpin motif.	3UX4	Data File Jmol Viewer 3UX4	Strugatsky et al. (2013). Strugatsky D, McNulty R, Munson K, Chen CK, Soltis SM, Sachs G, & Luecke H (2013). Structure of the proton-gated urea channel from the gastric pathogen Helicobacter pylori. Nature 493 :255-258. PubMed Id: 23222544. doi:10.1038/nature11684.
Channels: Intercellular Channels found in sporulating bacteria that connect mother cell to forespore
*SpoIIQ-SpoIIIAH Complex: Bacillus subtilis* B Bacteria (expressed in E. coli), 2.26 Å** This is the protomer structure. Modeling studies suggest that the pore is formed from 12 protomers to form a channel with a diameter of 60 Å.	3TUF	Data File Jmol Viewer 3TUF	Levdikov et al. (2012). Levdikov VM, Blagova EV, McFeat A, Fogg MJ, Wilson KS, & Wilkinson AJ (2012). Structure of components of an intercellular channel complex in sporulating Bacillus subtilis. Proc Natl Acad Sci USA 109 :5441-5445. PubMed Id: 22431604. doi:10.1073/pnas.1120087109.
*SpoIIQ-SpoIIIAH Complex: Bacillus subtilis* B Bacteria (expressed in E. coli), 2.82 Å** The structure is of the protomer. Modeling studies suggest that the pore is formed from 15 or 18 protomers to form a channel with a diameter of 82 or 116 Å.	3UZ0	Data File Jmol Viewer 3UZ0	Meisner et al. (2012). Meisner J, Maehigashi T, André I, Dunham CM, & Moran CP Jr (2012). Structure of the basal components of a bacterial transporter. Proc Natl Acad Sci USA 109 :5446-5451. PubMed Id: 22431613. doi:10.1073/pnas.1120113109.
Channels: Amt/Mep/Rh proteins
*AmtB ammonia channel (mutant): Escherichia coli* B Bacteria, 1.40 Å** 1U7G is Protein + ammonia. Apoprotein, 2.0 Å: 1U77 Protein + methylammonia, 1.85 Å: 1U7C	1U7G	Data File Jmol Viewer 1U7G 1U7C 1U77 ammonia transporter AmtB	Khademi et al. (2004). Khademi S, O'Connell J 3rd, Remis J, Robles-Colmenares Y, Miercke LJ, & Stroud RM (2004). Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 Å. Science 305 :1587-1594. PubMed Id: 15361618.
*AmtB ammonia channel (wild-type): Escherichia coli* B Bacteria, 1.8 Å (P6₃ crystal form)** R3 crystal form: 1XQE, 2.1 Å resolution	1XQF	Data File Jmol Viewer 1XQF 1XQE	Zheng et al. (2004). Zheng L, Kostrewa D, Berneche S, Winkler FK, & Li XD (2004). The mechanism of ammonia transport based on the crystal structure of AmtB of Escherichia coli. Proc Natl Acad Sci U S A 101 :17090-17095. PubMed Id: 15563598.
*AmtB ammonia channel (wild-type): Escherichia coli* B Bacteria, 2.1 Å** Wild-type in the presence of ammonium with imidazole: 2NOP, 2.0 Å H168E mutant in the presence of ammonium: 2NOW, 2.2 Å H168A mutant in the presence of ammonium with imidazole: 2NPC, 2.1 Å H168F mutant in the presence of ammonium with imidazole: 2NPD, 2.1 Å H318A mutant in the absence of ammonium: 2NPE, 2.1 Å H318F mutant in the presence of ammonium: 2NPG, 2.0 Å H318F mutant in the presence of ammonium with imidazole: 2NPJ, 2.0 Å H168A/H318A mutant in the presence of ammonium with imidazole: 2NPK, 2.0 Å	2NMR	Data File Jmol Viewer 2NMR 2NPD 2NPJ 2NOP 2NPE 2NPK 2NOW 2NPC 2NPG	Javelle et al. (2006). Javelle A, Lupo D, Zheng L, Li XD, Winkler FK, & Merrick M (2006). An unusual twin-his arrangement in the pore of ammonia channels is essential for substrate conductance. J Biol Chem 281 :39492-39498. PubMed Id: 17040913.
*AmtB ammonia channel in complex with GlnK: Escherichia coli* B Bacteria, 2.5 Å**	2NUU	Data File Jmol Viewer 2NUU	Conroy et al. (2007). Conroy MJ, Durand A, Lupo D, Li X-D, Bullough PA, Winkler FK, & Merrick M (2007). The crystal structure of the Escherichia coli AmtB-GlnK complex reveals how GlnK regulates the ammonia channel. Proc Natl Acad Sci USA 104 :1213-1218. PubMed Id: 17220269.
*AmtB ammonia channel in complex with inhibitory GlnK: Escherichia coli* B Bacteria, 1.96 Å**	2NS1	Data File Jmol Viewer 2NS1	Gruswitz et al. (2007). Gruswitz F, O'Connell III J, & Stroud RM (2007). Inhibitory complex of the transmembrane ammonia channel, AmtB, and the cytosolic regulatory protein, GlnK, at 1.96 Å. Proc Natl Acad Sci USA 104 :42-47. PubMed Id: 17190799.
*AmtB ammonia channel in complex with phosphatidylglycerol: Escherichia coli* B Bacteria, 2.30 Å** Structure reveals distinct conformational changes that re-position AmtB residues to interact with the lipid bilayer.	4NH2	Data File Jmol Viewer 4NH2	Laganowsky et al. (2014). Laganowsky A, Reading E, Allison TM, Ulmschneider MB, Degiacomi MT, Baldwin AJ, & Robinson CV (2014). Membrane proteins bind lipids selectively to modulate their structure and function. Nature 510 :172-175. PubMed Id: 24899312. doi:10.1038/nature13419.
*AmtB ammonia channel with bound TopFluor cardiolipin: Escherichia coli* B Bacteria, 2.45 Å**	6B21	Data File Jmol Viewer 6B21	Patrick et al. (2018). Patrick JW, Boone CD, Liu W, Conover GM, Liu Y, Cong X, & Laganowsky A (2018). Allostery revealed within lipid binding events to membrane proteins. Proc Natl Acad Sci USA 115 12:2976-2981. PubMed Id: 29507234. doi:10.1073/pnas.1719813115.
*Amt-1 ammonium channel: Archaeoglobus fulgidus* A Archaea (expressed in E. coli), 1.72 Å** Native protein: 2B2F. Protein + 20 mM Ammonium Sulfate: 2B2H Protein + 80 mM Ammonium Sulfate: 2B2I Protein+xenon: 2B2J	2B2F	Data File Jmol Viewer 2B2F 2B2H 2B2I 2B2J	Andrade et al. (2005). Andrade SL, Dickmanns A, Ficner R, & Einsle O (2005). Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus. Proc Natl Acad Sci U S A 102 :14994-14999. PubMed Id: 16214888.
*Rh protein, possible ammonia or CO₂ channel: Nitrosomonas europaea* B Bacteria (expressed in Methylococcus capsulatus), 1.85 Å** CO₂ pressurized protein, 1.85 Å: 3B9Z	3B9Y	Data File Jmol Viewer 3B9Y 3B9Z	Li et al. (2007). Li X, Jayachandran S, Nguyen HH, & Chan MK (2007). Structure of the Nitrosomonas europaea Rh protein. Proc Natl Acad Sci U S A 104 :19279-19284. PubMed Id: 18040042.
*Rh protein, possible ammonia or CO₂ channel: Nitrosomonas europaea* B Bacteria (expressed in E. coli), 1.30 Å**	3B9W	Data File Jmol Viewer 3B9W	Lupo et al. (2007). Lupo D, Li XD, Durand A, Tomizaki T, Cherif-Zahar B, Matassi G, Merrick M, & Winkler FK (2007). The 1.3-Å resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH₃transport by Rhesus family proteins. Proc Natl Acad Sci U S A 104 :19303-19308. PubMed Id: 18032606.
*Human Rh C glycoprotein ammonia transporter: Homo sapiens* E Eukaryota (expressed in HEK293s cells), 2.10 Å**	3HD6	Data File Jmol Viewer 3HD6	Gruswitz et al. (2010). Gruswitz F, Chaudhary S, Ho JD, Schlessinger A, Pezeshki B, Ho CM, Sali A, Westhoff CM, & Stroud RM (2010). Function of human Rh based on structure of RhCG at 2.1 Å. Proc Natl Acad Sci USA 107 :9638-9643. PubMed Id: 20457942.
*Mep2 ammonium transceptor: Saccharomyces cerevisiae* E Eukaryota, 3.2 Å**	5AEX	Data File Jmol Viewer 5AEX	van den Berg et al. (2016). van den Berg B, Chembath A, Jefferies D, Basle A, Khalid S, & Rutherford JC (2016). Structural basis for Mep2 ammonium transceptor activation by phosphorylation. Nat Commun 7 :11337. PubMed Id: 27088325. doi:10.1038/ncomms11337.
*Mep2 ammonium transceptor (R3): Candida albicans* E Eukaryota (expressed in S. cerevisiae), 1.47 Å** P3, 1.64 Å: 5AF1 442Δ, 3.4 Å: 5AID R452D,S453D mutant, 2.4 Å: 5AH3 S453D mutant, 2.07 Å: 5FUF	5AEZ	Data File Jmol Viewer 5AEZ 5AH3 5AF1 5AID 5FUF	van den Berg et al. (2016). van den Berg B, Chembath A, Jefferies D, Basle A, Khalid S, & Rutherford JC (2016). Structural basis for Mep2 ammonium transceptor activation by phosphorylation. Nat Commun 7 :11337. PubMed Id: 27088325. doi:10.1038/ncomms11337.
*Ammonium sensor/transducer: Candidatus (Kuenenia stuttgartiensis)* B Bacteria (expressed in E. colli), 1.98 Å** Regarding Candidatus, see https://en.wikipedia.org/wiki/Candidatus	6EU6	Data File Jmol Viewer 6EU6	Pflüger et al. (2018). Pflüger T, Hernández CF, Lewe P, Frank F, Mertens H, Svergun D, Baumstark MW, Lunin VY, Jetten MSM, & Andrade SLA (2018). Signaling ammonium across membranes through an ammonium sensor histidine kinase. Nat Commun 9 1:164. PubMed Id: 29323112. doi:10.1038/s41467-017-02637-3.
Cys-Loop Receptor Family Cation-selective and Anion-selective Ligand-gated Channels Cation-selective include nicotinic acetylcholine and serotonin 5-HT₃ receptors. Anion-selective include γ-aminobutyric, glycine, and invertebrate glutamate-gated chloride channels (GluCl)
*Nicotinic Acetylcholine Receptor Pore (closed state): Torpedo marmorata* E Eukaryota, 4.0 Å** Electron Diffraction	1OED	Data File Jmol Viewer 1OED AChR pore alpha subunit AChR pore beta subunit AChR pore gamma subunit AChR pore delta subunit	Miyazawa et al. (2003). Miyazawa A, Fujiyoshi Y, & Unwin N (2003). Structure and gating mechanism of the acetylcholine receptor pore. Nature 423 :949-955. PubMed Id: 12827192.
*Nicotinic Acetylcholine Receptor, refined structure: Torpedo marmorata* E Eukaryota, 4.0 Å** Electron Diffraction	2BG9	Data File Jmol Viewer 2BG9	Unwin (2005). Unwin N. (2005). Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution. J Mol Biol 346 :967-989. PubMed Id: 15701510.
*Acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class): Torpedo marmorata* E Eukaryota, 6.2 Å** Open class, 6.5 Å: 4AQ9	4AQ5	Data File Jmol Viewer 4AQ5 4AQ9	Unwin & Fujiyoshi (2012). Unwin N & Fujiyoshi Y (2012). Gating movement of acetylcholine receptor caught by plunge-freezing. J Mol Biol 422 :617-634. PubMed Id: 22841691. doi:10.1016/j.jmb.2012.07.010.
*acetylcholine (ACh) receptor in complex with alpha-bungarotoxin in nanodiscs: Tetronarce californica* E Eukaryota, 2.69 Å**	6UWZ	Data File Jmol Viewer 6UWZ	Rahman et al. (2020). Rahman MM, Teng J, Worrell BT, Noviello CM, Lee M, Karlin A, Stowell MHB, & Hibbs RE (2020). Structure of the Native Muscle-type Nicotinic Receptor and Inhibition by Snake Venom Toxins. Neuron 106 6:952-962.e5. PubMed Id: 32275860. doi:10.1016/j.neuron.2020.03.012.
*acetylcholine (ACh) receptor, apo form: Tetronarce californica* E Eukaryota, 2.50 Å** cryo-EM structure with added cholesterol, 2.74 Å 7SMQ with carbachol (desensitized state), 2.77 Å 7SMR with d-tubocurarine, 3.18 Å 7SMS in complex with d-tubocurarine and carbachol, 2.56 Å 7SMT	7SMM	Data File Jmol Viewer 7SMM 7SMQ 7SMT 7SMR 7SMS	Rahman et al. (2022). Rahman MM, Basta T, Teng J, Lee M, Worrell BT, Stowell MHB, & Hibbs RE (2022). Structural mechanism of muscle nicotinic receptor desensitization and block by curare. Nat Struct Mol Biol 29 4:386-394. PubMed Id: 35301478. doi:10.1038/s41594-022-00737-3.
*Nicotinic acetylcholine (ACh) receptor, resting conformation: Tetronarce californica* E Eukaryota, 2.90 Å** cryo-EM structure with bound nicotine, 2.50 Å 7QL5 with bound carbamylcholine, 3.23 Å 7QL6	7QKO	Data File Jmol Viewer 7QKO 7QL5 7QL6	Zarkadas et al. (2022). Zarkadas E, Pebay-Peyroula E, Thompson MJ, Schoehn G, Uchański T, Steyaert J, Chipot C, Dehez F, Baenziger JE, & Nury H (2022). Conformational transitions and ligand-binding to a muscle-type nicotinic acetylcholine receptor. Neuron 110 8:1358-1370.e5. PubMed Id: 35139364. doi:10.1016/j.neuron.2022.01.013.
*acetylcholine (ACh) receptor in complex with alpha-neurotoxin in nanodiscs: Tetronarce californica* E Eukaryota, 3.15 Å** cryo-EM structure	7Z14	Data File Jmol Viewer 7Z14	Nys et al. (2022). Nys M, Zarkadas E, Brams M, Mehregan A, Kambara K, Kool J, Casewell NR, Bertrand D, Baenziger JE, Nury H, & Ulens C (2022). The molecular mechanism of snake short-chain α-neurotoxin binding to muscle-type nicotinic acetylcholine receptors. Nat Commun 13 1:4543. PubMed Id: 35927270. doi:10.1038/s41467-022-32174-7.
*Nicotinic acetylcholine (ACh) receptor in complex with rocuronium, resting-like state: Tetronarce californica* E Eukaryota, 2.90 Å** cryo-EM structure in complex with rocuronium, pore-blocked state, 2.90 Å: 8F2S in complex with etomidate, desensitized-like state, 2.79 Å: 8F6Y in complex with succinylcholine, desensitized-like state, 2.70 Å: 8F6Z	8ESK	Data File Jmol Viewer 8ESK 8F6Y 8F2S 8F6Z	Goswami et al. (2023). Goswami U, Rahman MM, Teng J, & Hibbs RE (2023). Structural interplay of anesthetics and paralytics on muscle nicotinic receptors. Nat Commun 14 1:3169. PubMed Id: 37264005. doi:10.1038/s41467-023-38827-5.
*Nicotinic Acetylcholine α4β2 Receptor: Homo sapiens* E Eukaryota (expressed in HEK293S), 3.94 Å**	5KXI	Data File Jmol Viewer 5KXI	Morales-Perez et al. (2016). Morales-Perez CL, Noviello CM, & Hibbs RE (2016). X-ray structure of the human α4β2 nicotinic receptor. Nature 538 :411-415. PubMed Id: 27698419. doi:10.1038/nature19785.
*Nicotinic Acetylcholine α4β2 Receptor, 2α3β stiochiometry: Homo sapiens* E Eukaryota (expressed in HEK cells), 3.7 Å** cryo-EM structure 3α2β stiochiometry, 3.9 Å: 6CNK	6CNJ	Data File Jmol Viewer 6CNJ 6CNK	Walsh et al. (2018). Walsh RM Jr, Roh SH, Gharpure A, Morales-Perez CL, Teng J, & Hibbs RE (2018). Structural principles of distinct assemblies of the human α4β2 nicotinic receptor. Nature 557 7704:261-265. PubMed Id: 29720657. doi:10.1038/s41586-018-0081-7.
*Nicotinic Acetylcholine α3β4 Receptor: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.34 Å** cryo-EM structure in complex with AT-1001, 3.87 Å: 6PV8	6PV7	Data File Jmol Viewer 6PV7 6PV8	Gharpure et al. (2019). Gharpure A, Teng J, Zhuang Y, Noviello CM, Walsh RM Jr, Cabuco R, Howard RJ, Zaveri NT, Lindahl E, & Hibbs RE (2019). Agonist Selectivity and Ion Permeation in the α3β4 Ganglionic Nicotinic Receptor. Neuron 104 3:501-511.e6. PubMed Id: 31488329. doi:10.1016/j.neuron.2019.07.030.
*Nicotinic Acetylcholine α4β2 Receptor with varenicline in complex with anti-BRIL synthetic antibody BAK5: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.87 Å** cryo-EM structure in complex with varenicline, 3.71 Å: 6UR8 structure of BRIL bound to an affinity matured synthetic antibody (x-ray), 1.87 Å: 6CBV	6USF	Data File Jmol Viewer 6USF 6CBV 6UR8	Mukherjee et al. (2020). Mukherjee S, Erramilli SK, Ammirati M, Alvarez FJD, Fennell KF, Purdy MD, Skrobek BM, Radziwon K, Coukos J, Kang Y, Dutka P, Gao X, Qiu X, Yeager M, Eric Xu H, Han S, & Kossiakoff AA (2020). Synthetic antibodies against BRIL as universal fiducial marks for single-particle cryoEM structure determination of membrane proteins. Nat Commun 11 1. PubMed Id: 32221310. doi:10.1038/s41467-020-15363-0.
*Prokaryotic pentameric ligand-gated ion channel (ELIC): Erwinia chrysanthemi* B Bacteria (expressed in E. coli), 3.3 Å** First high-resolution x-ray structure of an AChR-like channel.	2VL0	Data File Jmol Viewer 2VL0	Hilf & Dutzler (2008). Hilf RJC & Dutzler R (2008). X-ray structure of a prokaryotic pentameric ligand-gated ion channel. Nature 452 :375-379. PubMed Id: 18322461.
*Prokaryotic pentameric ligand-gated ion channel (ELIC) in complex with acetylcholine: Erwinia chrysanthemi* B Bacteria (expressed in E. coli), 2.91 Å** Apo protein, 3.09 Å: 3RQU	3RQW	Data File Jmol Viewer 3RQW 3RQU	Pan et al. (2012). Pan J, Chen Q, Willenbring D, Yoshida K, Tillman T, Kashlan OB, Cohen A, Kong XP, Xu Y, & Tang P (2012). Structure of the pentameric ligand-gated ion channel ELIC cocrystallized with its competitive antagonist acetylcholine. Nature Commun 3 :714. PubMed Id: 22395605. doi:10.1038/ncomms1703.
*Prokaryotic pentameric ligand-gated ion channel (ELIC) in complex with bromoform: Erwinia chrysanthemi* B Bacteria (expressed in E. coli), 3.65 Å**	3ZKR	Data File Jmol Viewer 3ZKR	Spurny et al. (2013). Spurny R, Billen B, Howard RJ, Brams M, Debaveye S, Price KL, Weston DA, Strelkov SV, Tytgat J, Bertrand S, Bertrand D, Lummis SC, & Ulens C (2013). Multi-Site Binding Of A General Anesthetic To The Prokaryotic Pentameric Ligand-Gated Ion Channel ELIC. J Biol Chem 288 :8355-8364. PubMed Id: 23364792. doi:10.1074/jbc.M112.424507.
*Prokaryotic pentameric ligand-gated ion channel (ELIC) in complex with Br-memantine: Dickeya chrysanthemi* B Bacteria (expressed in E. coli), 3.20 Å** note: species formerly Erwinia chrysanthemi, now renamed as Dickeya dadantii, although the PDB designates it as Dickeya chrysanthemi. complexed with memantine, 3.90 Å: 4TWF apo form, 3.60 Å: 4TWH	4TWD	Data File Jmol Viewer 4TWD 4TWF 4TWH	Ulens et al. (2014). Ulens C, Spurny R, Thompson AJ, Alqazzaz M, Debaveye S, Han L, Price K, Villalgordo JM, Tresadern G, Lynch JW, & Lummis SC (2014). The Prokaryote Ligand-Gated Ion Channel ELIC Captured in a Pore Blocker-Bound Conformation by the Alzheimer's Disease Drug Memantine. Structure 22 :1399-1407. PubMed Id: 25199693. doi:10.1016/j.str.2014.07.013.
*Prokaryotic pentameric ligand-gated ion channel, 7'C pore mutant (L238C): Dickeya chrysanthemi* B Bacteria (expressed in E. coli), 2.5 Å** Delta8 truncation mutant, 2.78 Å: 6HJY F16'S pore mutant (F247S) with alternate M4 conformation, 3.45 Å: 6HK0	6HJX	Data File Jmol Viewer 6HJX 6HJY 6HK0	Hénault et al. (2019). Hénault CM, Govaerts C, Spurny R, Brams M, Estrada-Mondragon A, Lynch J, Bertrand D, Pardon E, Evans GL, Woods K, Elberson BW, Cuello LG, Brannigan G, Nury H, Steyaert J, Baenziger JE, & Ulens C (2019). A lipid site shapes the agonist response of a pentameric ligand-gated ion channel. Nat Chem Biol 15 12:1156-1164. PubMed Id: 31591563. doi:10.1038/s41589-019-0369-4.
*Prokaryotic pentameric ligand-gated ion channel (ELIC) in POPC-only nanodiscs: Dickeya dadantii* B Bacteria (expressed in E. coli), 4.1 Å** cryo-EM structure ELIC-propylammonium complex, 3.3 Å: 6V03 NOTE: Dickeya dadantii was formerly known as Erwinia chrysanthemi.	6V0B	Data File Jmol Viewer 6V0B 6V03	Kumar et al. (2020). Kumar P, Wang Y, Zhang Z, Zhao Z, Cymes GD, Tajkhorshid E, & Grosman C (2020). Cryo-EM structures of a lipid-sensitive pentameric ligand-gated ion channel embedded in a phosphatidylcholine-only bilayer. Proc Natl Acad Sci USA 117 3:1788-1798. PubMed Id: 31911476. doi:10.1073/pnas.1906823117.
*Prokaryotic pentameric ligand-gated ion channel (ELIC) with PAM nanobody: Dickeya chrysanthemi* B Bacteria (expressed in E. coli), 2.59 Å** in complex with NAM nanobody, 3.25 Å: 6SSP	6SSI	Data File Jmol Viewer 6SSI 6SSP	Brams et al. (2020). Brams M, Govaerts C, Kambara K, Price KL, Spurny R, Gharpure A, Pardon E, Evans GL, Bertrand D, Lummis SC, Hibbs RE, Steyaert J, & Ulens C (2020). Modulation of the Erwinia ligand-gated ion channel (ELIC) and the 5-HT3 receptor via a common vestibule site. Elife 9 :e51511. PubMed Id: 31990273. doi:10.7554/eLife.51511.
*Prokaryotic pentameric ligand-gated ion channel (GLIC): Gloeobacter violaceus* B Bacteria (expressed in E. coli), 3.1 Å** Related to ELIC (above), this pentameric channel is apparently in an open state. E221A mutant, 3.50 Å: 3EI0	3EHZ	Data File Jmol Viewer 3EHZ 3EI0	Hilf & Dutzler (2009). Hilf RJC & Dutzler R (2009). Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel. Nature 457 :115-118. PubMed Id: 18987630.
*Prokaryotic pentameric ligand-gated ion channel (GLIC): Gloeobacter violaceus* B Bacteria (expressed in E. coli), 2.9 Å** Related to ELIC (above), this pentameric channel is apparently in an open state.	3EAM	Data File Jmol Viewer 3EAM	Bocquet et al. (2009). Bocquet N, Nury H, Baaden M, Le Poupon C, Changeux JP, Delarue M, & Corringer PJ (2009). X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation. Nature 457 :111-114. PubMed Id: 18987633.
*Prokaryotic pentameric ligand-gated ion channel (GLIC), wildtype-TBSb complex: Gloeobacter violaceus* B Bacteria (expressed in E. coli), 3.70 Å** Wildtype-TEAs complex, 3.50 Å: 2XQ5 E221D-TEAs complex, 3.20 Å: 2XQ9 Wildtype-TMAs complex, 3.60 Å: 2XQ4 Wildtype-bromo-lidocaine complex, 3.50 Å: 2XQ3 Wildtype-Cd²⁺ complex, 3.40 Å: 2XQ7 Wildtype-Zn²⁺ complex, 3.60 Å: 2XQ8 Wildtype-Cs⁺ complex, 3.70 Å: 2XQ6	2XQA	Data File Jmol Viewer 2XQA 2XQ6 2XQ3 2XQ9 2XQ7 2XQ5 2XQ8 2XQ4	Hilf et al. (2010). Hilf RJ, Bertozzi C, Zimmermann I, Reiter A, Trauner D, & Dutzler R (2010). Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel. Nat Struct Mol Biol 17 :1330-1336. PubMed Id: 21037567.
*Prokaryotic pentameric ligand-gated ion channel (GLIC): Gloeobacter violaceus* B Bacteria (expressed in E. coli), 2.40 Å** Channel is in the open state. Selenium-derived DDM, 3.30 Å: 4IL4 With sulfates, 3.00 Å: 4ILC A237F mutant + CsCl, 3.50 Å: 4ILA A237F mutant + NaBr, 2.83 Å: 4IL9 A237F mutant + RbCl, 3.15 Å: 4ILB	4HFI	Data File Jmol Viewer 4HFI 4ILA 4IL9 4ILC 4IL4 4ILB	Sauguet et al. (2013). Sauguet L, Poitevin F, Murail S, Van Renterghem C, Moraga-Cid G, Malherbe L, Thompson AW, Koehl P, Corringer PJ, Baaden M, & Delarue M. (2013). Structural basis for ion permeation mechanism in pentameric ligand-gated ion channels. EMBO J 32 :728-741. PubMed Id: 23403925. doi:10.1038/emboj.2013.17.
*Prokaryotic "pentameric" ligand-gated ion channel (GLIC) with hexameric quaternary structure: Gloeobacter violaceus* B Bacteria (expressed in E. coli), 2.3 Å**	3IGQ	Data File Jmol Viewer 3IGQ	Nury et al. (2010). Nury H, Bocquet N, Le Poupon C, Raynal B, Haouz A, Corringer PJ, & Delarue M (2010). Crystal structure of the extracellular domain of a bacterial ligand-gated ion channel. J Mol Biol 395 :1114-1127. PubMed Id: 19917292.
*Prokaryotic pentameric ligand-gated ion channel (GLIC) in complex with propofol anesthetic: Gloeobacter violaceus* B Bacteria (expressed in E. coli), 3.30 Å** In complex with desflurane, 3.20 Å: 3P4W	3P50	Data File Jmol Viewer 3P50 3P4W	Nury et al. (2011). Nury H, Van Renterghem C, Weng Y, Tran A, Baaden M, Dufresne V, Changeux JP, Sonner JM, Delarue M, & Corringer PJ (2011). X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channe. Nature 469 :428-431. PubMed Id: 21248852.
*Prokaryotic pentameric ligand-gated ion channel (GLIC) in complex with ketamine anesthetic: Gloeobacter violaceus* B Bacteria (expressed in E. coli), 2.99 Å**	4F8H	Data File Jmol Viewer 4F8H	Pan et al. (2012). Pan J, Chen Q, Willenbring D, Mowrey D, Kong XP, Cohen A, Divito CB, Xu Y, & Tang P (2012). Structure of the Pentameric Ligand-Gated Ion Channel GLIC Bound with Anesthetic Ketamine. Structure 20 :1463-1469. PubMed Id: 22958642. doi:10.1016/j.str.2012.08.009.
*Prokaryotic pentameric ligand-gated ion channel (GLIC), pH 4: Gloeobacter violaceus* B Bacteria (expressed in D. melanogaster), 3.35 Å** Neutral pH, 4.35 Å: 4NPQ	4NPP	Data File Jmol Viewer 4NPP 4NPQ	Sauguet et al. (2014). Sauguet L, Shahsavar A, Poitevin F, Huon C, Menny A, Nemecz A, Haouz A, Changeux JP, Corringer PJ, & Delarue M (2014). Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation. Proc Natl Acad Sci USA 111 3:966-971. PubMed Id: 24367074. doi:10.1073/pnas.1314997111.
*Prokaryotic pentameric ligand-gated ion channel (GLIC): Gloeobacter violaceus* B Bacteria (expressed in E. coli), 3.00 Å** complex with bromoacetate, 3.40 Å: 4QH1	4QH5	Data File Jmol Viewer 4QH5 4QH1	Fourati et al. (2015). Fourati Z, Sauguet L, & Delarue M (2015). Genuine open form of the pentameric ligand-gated ion channel GLIC. Acta Crystallogr D Biol Crystallogr 71 :454-460. PubMed Id: 25760595. doi:10.1107/S1399004714026698.
*Prokaryotic pentameric ligand-gated ion channel (GLIC), Bromoform bound, K33C-L246C mutant: Gloeobacter violaceus* B Bacteria (expressed in E. coli), 2.95 Å** K33C-N245C cross-linked mutant, bromoform bound, 3.15 Å: 5HCM	5HCJ	Data File Jmol Viewer 5HCJ 5HCM	Laurent et al. (2016). Laurent B, Murail S, Shahsavar A, Sauguet L, Delarue M, & Baaden M (2016). Sites of Anesthetic Inhibitory Action on a Cationic Ligand-Gated Ion Channel. Structure 24 :595-605. PubMed Id: 27021161. doi:10.1016/j.str.2016.02.014.
*Prokaryotic pentameric ligand-gated ion channel (GLIC) with bound thiopental: Gloeobacter violaceus* B Bacteria (expressed in E. coli), 3.5 Å** with bound brominated barbiturate, 3.3 Å: 5L4H with bound seleniated barbiturate, 3.3 Å: 5L47	5L4E	Data File Jmol Viewer 5L4E 5L47 5L4H	Fourati et al. (2017). Fourati Z, Ruza RR, Laverty D, Drège E, Delarue-Cochin S, Joseph D, Koehl P, Smart T, & Delarue M (2017). Barbiturates Bind in the GLIC Ion Channel Pore and Cause Inhibition by Stabilizing a Closed State. J Biol Chem 292 :1550-1558. PubMed Id: 27986812. doi:10.1074/jbc.M116.766964.
*Prokaryotic pentameric ligand-gated ion channel (GLIC) in complex with DHA: Gloeobacter violaceus* B Bacteria, 3.25 Å** DHA: docosahexaenoic acid	5J0Z	Data File Jmol Viewer 5J0Z	Basak et al. (2017). Basak S, Schmandt N, Gicheru Y, & Chakrapani S (2017). Crystal structure and dynamics of a lipid-induced potential desensitized-state of a pentameric ligand-gated channel. Elife 6 :e23886. PubMed Id: 28262093. doi:10.7554/eLife.23886.
*Prokaryotic pentameric ligand-gated ion channel (GLIC), open channel-stabilized mutant G-2'I + I9'A: Gloeobacter violaceus* B Bacteria (expressed in E. coli), 3.12 Å** open channel-stabilized mutant C27S + K33C + I9'A + N21'C, 3.36 Å: 5V6N	5V6O	Data File Jmol Viewer 5V6O 5V6N	Gonzalez-Gutierrez et al. (2017). Gonzalez-Gutierrez G, Wang Y, Cymes GD, Tajkhorshid E, & Grosman C (2017). Chasing the open-state structure of pentameric ligand-gated ion channels. J Gen Physiol 149 12:1119-1138. PubMed Id: 29089419. doi:10.1085/jgp.201711803.
*Prokaryotic pentameric ligand-gated ion channel (GLIC), H235Q apo mutant: Gloeobacter violaceus* B Bacteria (expressed in E. coli), 2.95 Å** H235Q mutant with propofol, 2.65 Å: 5MZR H235Q mutant with bromoform, 2.65 Å: 5MZT M205W mutant with propofol, 3.49 Å: 5MVN M205W mutant with bromoform, 2.8 Å: 5MZQ F14'A mutant with propofol, 3.1 Å: 5MUR F14'A -N15'A double mutant with propofol, 3.1 Å: 5MVM 2-22' locally-closed mutant with propofol, 3.19 Å: 5MUO	5NJY	Data File Jmol Viewer 5NJY 5MUO 5MVN 5MZR 5MZT 5MUR 5MZQ 5MVM	Fourati et al. (2018). Fourati Z, Howard RJ, Heusser SA, Hu H, Ruza RR, Sauguet L, Lindahl E, & Delarue M (2018). Structural Basis for a Bimodal Allosteric Mechanism of General Anesthetic Modulation in Pentameric Ligand-Gated Ion Channels. Cell Rep 23 4:993-1004. PubMed Id: 29694907. doi:10.1016/j.celrep.2018.03.108.
*Pentameric ligand-gated ion channel (GLIC), wild-type: Gloeobacter violaceus* B Bacteria (expressed in E. coli), 2.22 Å** Q193C mutant, 2.58 Å: 6HY5 Q193C mutant + MMTS, 3.5 Å: 6HYR Q193M mutant, 2.95 Å: 6HY9 Q193L mutant, 3.39 Å: 6HYA Y197F-P250C mutant, 3.0 Å: 6HYX Y119A mutant, 2.8 Å: 6HYV Y119F mutant, 2.8 Å: 6HYW K248C mutant, 3.05 Å: 6HYZ K248A mutant, 2.75 Å: 6HZ0 E243C mutant, 2.5 Å: 6HZ1 E243G mutant, 3.15 Å: 6HZ3 E243C-I201W mutant, 3.0 Å: 6I08	6HZW	Data File Jmol Viewer 6HZW 6HY5 6HZ0 6I08 6HY9 6HYR 6HYX 6HYA 6HYV 6HZ1 6HYZ 6HYW 6HZ3	Hu et al. (2018). Hu H, Ataka K, Menny A, Fourati Z, Sauguet L, Corringer PJ, Koehl P, Heberle J, & Delarue M (2018). Electrostatics, proton sensor, and networks governing the gating transition in GLIC, a proton-gated pentameric ion channel. Proc Natl Acad Sci USA 115 52:E12172-E12181. PubMed Id: 30541892. doi:10.1073/pnas.1813378116.
*Prokaryotic pentameric ligand-gated ion channel (GLIC), pH 7: Gloeobacter violaceus* B Bacteria (expressed in E. coli), 4.10 Å** cryo-EM structure at pH 5, 3.40 Å 6ZGJ at pH 3, 3.60 Å 6ZGK	6ZGD	Data File Jmol Viewer 6ZGD 6ZGK 6ZGJ	Rovšnik et al. (2021). Rovšnik U, Zhuang Y, Forsberg BO, Carroni M, Yvonnesdotter L, Howard RJ, & Lindahl E (2021). Dynamic closed states of a ligand-gated ion channel captured by cryo-EM and simulations. Life Sci Alliance 4 8:e202101011. PubMed Id: 34210687. doi:10.26508/lsa.202101011.
*Prokaryotic pentameric ligand-gated ion channel (ELIC) in POPC nanodisc: Dickeya dadantii* B Bacteria (expressed in E. coli), 3.14 Å** cryo-EM structure with cysteamine in POPC nanodisc, 3.14 Å: 8D64 apo in 2:1:1 POPC:POPE:POPG nanodisc, 3.47 Å: 8D65 with cysteamine in 2:1:1 POPC:POPE:POPG nanodisc, 3.14 Å: 8D66 with cysteamine in 2:1:1 POPC:POPE:POPG nanodisc, 3.30 Å: 8D67 with cysteamine in 2:1:1 POPC:POPE:POPG nanodisc in open conformation, 3.36 Å: 8VUW. Supersedes 8D68.	8D63	Data File Jmol Viewer 8D63 8D64 8D66 8D65 8VUW 8D67	Petroff et al. (2022). Petroff JT 2nd, Dietzen NM, Santiago-McRae E, Deng B, Washington MS, Chen LJ, Trent Moreland K, Deng Z, Rau M, Fitzpatrick JAJ, Yuan P, Joseph TT, Hénin J, Brannigan G, & Cheng WWL (2022). Open-channel structure of a pentameric ligand-gated ion channel reveals a mechanism of leaflet-specific phospholipid modulation. Nat Commun 13 1:7017. PubMed Id: 36385237. doi:10.1038/s41467-022-34813-5.
*Prokaryotic pentameric ligand-gated ion channel (pLGIC) with additional N-terminal domain, closed pore: Desulfofustis sp. PB-SRB1* B Bacteria (expressed in E. coli), 3.55 Å** open conformation, 3.83 Å: 6V4A DeCLIC N-terminal Domain 34-202, 1.75 Å:	6V4S	Data File Jmol Viewer 6V4S 6V4A	Hu et al. (2020). Hu H, Howard RJ, Bastolla U, Lindahl E, & Delarue M (2020). Structural basis for allosteric transitions of a multidomain pentameric ligand-gated ion channel. Proc Natl Acad Sci USA 117 24:13437-13446. PubMed Id: 32482881. doi:10.1073/pnas.1922701117.
*Prokaryotic pentameric ligand-gated ion channel (sTeLIC), wild-type: endo-symbiont of Tevnia jerichonana* B Bacteria (expressed in E. coli), 2.3 Å** crystallized with 4-bromo cinnamic acid, 3 Å: 6FLI in complex with Cs⁺, 4.2 Å: 6FVR in complex with Ba²⁺, 3.2 Å: 6FVS R86A mutant, 3.3 Å: 6FVQ	6FL9	Data File Jmol Viewer 6FL9 6FVQ 6FLI 6FVS 6FVR	Hu et al. (2018). Hu H, Nemecz Á Van Renterghem C, Fourati Z, Sauguet L, Corringer PJ, & Delarue M (2018). Crystal structures of a pentameric ion channel gated by alkaline pH show a widely open pore and identify a cavity for modulation. Proc Natl Acad Sci USA 115 17:E3959-E3968. PubMed Id: 29632192. doi:10.1073/pnas.1717700115.
*Human glycine receptor (hGlyR-α1) transmembrane domain monomer: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure** Pentameric open-channel structure (putative): 2M6I	2M6B	Data File Jmol Viewer 2M6B 2M6I	Mowrey et al. (2013). Mowrey DD, Cui T, Jia Y, Ma D, Makhov AM, Zhang P, Tang P, & Xu Y (2013). Open-Channel Structures of the Human Glycine Receptor ?1 Full-Length Transmembrane Domain. Structure 21 :1897-1904. PubMed Id: 23994010. doi:10.1016/j.str.2013.07.014.
*Human glycine receptor (hGlyR-α3) in complex with strychnine: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.04 Å**	5CFB	Data File Jmol Viewer 5CFB	Huang et al. (2015). Huang X, Chen H, Michelsen K, Schneider S, & Shaffer PL (2015). Crystal structure of human glycine receptor-α3 bound to antagonist strychnine. Nature 526 7572:277-280. PubMed Id: 26416729. doi:10.1038/nature14972.
*Human glycine receptor (hGlyR-α3) N38Q mutant in complex with AM-3607: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.61 Å** wildtype w. bound AM-3607, 3.25 Å: 5TIO	5TIN	Data File Jmol Viewer 5TIN 5TIO	Huang et al. (2017). Huang X, Shaffer PL, Ayube S, Bregman H, Chen H, Lehto SG, Luther JA, Matson DJ, McDonough SI, Michelsen K, Plant MH, Schneider S, Simard JR, Teffera Y, Yi S, Zhang M, DiMauro EF, & Gingras J (2017). Crystal structures of human glycine receptor α3 bound to a novel class of analgesic potentiators. Nat Struct Mol Biol 24 :108-113. PubMed Id: 27991902. doi:10.1038/nsmb.3329.
*Human glycine receptor (hGlyR-α3) in complex with Gly and ivermectin: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.85 Å** N38Q mutant with bound AM-3607, 3.1 Å: 5VDI	5VDH	Data File Jmol Viewer 5VDH 5VDI	Huang et al. (2017). Huang X, Chen H, & Shaffer PL (2017). Crystal Structures of Human GlyRα3 Bound to Ivermectin. Structure 25 :945-950.e2. PubMed Id: 28479061. doi:10.1016/j.str.2017.04.007.
*α1 GlyR Glycine receptor in complex with strychnine: Danio rerio* E Eukaryota (expressed in S. frugiperda), 3.9 Å** cryo-EM structure in complex with glycine, 3.9 Å: 3JAE in complex with glycine/invermectin, 3.8 Å: 3JAF	3JAD	Data File Jmol Viewer 3JAD 3JAE 3JAF	Du et al. (2015). Du J, Lü W, Wu S, Cheng Y, & Gouaux E (2015). Glycine receptor mechanism elucidated by electron cryo-microscopy. Nature 526 7572:224-229. PubMed Id: 26344198. doi:10.1038/nature14853.
*α1 GlyR Glycine receptor, full-length in nanodiscs. Apo/Resting conformation: Danio rerio* E Eukaryota (expressed in Spodoptera frugiperda), 3.33 Å** cryo-EM structure Gly-bound desensitized conformation, 3.55 Å: 6UBT Gly/PTX-bound open/blocked conformation, 3.50 Å: 6UD3 Gly/IVM-conformation (State-1), 3.14 Å: 6VM0 Gly/IVM-conformation (State-2), 3.34 Å: 6VM2 Gly/IVM-conformation (State-3), 3.07 Å: 6VM3	6UBS	Data File Jmol Viewer 6UBS 6VM2 6UD3 6VM3 6UBT 6VM0	Kumar et al. (2020). Kumar A, Basak S, Rao S, Gicheru Y, Mayer ML, Sansom MSP, & Chakrapani S (2020). Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs. Nat Commun 11 1:3752. PubMed Id: 32719334. doi:10.1038/s41467-020-17364-5.
*α1 GlyR Glycine receptor in nanodisc, desensitized with bound glycine: Danio rerio* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** cryo-EM structure with bound taurine, 3.00 Å: 6PLS closed state with bound taurine, 3.20 Å: 6PLT desensitized state with bound GABA, 3.30 Å: 6PLU closed state with bound GABA, 3.30 Å: 6PLV in SMA: with bound GABA, super-open state, 3.00 Å: 6PLW with bound GABA, desensitized state, 2.90 Å: 6PLX with bound GABA, open state, 2.90 Å: 6PLY with bound GABA, closed state, 3.00 Å: 6PLZ with bound taurine, super-open state, 3.10 Å: 6PM0 with bound taurine, desensitized state, 3.00 Å: 6PM1 with bound taurine, open state, 3.00 Å: 6PM2 with bound taurine, closed state, 3.00 Å: 6PM3 with bound glycine, super-open state, 4.00 Å: 6PM4 with bound glycine, desensitized state, 3.10 Å: 6PM5 YGF mutant with bound GABA, open state, 3.30 Å: 6PLO YGF mutant with bound GABA, desensitized state, 3.30 Å: 6PLP YGF mutant with bound GABA, super-open state, 3.40 Å: 6PLQ in micelle, apo state, 2.90 Å: 6PXD	6PLR	Data File Jmol Viewer 6PLR 6PLS 6PLT 6PLP 6PM4 6PXD 6PLX 6PM0 6PM3 6PLQ 6PLW 6PLY 6PLZ 6PM5 6PLV 6PLU 6PM1 6PM2 6PLO	Yu et al. (2021). Yu J, Zhu H, Lape R, Greiner T, Du J, Lü W, Sivilotti L, & Gouaux E (2021). Mechanism of gating and partial agonist action in the glycine receptor. Cell 184 4:957-968.e21. PubMed Id: 33567265. doi:10.1016/j.cell.2021.01.026.
*α1 GlyR Glycine receptor in presence of 32uM Tetrahydrocannabinol: Danio rerio* E Eukaryota (expressed in Spodoptera frugiperda), 3.09 Å** cryo-EM structure in presence of 0.1mM Glycine, 2.61 Å: 7M6N in presence of 0.1mM Glycine and 32uM Tetrahydrocannabinol, 2.84 Å: 7M6O in presence of 1mM Glycine and 32uM Tetrahydrocannabinol, State 1, 2.91 Å: 7M6Q in presence of 1mM Glycine, 3.28 Å: 7M6P in presence of 1mM Glycine and 32uM Tetrahydrocannabinol, State 3, 3.61 Å: 7M6S	7M6M	Data File Jmol Viewer 7M6M 7M6N 7M6O 7M6P 7M6S 7M6Q	Kumar et al. (2022). Kumar A, Kindig K, Rao S, Zaki AM, Basak S, Sansom MSP, Biggin PC, & Chakrapani S (2022). Structural basis for cannabinoid-induced potentiation of alpha1-glycine receptors in lipid nanodiscs. Nat Commun 13 1:4862. PubMed Id: 35982060. doi:10.1038/s41467-022-32594-5.
*α1β_Bheteromeric Glycine Receptor, strychnine-bound state: Danio rerio* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å** cryo-EM structure in glycine-bound state, 3.20 Å: 7TVI in 1 mM glycine 20 uM ivermectin state, 3.00 Å: 8FE1	7TU9	Data File Jmol Viewer 7TU9 8FE1 7TVI	Gibbs et al. (2023). Gibbs E, Klemm E, Seiferth D, Kumar A, Ilca SL, Biggin PC, & Chakrapani S (2023). Conformational transitions and allosteric modulation in a heteromeric glycine receptor. Nat Commun 14 1:1363. PubMed Id: 36914669. doi:10.1038/s41467-023-37106-7.
*GluClα anion-selective receptor (Fab-invermectin complex): Caenorhabditis elegans* E Eukaryota (expressed in S. frugiperda), 3.26 Å** With glutamate, 3.35 Å:3RIF With picrotoxin, 3.40 Å:3RI5 With iodide, 3.80 Å:3RIA	3RHW	Data File Jmol Viewer 3RHW 3RIA 3RIF 3RI5	Hibbs & Gouaux (2011). Hibbs RE & Gouaux E (2011). Principles of activation and permeation in an anion-selective Cys-loop receptor Nature 474 :54-60. PubMed Id: 21572436. doi:10.1038/nature10139.
*α7 neuronal ACh recptor TM domain: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure**	2MAW	Data File Jmol Viewer 2MAW	Bondarenko et al. (2014). Bondarenko V, Mowrey DD, Tillman TS, Seyoum E, Xu Y, & Tang P (2014). NMR structures of the human α7 nAChR transmembrane domain and associated anesthetic binding sites. Biochim. Biophys. Acta 1838 :1389-1395. PubMed Id: 24384062. doi:10.1016/j.bbamem.2013.12.018.
*α7 nicotinic acetylcholine receptor bound to alpha-bungarotoxin in closed resting state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure bound to epibatidine and PNU-120596 in the activated state, 2.70 Å: 7KOX bound to epibatidine in a desensitized state, 3.60 Å: 7KOQ	7KOO	Data File Jmol Viewer 7KOO 7KOQ 7KOX	Noviello et al. (2021). Noviello CM, Gharpure A, Mukhtasimova N, Cabuco R, Baxter L, Borek D, Sine SM, & Hibbs RE (2021). Structure and gating mechanism of the α7 nicotinic acetylcholine receptor. Cell 184 8:2121-2134.e13. PubMed Id: 33735609. doi:10.1016/j.cell.2021.02.049.
*α7 nicotinic acetylcholine receptor, apo form: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.18 Å** cryo-EM structure bound to EVP-6124, 2.85 Å: 7EKP bound to EVP-6124 and PNU-120596, 3.02 Å: 7EKT	7EKI	Data File Jmol Viewer 7EKI 7EKT 7EKP	Zhao et al. (2021). Zhao Y, Liu S, Zhou Y, Zhang M, Chen H, Eric Xu H, Sun D, Liu L, & Tian C (2021). Structural basis of human α7 nicotinic acetylcholine receptor activation. Cell Res . PubMed Id: 33958730. doi:10.1038/s41422-021-00509-6.
*α7 neuronal ACh receptor, intracellular domain with transmembrane domain: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure**	7RPM	Data File Jmol Viewer 7RPM	Bondarenko et al. (2022). Bondarenko V, Wells MM, Chen Q, Tillman TS, Singewald K, Lawless MJ, Caporoso J, Brandon N, Coleman JA, Saxena S, Lindahl E, Xu Y, & Tang P (2022). Structures of highly flexible intracellular domain of human α7 nicotinic acetylcholine receptor. Nat Commun 13 1:793. PubMed Id: 35145092. doi:10.1038/s41467-022-28400-x.
*GABA_A receptor (β3 homopentamer): Homo sapiens* E Eukaryota (expressed in HEK293F cells), 2.97 Å**	4COF	Data File Jmol Viewer 4COF	Miller et al. (2014). Miller PS, & Aricescu AR (2014). Crystal structure of a human GABA_A receptor. Nature 512 :270-275. PubMed Id: 24909990. doi:10.1038/nature13293.
*GABA_A receptor (α1β2γ2) in complex with GABA and flumazenil antagonist: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.92 Å** cryo-EM structure conformation B, 3.86 Å: 6D6T	6D6U	Data File Jmol Viewer 6D6U 6D6T	Zhu et al. (2018). Zhu S, Noviello CM, Teng J, Walsh RM Jr, Kim JJ, & Hibbs RE (2018). Structure of a human synaptic GABA_A receptor. Nature 559 7712:67-72. PubMed Id: 29950725. doi:10.1038/s41586-018-0255-3.
*GABA_A receptor (α1β2γ2) in complex with bicuculline methbromide: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.12 Å** cryo-EM structure in complex with GABA plus propofol, 2.55 Å: 6X3T in complex with GABA plus flumazenil, 3.50 Å: 6X3U in complex with GABA plus etomidate, 3.50 Å: 6X3V in complex with GABA plus phenobarbital, 3.30 Å: 6X3W in complex with GABA plus diazepam, 2.92 Å: 6X3X in complex with GABA, 3.23 Å: 6X3Z in complex with GABA plus picrotoxin, 2.86 Å: 6X40	6X3S	Data File Jmol Viewer 6X3S 6X40 6X3Z 6X3X 6X3V 6X3U 6X3W 6X3T	Kim et al. (2020). Kim JJ, Gharpure A, Teng J, Zhuang Y, Howard RJ, Zhu S, Noviello CM, Walsh RM Jr, Lindahl E, & Hibbs RE (2020). Shared structural mechanisms of general anaesthetics and benzodiazepines. Nature 585 7824:303-308. PubMed Id: 32879488. doi:10.1038/s41586-020-2654-5.
*GABA_A receptor (α1β2γ2) in complex with zolpidem: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure in complex with DMCM, 2.90 Å 8DD3	8DD2	Data File Jmol Viewer 8DD2 8DD3	Zhu et al. (2022). Zhu S, Sridhar A, Teng J, Howard RJ, Lindahl E, & Hibbs RE (2022). Structural and dynamic mechanisms of GABAA receptor modulators with opposing activities. Nat Commun 13 1:4582. PubMed Id: 35933426. doi:10.1038/s41467-022-32212-4.
*GABA_A receptor (α1β3γ2L) in nanodiscs: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.2 Å** cryo-EM structure	6I53	Data File Jmol Viewer 6I53	Laverty et al. (2019). Laverty D, Desai R, Uchański T, Masiulis S, Stec WJ, Malinauskas T, Zivanov J, Pardon E, Steyaert J, Miller KW, & Aricescu AR (2019). Cryo-EM structure of the human α1β3γ2L GABA_A receptor in a lipid bilayer. Nature 565 7740:516-520. PubMed Id: 30602789. doi:10.1038/s41586-018-0833-4.
*GABA_A receptor (α1β3γ2L) in complex with picrotoxin: Homo sapiens* E Eukaryota (expressed in HEK293S cells), 3.1 Å** cryo-EM structure of protein in nanodiscs in complex with picrotoxin & GABA, 3.04 Å: 6HUJ in complex with bicuculline, 3.69 Å: 6HUK in complex with alprazolam (Xanax) & GABA, 3.26 Å: 6HUO in complex with diazepam (Valium) & GABA, 3.58 Å: 6HUP	6HUG	Data File Jmol Viewer 6HUG 6HUP 6HUO 6HUJ 6HUK	Masiulis et al. (2019). Masiulis S, Desai R, Uchański T, Serna Martin I, Laverty D, Karia D, Malinauskas T, Zivanov J, Pardon E, Kotecha A, Steyaert J, Miller KW, & Aricescu AR (2019). GABA_A receptor signalling mechanisms revealed by structural pharmacology. Nature 565 7740:454-459. PubMed Id: 30602790. doi:10.1038/s41586-018-0832-5.
*GABA_A receptor (β3 homopentamer) in complex with histamine and megabody Mb25 in lipid nanodisc: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 1.70 Å** cryo-EM structure	7A5V	Data File Jmol Viewer 7A5V	Nakane et al. (2020). Nakane T, Kotecha A, Sente A, McMullan G, Masiulis S, Brown PMGE, Grigoras IT, Malinauskaite L, Malinauskas T, Miehling J, Uchański T, Yu L, Karia D, Pechnikova EV, de Jong E, Keizer J, Bischoff M, McCormack J, Tiemeijer P, Hardwick SW, Chirgadze DY, Murshudov G, Aricescu AR, & Scheres SHW (2020). Single-particle cryo-EM at atomic resolution. Nature 587 7832:152-156. PubMed Id: 33087931. doi:10.1038/s41586-020-2829-0.
*GABA_A receptor (β3 homopentamer) in complex with histamine and megabody Mb25: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.49 Å** cryo-EM structure x-ray structures: structure of Mb-cHopQ-Nb207, 2.84 Å 6QD6 structure of Megabody Mb-Nb207-c7HopQ_G10, 3.15 Å 6XV8 structure of Megabody Mb-Nb207-cYgjK_NO, 1.90 Å 6XUX	6QFA	Data File Jmol Viewer 6QFA 6XV8 6QD6 6XUX	Uchański et al. (2021). Uchański T, Masiulis S, Fischer B, Kalichuk V, López-Sánchez U, Zarkadas E, Weckener M, Sente A, Ward P, Wohlkönig A, Zögg T, Remaut H, Naismith JH, Nury H, Vranken W, Aricescu AR, Pardon E, & Steyaert J (2021). Megabodies expand the nanobody toolkit for protein structure determination by single-particle cryo-EM. Nat Methods 18 1:60-68. PubMed Id: 33408403. doi:10.1038/s41592-020-01001-6.
*GABA_A receptor (αββαβ) with bound α-Cobratoxin: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure + GABA + Zn²⁺, 2.79 Å 7PBZ + GABA, 3.04 Å 7PBD	7PC0	Data File Jmol Viewer 7PC0 7PBD 7PBZ	Kasaragod et al. (2022). Kasaragod VB, Mortensen M, Hardwick SW, Wahid AA, Dorovykh V, Chirgadze DY, Smart TG, & Miller PS (2022). Mechanisms of inhibition and activation of extrasynaptic αβ GABAA receptors. Nature 602 7897:529-533. PubMed Id: 35140402. doi:10.1038/s41586-022-04402-z.
*GABA_A receptor (α4β3δ), apo: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.50 Å** cryo-EM structure in complex with GABA and histamine, 3.00 Å 7QN7 in complex with GABA and histamine (pre-open/closed state), 2.90 Å 7QN9 in complex with THIP and histamine, 2.90 Å 7QNC β3δ apo, 2.90 Å 7QN6 β3δ in complex with histamine, 3.10 Å 7QN8 β3δ in complex with THIP and histamine, 3.40 Å 7QND α4β3γ2 in complex with GABA, 3.00 Å 7QNA β3γ2 in complex with GABA, 3.10 Å 7QNB α1β3γ2 in complex with Ro15-4513, 2.70 Å 7QNE	7QN5	Data File Jmol Viewer 7QN5 7QN6 7QNA 7QN8 7QND 7QNB 7QNE 7QN7 7QN9 7QNC	Sente et al. (2022). Sente A, Desai R, Naydenova K, Malinauskas T, Jounaidi Y, Miehling J, Zhou X, Masiulis S, Hardwick SW, Chirgadze DY, Miller KW, & Aricescu AR (2022). Differential assembly diversifies GABAA receptor structures and signalling. Nature 604 7904:190-194. PubMed Id: 35355020. doi:10.1038/s41586-022-04517-3.
*GABA_A receptor in complex with autoimmune antibody Fab175: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure in complex with autoimmune antibody Fab115, 3.00 Å: 7T0W	7T0Z	Data File Jmol Viewer 7T0Z 7T0W	Noviello et al. (2022). Noviello CM, Kreye J, Teng J, Prüss H, & Hibbs RE (2022). Structural mechanisms of GABAA receptor autoimmune encephalitis. Cell 185 14:2469-2477.e13. PubMed Id: 35803245. doi:10.1016/j.cell.2022.06.025.
*Benzodiazepine-sensitive α1β1γ2S tri-heteromeric GABA_A receptor: Rattus norvegicus* E Eukaryota (expressed in TSA201 cells), 3.8 Å** cryo-EM structure Structure is in complex with GABA extra cellular domain (ECD), 3.1 Å: 6DW1	6DW0	Data File Jmol Viewer 6DW0 6DW1	Phulera et al. (2018). Phulera S, Zhu H, Yu J, Claxton DP, Yoder N, Yoshioka C, & Gouaux E (2018). Cryo-EM structure of the benzodiazepine-sensitive α1β1γ2S tri-heteromeric GABA_A receptor in complex with GABA. Elife 7 :e39383. PubMed Id: 30044221. doi:10.7554/eLife.39383.
*Serotonin 5-HT_3A receptor: Mus musculus* E Eukaryota (expressed in HEK293F cells), 3.50 Å**	4PIR	Data File Jmol Viewer 4PIR	Hassaine et al. (2014). Hassaine G, Deluz C, Grasso L, Wyss R, Tol MB, Hovius R, Graff A, Stahlberg H, Tomizaki T, Desmyter A, Moreau C, Li XD, Poitevin F, Vogel H, & Nury H (2014). X-ray structure of the mouse serotonin 5-HT₃ receptor. Nature 512 :276-281. PubMed Id: 25119048. doi:10.1038/nature13552.
*Serotonin 5-HT_3A receptor: Mus musculus* E Eukaryota (expressed in S. frugiperda), 4.31 Å** cryo-EM structure	6BE1	Data File Jmol Viewer 6BE1	Basak et al. (2018). Basak S, Gicheru Y, Samanta A, Molugu SK, Huang W, Fuente M, Hughes T, Taylor DJ, Nieman MT, Moiseenkova-Bell V, & Chakrapani S (2018). Cryo-EM structure of 5-HT3A receptor in its resting conformation. Nat Commun 9 :514. PubMed Id: 29410406. doi:10.1038/s41467-018-02997-4.
*Serotonin 5-HT_3A receptor with bound serotonin, F conformation: Mus musculus* E Eukaryota (expressed in HEK293 cells), 4.1 Å** cryo-EM structure I1 conformation, 4.2 Å: 6HIO I2 conformation, 3.2 Å: 6HIQ with bound tropisetron, T conformation, 4.5 Å: 6HIS	6HIN	Data File Jmol Viewer 6HIN 6HIO 6HIS 6HIQ	Polovinkin et al. (2018). Polovinkin L, Hassaine G, Perot J, Neumann E, Jensen AA, Lefebvre SN, Corringer PJ, Neyton J, Chipot C, Dehez F, Schoehn G, & Nury H (2018). Conformational transitions of the serotonin 5-HT3 receptor. Nature 563 7730:275-279. PubMed Id: 30401839. doi:10.1038/s41586-018-0672-3.
*Serotonin 5-HT_3A receptor with bound serotonin, State 1: Mus musculus* E Eukaryota (expressed in sf9 cells), 3.32 Å** cryo-EM structure State 2, 3.89 Å: 6DG8	6DG7	Data File Jmol Viewer 6DG7 6DG8	Basak et al. (2018). Basak S, Gicheru Y, Rao S, Sansom MSP, & Chakrapani S (2018). Cryo-EM reveals two distinct serotonin-bound conformations of full-length 5-HT_3A receptor. Nature 563 7730:270-274. PubMed Id: 30401837. doi:10.1038/s41586-018-0660-7.
*Serotonin 5-HT_3A receptor with bound granisetron: mus musculus* E Eukaryota, 2.92 Å**	6NP0	Data File Jmol Viewer 6NP0	Basak et al. (2019). Basak S, Gicheru Y, Kapoor A, Mayer ML, Filizola M, & Chakrapani S (2019). Molecular mechanism of setron-mediated inhibition of full-length 5-HT_3A receptor. Nat Commun 10 1. PubMed Id: 31324772. doi:10.1038/s41467-019-11142-8.
*Serotonin 5-HT_3A receptor in complex with palonosetron: Mus musculus* E Eukaryota (expressed in HEK-293 cells), 2.82 Å** cryo-EM structure	6Y1Z	Data File Jmol Viewer 6Y1Z	Zarkadas et al. (2020). Zarkadas E, Zhang H, Cai W, Effantin G, Perot J, Neyton J, Chipot C, Schoehn G, Dehez F, & Nury H (2020). The Binding of Palonosetron and Other Antiemetic Drugs to the Serotonin 5-HT3 Receptor. Structure 28 10:1131-1140.e4. PubMed Id: 32726573. doi:10.1016/j.str.2020.07.004.
*Serotonin 5-HT_3A receptor in presence of Palonosetron: Mus musculus* E Eukaryota (expressed in Spodoptera frugiperda), 3.35 Å** cryo-EM structure in presence of Ondansetron, 3.06 Å: 6W1M in presence of Alosetron, 2.92 Å: 6W1J	6W1Y	Data File Jmol Viewer 6W1Y 6W1J 6W1M	Basak et al. (2020). Basak S, Kumar A, Ramsey S, Gibbs E, Kapoor A, Filizola M, & Chakrapani S (2020). High-resolution structures of multiple 5-HT_3AR-setron complexes reveal a novel mechanism of competitive inhibition. Elife 9 :e57870. PubMed Id: 33063666. doi:10.7554/eLife.57870.
*Serotonin 5-HT_3A receptor with bound serotonin in Salipro bilayer discs: Mus musculus* E Eukaryota (expressed in HEK293 cells), 2.80 Å** cryo-EM structure apo, C5 symmetric, 3.20 Å: 6Y59 apo, asymmetric, 3.10 Å: 6Y5B	6Y5A	Data File Jmol Viewer 6Y5A 6Y59 6Y5B	Zhang et al. (2021). Zhang Y, Dijkman PM, Zou R, Zandl-Lang M, Sanchez RM, Eckhardt-Strelau L, Köfeler H, Vogel H, Yuan S, & Kudryashev M (2021). Asymmetric opening of the homopentameric 5-HT3A serotonin receptor in lipid bilayers. Nat Commun 12 1:1074. PubMed Id: 33594077. doi:10.1038/s41467-021-21016-7.
*Octopus sensory receptor CRT1: Octopus bimaculoides* E Eukaryota (expressed in HEK293 cells), 2.62 Å** cryo-EM structure	8EIS	Data File Jmol Viewer 8EIS	Kang et al. (2023). Kang G, Allard CAH, Valencia-Montoya WA, van Giesen L, Kim JJ, Kilian PB, Bai X, Bellono NW, & Hibbs RE (2023). Sensory specializations drive octopus and squid behaviour. Nature 616 7956:378-383. PubMed Id: 37045917. doi:10.1038/s41586-023-05808-z.
*Squid sensory receptor CRB1: Sepioloidea lineolata* E Eukaryota (expressed in HEK293 cells), 3.13 Å** cryo-EM structure	8EIZ	Data File Jmol Viewer 8EIZ	Kang et al. (2023). Kang G, Allard CAH, Valencia-Montoya WA, van Giesen L, Kim JJ, Kilian PB, Bai X, Bellono NW, & Hibbs RE (2023). Sensory specializations drive octopus and squid behaviour. Nature 616 7956:378-383. PubMed Id: 37045917. doi:10.1038/s41586-023-05808-z.
Type VII Secretion Systems
*ring-shaped virulence factor EspB of the ESX-1 system: Mycobacterium tuberculosis* B Bacteria (expressed in E. coli), 3.37 Å** cryoEM structure	6XZC	Data File Jmol Viewer 6XZC	Piton et al. (2020). Piton J, Pojer F, Wakatsuki S, Gati C, & Cole ST (2020). High resolution CryoEM structure of the ring-shaped virulence factor EspB from Mycobacterium tuberculosis. J Struct Biol X 4 :100029. PubMed Id: 32875288. doi:10.1016/j.yjsbx.2020.100029.
*PE-PPE domains of ESX-1 secreted protein EspB_7-278, C222₁ in the presence of Ca: Mycobacterium tuberculosis* B Bacteria (expressed in E. coli), 1.82 Å** I222 space group, 2.14 Å: 4XXN no calcium, C222₁ space group, 1.50 Å: 4XXX full length, C222₁ space group, 3.04 Å: 4XY3	4XWP	Data File Jmol Viewer 4XWP 4XXX 4XXN 4XY3	Korotkova et al. (2015). Korotkova N, Piton J, Wagner JM, Boy-Röttger S, Japaridze A, Evans TJ, Cole ST, Pojer F, & Korotkov KV (2015). Structure of EspB, a secreted substrate of the ESX-1 secretion system of Mycobacterium tuberculosis. J Struct Biol 191 2:236-244. PubMed Id: 26051906. doi:10.1016/j.jsb.2015.06.003.
*Mycobacterial secretion system ESX-5 inner membrane complex, Composite C1 model: Mycobacterium tuberculosis* B Bacteria (expressed in Mycolicibacterium smegmatis), 4.03 Å** cryo-EM structure Composite C3 model, 3.82 Å: 7NPR periplasmic assembly of inner membrane complex, C1 model, 3.81 Å: 7NPS Cytosolic bridge of intact ESX-5, 3.27 Å: 3.27 Å: 7NPB MycP5-free ESX-5 complex, state I, 4.48 Å: 7NPU MycP5-free ESX-5 complex, State II, 6.66 Å: 7NPV	7NP7	Data File Jmol Viewer 7NP7 7NPR 7NPB 7NPV 7NPS 7NPU	Bunduc et al. (2021). Bunduc CM, Fahrenkamp D, Wald J, Ummels R, Bitter W, Houben ENG, & Marlovits TC (2021). Structure and dynamics of a mycobacterial type VII secretion system. Nature 593 7859:445-448. PubMed Id: 33981042. doi:10.1038/s41586-021-03517-z.
*Mycobacterial secretion system, ESX-3 core complex: Mycolicibacterium smegmatis* B Bacteria, 3.8 Å** cryo-EM structure protomer 1 of the ESX-3 core complex, 3.7 Å: 6SGX EccB3 dimer from the ESX-3 core complex, 4.6 Å: 6SGY protomer 2 of the ESX-3 core complex, 6SGZ	6SGW	Data File Jmol Viewer 6SGW 6SGX 6SGZ 6SGY	Famelis et al. (2019). Famelis N, Rivera-Calzada A, Degliesposti G, Wingender M, Mietrach N, Skehel JM, Fernandez-Leiro R, Böttcher B, Schlosser A, Llorca O, & Geibel S (2019). Architecture of the mycobacterial type VII secretion system. Nature 576 7786:321-325. PubMed Id: 31597161. doi:10.1038/s41586-019-1633-1.
*ESX-3 Mycobacterial secretion system complete structure: Mycolicibacterium smegmatis* B Bacteria, 3.7 Å** cryo-EM structure	6UMM	Data File Jmol Viewer 6UMM	Poweleit et al. (2019). Poweleit N, Czudnochowski N, Nakagawa R, Trinidad DD, Murphy KC, Sassetti CM, & Rosenberg OS (2019). The structure of the endogenous ESX-3 secretion system. Elife 8 :e52983. PubMed Id: 31886769. doi:10.7554/eLife.52983.
*ESX-5 Type VII Secretion System hexameric pore complex: Mycobacterium xenopi* B Bacteria (expressed in Mycolicibacterium smegmatis), 3.00 Å** cryo-EM structure 3.40 Å: 7B9S x-ray: EccD5 ubiqutin like domain, 1.66 Å: 7B7J	7B9F	Data File Jmol Viewer 7B9F 7B9S 7B7J	Beckham et al. (2021). Beckham KSH, Ritter C, Chojnowski G, Ziemianowicz DS, Mullapudi E, Rettel M, Savitski MM, Mortensen SA, Kosinski J, & Wilmanns M (2021). Structure of the mycobacterial ESX-5 type VII secretion system pore complex. Sci Adv 7 26:eabg9923. PubMed Id: 34172453. doi:10.1126/sciadv.abg9923.
G PROTEIN-COUPLED RECEPTORS (GPCRs) Wikipedia Entry GPCRdb Home Page GPCR Molecular Dynamics Database
G Protein-Coupled Receptors: Class A
*Rhodopsin: Bos taurus (Bovine) Rod Outer Segment* E Eukaryota, 2.80 Å** See also 1HZX and RPE65 retinoid isomerase	1F88	Data File Jmol Viewer 1F88 1HZX rhodopsin	Palczewski et al. (2000). Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, & Miyano M (2000). Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289 :739-745. PubMed Id: 10926528.
*Rhodopsin: Bos taurus (Bovine) Rod Outer Segment* E Eukaryota, 2.6 Å**	1L9H	Data File Jmol Viewer 1L9H	Okada et al. (2002). Okada T, Fujiyoshi Y, Silow M, Navarro J, Landau EM, & Shichida Y (2002). Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography. Proc Natl Acad Sci U S A 99 :5982-5987. PubMed Id: 11972040.
*Rhodopsin: Bos taurus (Bovine) Rod Outer Segment* E Eukaryota, 2.65 Å**	1GZM	Data File Jmol Viewer 1GZM	Li et al. (2004). Li J, Edwards PC, Burghammer M, Villa C, & Schertler GF (2004). Structure of bovine rhodopsin in a trigonal crystal form. J Mol Biol. 343 :511-521. PubMed Id: 15491621.
*Rhodopsin: Bos taurus* E Eukaryota, 2.65 Å** Alternative model for 1GZM. Described using spacegroup P6₄	3C9L	Data File Jmol Viewer 3C9L	Stenkamp (2008). Stenkamp RE (2008). Alternative models for two crystal structures of bovine rhodopsin. Acta Crystallogr D Biol Crystallogr D64 :902-904. PubMed Id: 18645239. doi:10.1107/S0907444908017162.
*Rhodopsin: Bos taurus (Bovine) Rod Outer Segment* E Eukaryota, 2.2 Å**	1U19	Data File Jmol Viewer 1U19	Okada et al. (2004). Okada T, Sugihara M, Bondar AN, Elstner M, Entel P, & Buss V (2004). The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure. J Mol Biol 342 :571-583. PubMed Id: 15327956.
*Rhodopsin: Bos taurus (Bovine) Rod Outer Segment* E Eukaryota (expressed in COS cells), 3.4 Å** Recombinant rhodopsin mutant, N2C/D282C	2J4Y	Data File Jmol Viewer 2J4Y	Standfuss et al. (2007). Standfuss J, Xie G, Edwards PC, Burghammer M, Oprian DD, & Schertler GF (2007). Crystal structure of a thermally stable rhodopsin mutant. J Mol Biol 372 :1179-1188. PubMed Id: 17825322.
*Rhodopsin: Bos taurus* E Eukaryota, 3.40 Å** Recombinant rhodopsin mutant, N2C/D282C. Refinement of 2J4Y using P6₄ subgroup.	3C9M	Data File Jmol Viewer 3C9M	Stenkamp (2008). Stenkamp RE (2008). Alternative models for two crystal structures of bovine rhodopsin. Acta Crystallogr D Biol Crystallogr D64 :902-904. PubMed Id: 18645239. doi:10.1107/S0907444908017162.
*Rhodopsin, photoactivated: Bos taurus (Bovine) Rod Outer Segment* E Eukaryota, 4.15 Å** Ground state, rhombohedral crystals, 3.8 Å 2I35. Ground state, trigonal crystals, 4.1 Å 2I36.	2I37	Data File Jmol Viewer 2I37 2I36 2I35	Salom et al. (2006). Salom D, Ladowski DT, Stenkamp RE, Trong IL, Golczak M, Jastrzebska B, Harris T, Ballesteros JA & Palczewski K (2006). Crystal structure of a photoactivated deprotonated intermediate of rhodopsin. Proc Natl Acad Sci USA 103 :16123-16128. PubMed Id: 17060607.
*Rhodopsin in ligand-free state (opsin): Bos taurus (Bovine) Rod Outer Segment* E Eukaryota, 2.9 Å** 2 molecules in asymmetric unit.	3CAP	Data File Jmol Viewer 3CAP	Park et al. (2008). Park JH, Scheerer P, Hofmann KP, Choe HW, & Ernst OP (2008). Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454 :183-187. PubMed Id: 18563085.
*Rhodopsin in ligand-free state (opsin): Bos taurus* E Eukaryota, 2.65 Å** with bound GαCT2 peptide	4J4Q	Data File Jmol Viewer 4J4Q	Park et al. (2013). Park JH, Morizumi T, Li Y, Hong JE, Pai EF, Hofmann KP, Choe HW, & Ernst OP (2013). Opsin, a structural model for olfactory receptors? Angew Chem Int Ed Engl 52 :11021-11024. PubMed Id: 24038729. doi:10.1002/anie.201302374.
*Rhodopsin in ligand-free state (opsin): Bos taurus* E Eukaryota, 2.29 Å** with bound GαCT2 peptide.	4X1H	Data File Jmol Viewer 4X1H	Blankenship et al. (2015). Blankenship E, Vahedi-Faridi A, & Lodowski DT (2015). The High-Resolution Structure of Activated Opsin Reveals a Conserved Solvent Network in the Transmembrane Region Essential for Activation. Structure 23 :2358-2364. PubMed Id: 26526852. doi:10.1016/j.str.2015.09.015.
*Rhodopsin in ligand-free state (opsin) in complex with ArrFL-1: Bos taurus* E Eukaryota, 2.75 Å**	4PXF	Data File Jmol Viewer 4PXF	Szczepek et al. (2014). Szczepek M, Beyrière F, Hofmann KP, Elgeti M, Kazmin R, Rose A, Bartl FJ, von Stetten D, Heck M, Sommer ME, Hildebrand PW, & Scheerer P (2014). Crystal structure of a common GPCR-binding interface for G protein and arrestin. Nat Comms 5 :4801. PubMed Id: 25205354. doi:10.1038/ncomms5801.
*Rhodopsin, Ops-GαCT peptide complex: Bos taurus (Bovine) Rod Outer Segment E Eukaryota, 3.2 Å**	3DQB	Data File Jmol Viewer 3DQB	Scheerer et al. (2008). Scheerer P, Park JH, Hildebrand PW, Kim YJ, Krauss N, Choe HW, Hofmann KP, & Ernst OP (2008). Crystal structure of opsin in its G-protein-interacting conformation. Nature 455 :497-502. PubMed Id: 18818650.
*Rhodopsin in Meta II state: Bos taurus (Bovine) Rod Outer Segment* E Eukaryota, 3.00 Å** Metarhodopsin II in complex with C-terminal fragment of Gα (GαCT2), 2.85 Å: 3PQR	3PXO	Data File Jmol Viewer 3PXO 3PQR	Choe et al. (2011). Choe HW, Kim YJ, Park JH, Morizumi T, Pai EF, Krauß N, Hofmann KP, Scheerer P, & Ernst OP (2011). Crystal structure of metarhodopsin II. Nature 471 :651-655. PubMed Id: 21389988.
*Rhodopsin in constitutively active meta-II state: Bos taurus* E Eukaryota (expressed in HEK2935-GnTl^- cells), 3.30 Å** M257Y mutant in complex with GαCT.	4A4M	Data File Jmol Viewer 4A4M	Deupi et al. (2012). Deupi X, Edwards P, Singhal A, Nickle B, Oprian D, Schertler G, & Standfuss J (2012). Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II. Proc Natl Acad Sci USA 109 :119-124. PubMed Id: 22198838. doi:10.1073/pnas.1114089108.
*Rhodopsin in agonist-induced active state: Bos taurus* E Eukaryota, 3.00 Å**	2X72	Data File Jmol Viewer 2X72	Standfuss et al. (2011). Standfuss J, Edwards PC, D'Antona A, Fransen M, Xie G, Oprian DD, & Schertler GF (2011). The structural basis of agonist-induced activation in constitutively active rhodopsin Nature 471 7340:656-660. PubMed Id: 21389983. doi:10.1038/nature09795.
*Rhodopsin, N2C/D282C stabilized opsin bound to RS01: Bos taurus* E Eukaryota (expressed in HEK293S cells), 2.36 Å** bound to RS06, 2.62 Å: 6FK7 bound to RS08, 2.87 Å: 6FK8 bound to RS09, 2.63 Å:6FK9 bound to RS11, 2.7 Å: 6FKA bound to RS13, 3.03 Å: 6FKB bound to RS15, 2.46 Å: 6FKC bound to RS16, 2.49 Å: 6FKD	6FK6	Data File Jmol Viewer 6FK6 6FKA 6FK7 6FK8 6FK9 6FKB 6FKC 6FKD	Mattle et al. (2018). Mattle D, Kuhn B, Aebi J, Bedoucha M, Kekilli D, Grozinger N, Alker A, Rudolph MG, Schmid G, Schertler GFX, Hennig M, Standfuss J, & Dawson RJP (2018). Ligand channel in pharmacologically stabilized rhodopsin. Proc Natl Acad Sci USA 115 14:3640-3645. PubMed Id: 29555765. doi:10.1073/pnas.1718084115.
*Rhodopsin-Gαi-βγ complex: Bos taurus* E Eukaryota (expressed in HEK 293 cells), 4.38 Å** cryo-EM structure, N2C/M257Y/D282C mutant FAB fragment targeting Gi protein heterotrimer, 1.9 Å: 6QNK	6QNO	Data File Jmol Viewer 6QNO 6QNK	Tsai et al. (2019). Tsai CJ, Marino J, Adaixo R, Pamula F, Muehle J, Maeda S, Flock T, Taylor NM, Mohammed I, Matile H, Dawson RJ, Deupi X, Stahlberg H, & Schertler G (2019). Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the gβ subunit. Elife 8 :e46041. PubMed Id: 31251171. doi:10.7554/eLife.46041.
*Rhodopsin-Transducin Complex: Bos taurus* E Eukaryota, 3.9 Å** cryo-EM structure Rhodopsin-Transducin-Nanobody Complex, 3.3 Å: 6OYA	6OY9	Data File Jmol Viewer 6OY9 6OYA	Gao et al. (2019). Gao Y, Hu H, Ramachandran S, Erickson JW, Cerione RA, & Skiniotis G (2019). Structures of the Rhodopsin-Transducin Complex: Insights into G-Protein Activation. Mol Cell 75 4:781-790.e3. PubMed Id: 31300275. doi:10.1016/j.molcel.2019.06.007.
*Visual Signaling Complex between Transducin and Phosphodiesterase 6: Bos taurus* E Eukaryota (expressed in E. coli), 3.20 Å** cryo-EM structure	7JSN	Data File Jmol Viewer 7JSN	Gao et al. (2020). Gao Y, Eskici G, Ramachandran S, Poitevin F, Seven AB, Panova O, Skiniotis G, & Cerione RA (2020). Structure of the Visual Signaling Complex between Transducin and Phosphodiesterase 6. Mol Cell 80 2:237-245.e4. PubMed Id: 33007200. doi:10.1016/j.molcel.2020.09.013.
*Rhodopsin (native dimer) in nanodiscs: Bos taurus* E Eukaryota, 4.5 Å** cryo-EM structure	6OFJ	Data File Jmol Viewer 6OFJ	Zhao et al. (2019). Zhao DY, Pöge M, Morizumi T, Gulati S, Van Eps N, Zhang J, Miszta P, Filipek S, Mahamid J, Plitzko JM, Baumeister W, Ernst OP, & Palczewski K (2019). Cryo-EM structure of the native rhodopsin dimer in nanodiscs. J Biol Chem 294 39:14215-14230. PubMed Id: 31399513. doi:10.1074/jbc.RA119.010089.
*Rhodopsin, activated state (metarhodopsin II): Bos taurus* E Eukaryota, NMR structure**	1LN6	Data File Jmol Viewer 1LN6	Choi et al. (2002). Choi G, Landin J, Galan JF, Birge RR, Albert AD, & Yeagle PL (2002). Structural studies of metarhodopsin II, the activated form of the G-protein coupled receptor, rhodopsin. Biochemistry 41 :7318-7324. PubMed Id: 12044163.
*Rhodopsin in complex with rhodopsin kinase (GRK1): Bos taurus* E Eukaryota (expressed in Spodoptera frugiperda), 7.00 Å** cryo-EM structure GRK1-S5E/S488E/T489E in complex with rhodopsin, 5.80 Å: 7MT8 GRK1-S5E/S488E/T489E & Fab1 in complex with rhodopsin, 4.10 Å: 7MTA GRK1-S5E/S488E/T489E in complex with rhodopsin and Fab6, 4.00 Å: 7MTB	7MT9	Data File Jmol Viewer 7MT9 7MTB 7MT8 7MTA	Chen et al. (2021). Chen Q, Plasencia M, Li Z, Mukherjee S, Patra D, Chen CL, Klose T, Yao XQ, Kossiakoff AA, Chang L, Andrews PC, & Tesmer JJG (2021). Structures of rhodopsin in complex with G-protein-coupled receptor kinase 1. Nature 595 7868:600-605. PubMed Id: 34262173. doi:10.1038/s41586-021-03721-x.
*Rhodopsin, by serial femtosecond crystallography (SFX), at SACLA, dark state: Bos taurus* E Eukaryota, 1.80 Å** SFX data at SwissFEL, 1.80 Å: 7ZBE 1 ps photoactivation, TR-SFX data at SwissFEL, 1.80 Å: 8A6C 10 ps photoactivation, TR-SFX data at SwissFEL, 1.80 Å: 8A6D 100 ps photoactivation, TR-SFX data at SACLA, 1.80 Å: 8A6E	7ZBC	Data File Jmol Viewer 7ZBC 7ZBE 8A6D 8A6C 8A6E	Gruhl et al. (2023). Gruhl T, Weinert T, Rodrigues MJ, Milne CJ, Ortolani G, Nass K, Nango E, Sen S, Johnson PJM, Cirelli C, Furrer A, Mous S, Skopintsev P, James D, Dworkowski F, Båth P, Kekilli D, Ozerov D, Tanaka R, Glover H, Bacellar C, Brünle S, Casadei CM, Diethelm AD, Gashi D, Gotthard G, Guixà-González R, Joti Y, Kabanova V, Knopp G, Lesca E, Ma P, Martiel I, Mühle J, Owada S, Pamula F, Sarabi D, Tejero O, Tsai CJ, Varma N, Wach A, Boutet S, Tono K, Nogly P, Deupi X, Iwata S, Neutze R, Standfuss J, Schertler G, & Panneels V (2023). Ultrafast structural changes direct the first molecular events of vision. Nature 615 7954:939-944. PubMed Id: 36949205. doi:10.1038/s41586-023-05863-6.
*Rhodopsin, Squid: Todarodes pacificus* E Eukaryota, 2.50 Å**	2Z73	Data File Jmol Viewer 2Z73	Murakami & Kouyama (2008). Murakami M & Kouyama T (2008). Crystal structure of squid rhodopsin. Nature 453 :363-367. PubMed Id: 18480818.
*Rhodopsin, Squid: Todarodes pacificus* E Eukaryota, 3.7 Å** Shows intracellularly extended cytoplasmic region.	2ZIY	Data File Jmol Viewer 2ZIY	Shimamura et al. (2008). Shimamura T, Hiraki K, Takahashi N, Hori T, Ago H, Masuda K, Takio K, Ishiguro M, & Miyano M. (2008). Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region. J Biol Chem 283 :17753-17756. PubMed Id: 18463093.
*Rhodopsin, Squid; 9-cis isorhodopsin (Iso): Todarodes pacificus* E Eukaryota, 2.70 Å** Batho intermediate state, 2.80 Å: 3AYM	3AYN	Data File Jmol Viewer 3AYN 3AYM	Murakami & Kouyama (2011). Murakami M & Kouyama T (2011). Crystallographic analysis of the primary photochemical reaction of squid rhodopsin. J Mol Biol 413 :615-627. PubMed Id: 21906602. doi:10.1016/j.jmb.2011.08.044.
*Human rhodopsin with bound mouse visual arrestin: Homo sapiens* E Eukaryota (expressed in HEK293S cells), 3.30 Å** Engineered protein. T4 lysozyme (Cys-free) fused to N-terminus of rhodopsin and arrestin fused to C-terminus with a 15-residue linker. Structure determined by fS x-ray laser.	4ZWJ	Data File Jmol Viewer 4ZWJ	Kang et al. (2015). Kang Y, Zhou XE, Gao X, He Y, Liu W, Ishchenko A, Barty A, White TA, Yefanov O, Han GW, Xu Q, de Waal PW, Ke J, Tan MH, Zhang C, Moeller A, West GM, Pascal BD, Van Eps N, Caro LN, Vishnivetskiy SA, Lee RJ, Suino-Powell KM, Gu X, Pal K, Ma J, Zhi X, Boutet S, Williams GJ, Messerschmidt M, Gati C, Zatsepin NA, Wang D, James D, Basu S, Roy-Chowdhury S, Conrad CE, Coe J, Liu H, Lisova S, Kupitz C, Grotjohann I, Fromme R, Jiang Y, Tan M, Yang H, Li J, Wang M, Zheng Z, Li D, Howe N, Zhao Y, Standfuss J, Diederichs K, Dong Y, Potter CS, Carragher B, Caffrey M, Jiang H, Chapman HN, Spence JC, Fromme P, Weierstall U, Ernst OP, Katritch V, Gurevich VV, Griffin PR, Hubbell WL, Stevens RC, Cherezov V, Melcher K, & Xu HE (2015). Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Nature 523 :561-567. PubMed Id: 26200343. doi:10.1038/nature14656.
*Human rhodopsin with bound inhibitory G protein (G_i): Homo sapiens* E Eukaryota (expressed in Sf9 cells), 4.5 Å** cryo-EM structure	6CMO	Data File Jmol Viewer 6CMO	Kang et al. (2018). Kang Y, Kuybeda O, de Waal PW, Mukherjee S, Van Eps N, Dutka P, Zhou XE, Bartesaghi A, Erramilli S, Morizumi T, Gu X, Yin Y, Liu P, Jiang Y, Meng X, Zhao G, Melcher K, Ernst OP, Kossiakoff AA, Subramaniam S, & Xu HE (2018). Cryo-EM structure of human rhodopsin bound to an inhibitory G protein. Nature 558 7711:553-558. PubMed Id: 29899450. doi:10.1038/s41586-018-0215-y.
*Jumping spider rhodopsin-1: Hasarius adansoni* E Eukaryota (expressed in HEK293 cells), 2.14 Å**	6I9K	Data File Jmol Viewer 6I9K	Varma et al. (2019). Varma N, Mutt E, Mühle J, Panneels V, Terakita A, Deupi X, Nogly P, Schertler GFX, & Lesca E (2019). Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR. Proc Natl Acad Sci USA 116 29:14547-14556. PubMed Id: 31249143. doi:10.1073/pnas.1902192116.
*Orphan GPR17 class A receptor - G_i complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.02 Å** cryo-EM structure	7Y89	Data File Jmol Viewer 7Y89	Ye et al. (2022). Ye F, Wong TS, Chen G, Zhang Z, Zhang B, Gan S, Gao W, Li J, Wu Z, Pan X, & Du Y (2022). Cryo-EM structure of G-protein-coupled receptor GPR17 in complex with inhibitory G protein. MedComm (2020) 3 4:e159. PubMed Id: 36105372. doi:10.1002/mco2.159.
*Orphan GPR20 class A receptor - G_i complex: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.14 Å** cryo-EM structure with bound Fab046, 3.22 Å: 8HSC GPR20 - Fab046 complex, 3.08 Å: 8HS2	8HS3	Data File Jmol Viewer 8HS3 8HSC 8HS2	Lin et al. (2023). Lin X, Jiang S, Wu Y, Wei X, Han GW, Wu L, Liu J, Chen B, Zhang Z, Zhao S, Cherezov V, & Xu F (2023). The activation mechanism and antibody binding mode for orphan GPR20. Cell Discov 9 1:23. PubMed Id: 36849514. doi:10.1038/s41421-023-00520-8.
*Orphan GPR21 class A receptor - G_s complex, apo form: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.91 Å** cryo-EM structure	8HMV	Data File Jmol Viewer 8HMV	Wong et al. (2023). Wong TS, Gao W, Chen G, Qiu C, He G, Ye F, Wu Z, Zeng Z, & Du Y (2023). Cryo-EM structure of orphan G protein-coupled receptor GPR21. MedComm (2020) 4 1:e205. PubMed Id: 36721851. doi:10.1002/mco2.205.
*Orphan GPR21 class A receptor - G_s complex, wild-type: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.27 Å** cryo-EM structure m5 (5 mutations), 3.12 Å: 8HIX GPR21-G15 complex, wild-type, 3.80 Å: 8HJ2 GPR21-G15 complex, m5 (5 mutations), 3.12 Å: 8HJ0	8HJ1	Data File Jmol Viewer 8HJ1 8HJ0 8HIX 8HJ2	Lin et al. (2023). Lin X, Chen B, Wu Y, Han Y, Qi A, Wang J, Yang Z, Wei X, Zhao T, Wu L, Xie X, Sun J, Zheng J, Zhao S, & Xu F (2023). Cryo-EM structures of orphan GPR21 signaling complexes. Nat Commun 14 1:216. PubMed Id: 36639690. doi:10.1038/s41467-023-35882-w.
*Orphan GPR34 class A receptor with bound antagonist YL-365: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.34 Å** cryo-EM structure G_i complex with bound LysoPS (18:1), 3.27 Å: 8SAI	8IYX	Data File Jmol Viewer 8IYX 8SAI	Xia et al. (2023). Xia A, Yong X, Zhang C, Lin G, Jia G, Zhao C, Wang X, Hao Y, Wang Y, Zhou P, Yang X, Deng Y, Wu C, Chen Y, Zhu J, Tang X, Liu J, Zhang S, Zhang J, Xu Z, Hu Q, Zhao J, Yue Y, Yan W, Su Z, Wei Y, Zhou R, Dong H, Shao Z, & Yang S (2023). Cryo-EM structures of human GPR34 enable the identification of selective antagonists. Proc Natl Acad Sci U S A 120 39:e2308435120. PubMed Id: 37733739. doi:10.1073/pnas.2308435120.
*Orphan GPR35 class A receptor - G₁₃ complex with bound lodoxamide: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.20 Å** cryo-EM structure	8H8J	Data File Jmol Viewer 8H8J	Duan et al. (2022). Duan J, Liu Q, Yuan Q, Ji Y, Zhu S, Tan Y, He X, Xu Y, Shi J, Cheng X, Jiang H, Eric Xu H, & Jiang Y (2022). Insights into divalent cation regulation and G13-coupling of orphan receptor GPR35. Cell Discov 8 1:135. PubMed Id: 36543774. doi:10.1038/s41421-022-00499-8.
*Orphan GPR52 class A receptor, ligand-free form with flavodoxin fusion: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.9 Å** ligand-free form with rubredoxin fusion, 2.8 Å: 6LI2 in complex with agonist c17, 2.2 Å: 6LI0 GPR52-miniG_s-NB35, 3.32 Å: 6LI3	6LI1	Data File Jmol Viewer 6LI1 6LI2 6LI0 6LI3	Lin et al. (2020). Lin X, Li M, Wang N, Wu Y, Luo Z, Guo S, Han GW, Li S, Yue Y, Wei X, Xie X, Chen Y, Zhao S, Wu J, Lei M, & Xu F (2020). Structural basis of ligand recognition and self-activation of orphan GPR52. Nature 579 7797:152-157. PubMed Id: 32076264. doi:10.1038/s41586-020-2019-0.
*Orphan GPR61 class A receptor - G_s complex: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.16 Å** cryo-EM structure	8KGK	Data File Jmol Viewer 8KGK	Nie et al. (2023). Nie Y, Qiu Z, Chen S, Chen Z, Song X, Ma Y, Huang N, Cyster JG, & Zheng S (2023). Specific binding of GPR174 by endogenous lysophosphatidylserine leads to high constitutive Gs signaling. Nat Commun 14 1:5901. PubMed Id: 37737235. doi:10.1038/s41467-023-41654-3.
*Orphan GPR84 class A receptor - G_i complex with bound 3-hydroxy lauric acid: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.89 Å** cryo-EM structure with bound LY237, 3.23 Å: 8J19 apo, 3.24 Å: 8J1A	8J18	Data File Jmol Viewer 8J18 8J1A 8J19	Liu et al. (2023). Liu H, Zhang Q, He X, Jiang M, Wang S, Yan X, Cheng X, Liu Y, Nan FJ, Xu HE, Xie X, & Yin W (2023). Structural insights into ligand recognition and activation of the medium-chain fatty acid-sensing receptor GPR84. Nat Commun 14 1:3271. PubMed Id: 37277332. doi:10.1038/s41467-023-38985-6.
*Orphan GPR84 class A receptor - G_i complex with bound agonist 6-OAU: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.00 Å** cryo-EM structure	8G05	Data File Jmol Viewer 8G05	Zhang et al. (2023). Zhang X, Wang Y, Supekar S, Cao X, Zhou J, Dang J, Chen S, Jenkins L, Marsango S, Li X, Liu G, Milligan G, Feng M, Fan H, Gong W, & Zhang C (2023). Pro-phagocytic function and structural basis of GPR84 signaling. Nat Commun 14 1:5706. PubMed Id: 37709767. doi:10.1038/s41467-023-41201-0.
*Orphan GPR88 class A receptor - G_i1 complex, apo form: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å** cryo-EM structure with bound synthetic ligand 2PCCA, 2.40 Å: 7EJX	7WZ4	Data File Jmol Viewer 7WZ4 7EJX	Chen et al. (2022). Chen G, Xu J, Inoue A, Schmidt MF, Bai C, Lu Q, Gmeiner P, Liu Z, & Du Y (2022). Activation and allosteric regulation of the orphan GPR88-Gi1 signaling complex. Nat Commun 13 1:2375. PubMed Id: 35501348. doi:10.1038/s41467-022-30081-5.
*Orphan GPR101 class A receptor - G_s complex, apo state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.89 Å** cryo-EM structure with bound AA-14, 3.30 Å: 8W8R with bound AA-14, local refinement, 3.30 Å: 8W8S	8W8Q	Data File Jmol Viewer 8W8Q 8W8S 8W8R	Yang et al. (2023). Yang Z, Wang JY, Yang F, Zhu KK, Wang GP, Guan Y, Ning SL, Lu Y, Li Y, Zhang C, Zheng Y, Zhou SH, Wang XW, Wang MW, Xiao P, Yi F, Zhang C, Zhang PJ, Xu F, Liu BH, Zhang H, Yu X, Gao N, & Sun JP (2023). Structure of GPR101-Gs enables identification of ligands with rejuvenating potential. Nat Chem Biol . PubMed Id: 37945893. doi:10.1038/s41589-023-01456-6.
*Orphan GPR119 class A receptor - G_s complex with bound LPC: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.10 Å** cryo-EM structure with bound APD668, 2.80 Å: 7XZ6	7XZ5	Data File Jmol Viewer 7XZ5 7XZ6	Xu et al. (2022). Xu P, Huang S, Guo S, Yun Y, Cheng X, He X, Cai P, Lan Y, Zhou H, Jiang H, Jiang Y, Xie X, & Xu HE (2022). Structural identification of lysophosphatidylcholines as activating ligands for orphan receptor GPR119. Nat Struct Mol Biol 29 9:863-870. PubMed Id: 35970999. doi:10.1038/s41594-022-00816-5.
*Orphan GPR119 class A receptor - G_s complex with bound AR231453: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.87 Å** cryo-EM structure with bound MBX-2982, 2.33 Å:7WCM	7WCN	Data File Jmol Viewer 7WCN 7WCM	Qian et al. (2022). Qian Y, Wang J, Yang L, Liu Y, Wang L, Liu W, Lin Y, Yang H, Ma L, Ye S, Wu S, & Qiao A (2022). Activation and signaling mechanism revealed by GPR119-Gs complex structures. Nat Commun 13 1:7033. PubMed Id: 36396650. doi:10.1038/s41467-022-34696-6.
*Orphan GPR139 receptor - G_i complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** cryo-EM structure JNJ-63533054-miniG_s/q, 3.22 Å 7VUH JNJ-63533054-miniG_s/q with bound GTP, 3.30 Å 7VUI JNJ-63533054-miniG_s/q with bound GDP, 3.80 Å 7VUJ	7VUG	Data File Jmol Viewer 7VUG 7VUI 7VUJ 7VUH	Zhou et al. (2021). Zhou Y, Daver H, Trapkov B, Wu L, Wu M, Harpsøe K, Gentry PR, Liu K, Larionova M, Liu J, Chen N, Bräuner-Osborne H, Gloriam DE, Hua T, & Liu ZJ (2021). Molecular insights into ligand recognition and G protein coupling of the neuromodulatory orphan receptor GPR139. Cell Res . PubMed Id: 34916631. doi:10.1038/s41422-021-00591-w.
*Orphan GPR161 class A receptor - G_s complex: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.10 Å** cryo-EM structure	8KH4	Data File Jmol Viewer 8KH4	Nie et al. (2023). Nie Y, Qiu Z, Chen S, Chen Z, Song X, Ma Y, Huang N, Cyster JG, & Zheng S (2023). Specific binding of GPR174 by endogenous lysophosphatidylserine leads to high constitutive Gs signaling. Nat Commun 14 1:5901. PubMed Id: 37737235. doi:10.1038/s41467-023-41654-3.
*Orphan GPR161 class A receptor - G_s complex: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.74 Å** cryo-EM structure	8SMV	Data File Jmol Viewer 8SMV	Hoppe et al. (2024). Hoppe N, Harrison S, Hwang SH, Chen Z, Karelina M, Deshpande I, Suomivuori CM, Palicharla VR, Berry SP, Tschaikner P, Regele D, Covey DF, Stefan E, Marks DS, Reiter JF, Dror RO, Evers AS, Mukhopadhyay S, & Manglik A (2024). GPR161 structure uncovers the redundant role of sterol-regulated ciliary cAMP signaling in the Hedgehog pathway. Nat Struct Mol Biol . PubMed Id: 38326651. doi:10.1038/s41594-024-01223-8.
*Orphan GPR174 receptor - G_s complex with bound LPS: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.76 Å** cryo-EM structure	7XV3	Data File Jmol Viewer 7XV3	Liang et al. (2023). Liang J, Inoue A, Ikuta T, Xia R, Wang N, Kawakami K, Xu Z, Qian Y, Zhu X, Zhang A, Guo C, Huang Z, & He Y (2023). Structural basis of lysophosphatidylserine receptor GPR174 ligand recognition and activation. Nat Commun 14 1:1012. PubMed Id: 36823105. doi:10.1038/s41467-023-36575-0.
*Orphan GPR174 class A receptor - G_s complex with bound endogenous lysoPS: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.83 Å** cryo-EM structure	8KH5	Data File Jmol Viewer 8KH5	Nie et al. (2023). Nie Y, Qiu Z, Chen S, Chen Z, Song X, Ma Y, Huang N, Cyster JG, & Zheng S (2023). Specific binding of GPR174 by endogenous lysophosphatidylserine leads to high constitutive Gs signaling. Nat Commun 14 1:5901. PubMed Id: 37737235. doi:10.1038/s41467-023-41654-3.
*Orphan GPR183 (EBI2) receptor with bound GSK682753A: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.98 Å** cryo-EM structure G_i complex with bound 7α,25-OHC, 3.12 Å, 7TUZ	7TUY	Data File Jmol Viewer 7TUY 7TUZ	Chen et al. (2022). Chen H, Huang W, & Li X (2022). Structures of oxysterol sensor EBI2/GPR183, a key regulator of the immune response. Structure 30 7:1016-1024.e5. PubMed Id: 35537452. doi:10.1016/j.str.2022.04.006.
*OX₁ orexin receptor with bound suvorexant: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.75 Å** with bound SB-674042, 2.83 Å: 4ZJC	4ZJ8	Data File Jmol Viewer 4ZJ8 4ZJC	Yin et al. (2016). Yin J, Babaoglu K, Brautigam CA, Clark L, Shao Z, Scheuermann TH, Harrell CM, Gotter AL, Roecker AJ, Winrow CJ, Renger JJ, Coleman PJ, & Rosenbaum DM (2016). Structure and ligand-binding mechanism of the human OX1 and OX2 orexin receptors. Nat Struct Mol Biol 23 :293-299. PubMed Id: 26950369. doi:10.1038/nsmb.3183.
*OX₁ orexin receptor in complex with suvorexant: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.29 Å** in complex with filorexant, 2.34 Å: 6TP6 in complex with lemborexant, 2.22 Å: 6TOT in complex with daridorexant, 3.04 Å: 6TP3 in complex with EMPA, 2.11 Å: 6TOD in complex with GSK1059865, 2.13 Å: 6TOS in complex with SB-334867, 2.66 Å: 6TQ7 in complex with SB-408124, 2.66 Å: 6TQ9 in complex with Compound 14, 2.55 Å: 6TQ6 in complex with ACT-462206, 3.04 Å: 6TP4 in complex with Compound 16, 2.30 Å: 6TQ4	6TO7	Data File Jmol Viewer 6TO7 6TQ7 6TQ4 6TQ6 6TOS 6TP4 6TOT 6TP6 6TP3 6TOD 6TQ9	Rappas et al. (2020). Rappas M, Ali AAE, Bennett KA, Brown JD, Bucknell SJ, Congreve M, Cooke RM, Cseke G, de Graaf C, Doré AS, Errey JC, Jazayeri A, Marshall FH, Mason JS, Mould R, Patel JC, Tehan BG, Weir M, & Christopher JA (2020). Comparison of Orexin 1 and Orexin 2 Ligand Binding Modes Using X-ray Crystallography and Computational Analysis. J Med Chem 63 4:1528-1543. PubMed Id: 31860301. doi:10.1021/acs.jmedchem.9b01787.
*OX1 orexin receptor with bound subtype-selective antagonist: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.50 Å**	6V9S	Data File Jmol Viewer 6V9S	Hellmann et al. (2020). Hellmann J, Drabek M, Yin J, Gunera J, Pröll T, Kraus F, Langmead CJ, Hübner H, Weikert D, Kolb P, Rosenbaum DM, & Gmeiner P (2020). Structure-based development of a subtype-selective orexin 1 receptor antagonist. Proc Natl Acad Sci USA 117 30:18059-18067. PubMed Id: 32669442. doi:10.1073/pnas.2002704117.
*OX₂ orexin receptor with bound suvorexant: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.50 Å** 4S0V supersedes 4RNB. Engineered protein: Pyrococcus abysii glycogen synthase replaced 39 residues of the 3rd intracellular loop.	4S0V	Data File Jmol Viewer 4S0V	Yin et al. (2015). Yin J, Mobarec JC, Kolb P, & Rosenbaum DM (2015). Crystal structure of the human OX₂ orexin receptor bound to the insomnia drug suvorexant. Nature 519 7542:247-250. PubMed Id: 25533960. doi:10.1038/nature14035.
*OX₂ orexin receptor with bound antagonist EMPA: Homo sapiens* E Eukaryota (expressed in sf9 cells), 1.96 Å** Engineered protein: Pyrococcus abysii glycogen synthase replaced 39 residues of the 3rd intracellular loop. XFEL structure, 2.3 Å: 5WS3	5WQC	Data File Jmol Viewer 5WQC 5WS3	Suno et al. (2018). Suno R, Kimura KT, Nakane T, Yamashita K, Wang J, Fujiwara T, Yamanaka Y, Im D, Horita S, Tsujimoto H, Tawaramoto MS, Hirokawa T, Nango E, Tono K, Kameshima T, Hatsui T, Joti Y, Yabashi M, Shimamoto K, Yamamoto M, Rosenbaum DM, Iwata S, Shimamura T, & Kobayashi T (2018). Crystal Structures of Human Orexin 2 Receptor Bound to the Subtype-Selective Antagonist EMPA. Structure 26 :7-19.e5. PubMed Id: 29225076. doi:10.1016/j.str.2017.11.005.
*OX₂ orexin receptor in complex with suvorexant: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.74 Å** in complex with EMPA, 2.74 Å: 6TPG in complex with HTL6641, 2.61 Å: 6TPN	6TPJ	Data File Jmol Viewer 6TPJ 6TPG 6TPN	Rappas et al. (2020). Rappas M, Ali AAE, Bennett KA, Brown JD, Bucknell SJ, Congreve M, Cooke RM, Cseke G, de Graaf C, Doré AS, Errey JC, Jazayeri A, Marshall FH, Mason JS, Mould R, Patel JC, Tehan BG, Weir M, & Christopher JA (2020). Comparison of Orexin 1 and Orexin 2 Ligand Binding Modes Using X-ray Crystallography and Computational Analysis. J Med Chem 63 4:1528-1543. PubMed Id: 31860301. doi:10.1021/acs.jmedchem.9b01787.
*OX₂ orexin receptor in complex with G protein and natural peptide-agonist Orexin B (OxB): Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.20 Å** cryo-EM structure Complex with G Protein and Small-Molecule Agonist Compound 1, 3.00 Å: 7L1V	7L1U	Data File Jmol Viewer 7L1U 7L1V	Hong et al. (2021). Hong C, Byrne NJ, Zamlynny B, Tummala S, Xiao L, Shipman JM, Partridge AT, Minnick C, Breslin MJ, Rudd MT, Stachel SJ, Rada VL, Kern JC, Armacost KA, Hollingsworth SA, O'Brien JA, Hall DL, McDonald TP, Strickland C, Brooun A, Soisson SM, & Hollenstein K (2021). Structures of active-state orexin receptor 2 rationalize peptide and small-molecule agonist recognition and receptor activation. Nat Commun 12 1:815. PubMed Id: 33547286. doi:10.1038/s41467-021-21087-6.
*OX₂ orexin receptor in complex with G_i protein and TAK-925: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.17 Å** cryo-EM structure in complex with G_q protein and TAK-925, 3.30 Å: 7SR8	7SQO	Data File Jmol Viewer 7SQO 7SR8	Yin et al. (2022). Yin J, Kang Y, McGrath AP, Chapman K, Sjodt M, Kimura E, Okabe A, Koike T, Miyanohana Y, Shimizu Y, Rallabandi R, Lian P, Bai X, Flinspach M, De Brabander JK, & Rosenbaum DM (2022). Molecular mechanism of the wake-promoting agent TAK-925. Nat Commun 13 1:2902. PubMed Id: 35614071. doi:10.1038/s41467-022-30601-3.
*OX₂ orexin receptor with bound lemborexant: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.89 Å**	7XRR	Data File Jmol Viewer 7XRR	Asada et al. (2022). Asada H, Im D, Hotta Y, Yasuda S, Murata T, Suno R, & Iwata S (2022). Molecular basis for anti-insomnia drug design from structure of lemborexant-bound orexin 2 receptor. Structure 30 12:1582-1589.e4. PubMed Id: 36417909. doi:10.1016/j.str.2022.11.001.
*C3a anaphylatoxin chemotactic receptor (C3aR) - G_o complex, apo form; 200kV Glacios: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.19 Å** cryo-EM structure 300 kV Titan Krios, 3.26 Å: 8I9S with bound C3a (composite map), 3.18 Å: 8I9L with bound decapeptide EP54, 2.88 Å: 8I95 with bound pentadecameric peptide EP141, 3.10 Å: 8J6D G_q complex with bound decapeptide EP54, 3.57 Å: 8I9A	8I97	Data File Jmol Viewer 8I97 8I9L 8I9A 8I95 8I9S	Yadav et al. (2023). Yadav MK, Maharana J, Yadav R, Saha S, Sarma P, Soni C, Singh V, Saha S, Ganguly M, Li XX, Mohapatra S, Mishra S, Khant HA, Chami M, Woodruff TM, Banerjee R, Shukla AK, & Gati C (2023). Molecular basis of anaphylatoxin binding, activation, and signaling bias at complement receptors. Cell 186 22:4956-4973.e21. PubMed Id: 37852260. doi:10.1016/j.cell.2023.09.020.
*C5a anaphylatoxin chemotactic receptor 1 (C5aR) in complex with NDT9513727: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.7 Å** Thermostabilized protein.	5O9H	Data File Jmol Viewer 5O9H	Robertson et al. (2018). Robertson N, Rappas M, Doré AS, Brown J, Bottegoni G, Koglin M, Cansfield J, Jazayeri A, Cooke RM, & Marshall FH (2018). Structure of the complement C5a receptor bound to the extra-helical antagonist NDT9513727. Nature 553 :111-114. PubMed Id: 29300009. doi:10.1038/nature25025.
C5a anaphylatoxin chemotactic receptor 1 (C5aR) in complex with orthosteric antagonist PMX53 and allosteric antagonist NDT9513727: Homo sapiens E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å in complex with orthosteric antagonist PMX53 and allosteric antagonist avacopan, 2.20 Å: 6C1R Engineered protein. N-terminal BRIL fusion.	6C1Q	Data File Jmol Viewer 6C1Q 6C1R	Liu et al. (2018). Liu H, Kim HR, Deepak RNVK, Wang L, Chung KY, Fan H, Wei Z, & Zhang C (2018). Orthosteric and allosteric action of the C5a receptor antagonists. Nat Struct Mol Biol 25 6:472-481. PubMed Id: 29867214. doi:10.1038/s41594-018-0067-z.
*C5a anaphylatoxin chemotactic receptor 1 (C5aR) - G_i complex, with bound C5a anaphylatoxin: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.90 Å** cryo-EM structure with bound C5a peptide, 3.20 Å: 7Y65 with bound BM213, 2.90 Å: 7Y66 I116A mutant, with bound CO89, 2.80 Å: 7Y67	7Y64	Data File Jmol Viewer 7Y64 7Y65 7Y66 7Y67	Feng et al. (2023). Feng Y, Zhao C, Deng Y, Wang H, Ma L, Liu S, Tian X, Wang B, Bin Y, Chen P, Yan W, Fu P, & Shao Z (2023). Mechanism of activation and biased signaling in complement receptor C5aR1. Cell Res 33 4:312-324. PubMed Id: 36806352. doi:10.1038/s41422-023-00779-2.
*C5a anaphylatoxin chemotactic receptor 1 (C5aR1) - G_o complex with bound C5a (composite map): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.21 Å** cryo-EM structure with bound C5a (desArg form), 3.31 Å: 8JZZ	8IA2	Data File Jmol Viewer 8IA2 8JZZ	Yadav et al. (2023). Yadav MK, Maharana J, Yadav R, Saha S, Sarma P, Soni C, Singh V, Saha S, Ganguly M, Li XX, Mohapatra S, Mishra S, Khant HA, Chami M, Woodruff TM, Banerjee R, Shukla AK, & Gati C (2023). Molecular basis of anaphylatoxin binding, activation, and signaling bias at complement receptors. Cell 186 22:4956-4973.e21. PubMed Id: 37852260. doi:10.1016/j.cell.2023.09.020.
*C5a anaphylatoxin chemotactic receptor 1 (C5aR1) - G_o complex with bound C5a: Mus musculus* E Eukaryota (expressed in S. frugiperda), 3.89 Å** cryo-EM structure with bound C5a-pep, 3.39 Å: 8HPT	8HQC	Data File Jmol Viewer 8HQC 8HPT	Yadav et al. (2023). Yadav MK, Maharana J, Yadav R, Saha S, Sarma P, Soni C, Singh V, Saha S, Ganguly M, Li XX, Mohapatra S, Mishra S, Khant HA, Chami M, Woodruff TM, Banerjee R, Shukla AK, & Gati C (2023). Molecular basis of anaphylatoxin binding, activation, and signaling bias at complement receptors. Cell 186 22:4956-4973.e21. PubMed Id: 37852260. doi:10.1016/j.cell.2023.09.020.
*α_1A-adrenergic receptor miniG_sq-Nb29 complex with bound oxymetazoline: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.92 Å** cryo-EM structure with bound noradrenaline, 3.52 Å: 7YMH Nb6 complex with bound tamsulosin, 3.35 Å: 7YMJ	7YM8	Data File Jmol Viewer 7YM8 7YMH 7YMJ	Toyoda et al. (2023). Toyoda Y, Zhu A, Kong F, Shan S, Zhao J, Wang N, Sun X, Zhang L, Yan C, Kobilka BK, & Liu X (2023). Structural basis of α1A-adrenergic receptor activation and recognition by an extracellular nanobody. Nat Commun 14 1:3655. PubMed Id: 37339967. doi:10.1038/s41467-023-39310-x.
*α_1B-adrenergic receptor in complex with inverse agonist (+)-cyclazosin: Homo sapiens* E Eukaryota (expressed in E. coli), 2.87 Å**	7B6W	Data File Jmol Viewer 7B6W	Deluigi et al. (2022). Deluigi M, Morstein L, Schuster M, Klenk C, Merklinger L, Cridge RR, de Zhang LA, Klipp A, Vacca S, Vaid TM, Mittl PRE, Egloff P, Eberle SA, Zerbe O, Chalmers DK, Scott DJ, & Plückthun A (2022). Crystal structure of the α_1B-adrenergic receptor reveals molecular determinants of selective ligand recognition. Nat Commun 13 1:382. PubMed Id: 35046410. doi:10.1038/s41467-021-27911-3.
*α_2A adrenergic receptor in complex with an antagonist RSC: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.7 Å** Engineered protein. b₅₆₂RIL inserted in 3rd intracellular loop in complex with a partial agonist, 3.2 Å: 6KUY	6KUX	Data File Jmol Viewer 6KUX 6KUY	Qu et al. (2019). Qu L, Zhou Q, Xu Y, Guo Y, Chen X, Yao D, Han GW, Liu ZJ, Stevens RC, Zhong G, Wu D, & Zhao S (2019). Structural Basis of the Diversity of Adrenergic Receptors. Cell Rep 29 10:2929-2935.e4. PubMed Id: 31801060. doi:10.1016/j.celrep.2019.10.088.
*α_2A adrenergic receptor - G_oA complex with bound biased agonist 9087: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.47 Å** cryo-EM structure with bound biased agonist 4622, 3.40 Å: 7W7E	7W6P	Data File Jmol Viewer 7W6P 7W7E	Fink et al. (2022). Fink EA, Xu J, Hübner H, Braz JM, Seemann P, Avet C, Craik V, Weikert D, Schmidt MF, Webb CM, Tolmachova NA, Moroz YS, Huang XP, Kalyanaraman C, Gahbauer S, Chen G, Liu Z, Jacobson MP, Irwin JJ, Bouvier M, Du Y, Shoichet BK, Basbaum AI, & Gmeiner P (2022). Structure-based discovery of nonopioid analgesics acting through the α2A-adrenergic receptor. Science 377 6614:abn7065. PubMed Id: 36173843. doi:10.1126/science.abn7065.
*α_2B adrenergic receptor in complex with G_oA: Homo sapiens* E Eukaryota (expressed in Sf9 cells), 2.90 Å** cryo-EM structure in complex with G_i1, 4.1 Å: 6K42	6K41	Data File Jmol Viewer 6K41 6K42	Yuan et al. (2020). Yuan D, Liu Z, Kaindl J, Maeda S, Zhao J, Sun X, Xu J, Gmeiner P, Wang HW, & Kobilka BK (2020). Activation of the α_2B adrenoceptor by the sedative sympatholytic dexmedetomidine. Nat Chem Biol 16 5:507-512. PubMed Id: 32152538. doi:10.1038/s41589-020-0492-2.
*α_2C adrenergic receptor: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.8 Å** Engineered protein. Intracellular loop 3 residues 242-371 were replaced by a PGS fusion protein	6KUW	Data File Jmol Viewer 6KUW	Chen et al. (2019). Chen X, Xu Y, Qu L, Wu L, Han GW, Guo Y, Wu Y, Zhou Q, Sun Q, Chu C, Yang J, Yang L, Wang Q, Yuan S, Wang L, Hu T, Tao H, Sun Y, Song Y, Hu L, Liu ZJ, Stevens RC, Zhao S, Wu D, & Zhong G (2019). Molecular Mechanism for Ligand Recognition and Subtype Selectivity of ?2C Adrenergic Receptor. Cell Rep 29 10:2936-2943.e4. PubMed Id: 31801061. doi:10.1016/j.celrep.2019.10.112.
*β₁ adrenergic receptor (engineered): Meleagris gallopavo (turkey)* E Eukaryota (expressed in Trichoplusia ni), 2.7 Å**	2VT4	Data File Jmol Viewer 2VT4	Warne et al. (2008). Warne T, Serrano-Vega MJ, Baker JG, Moukhametzianov R, Edwards PC, Henderson R, Leslie AG, Tate CG, & Schertler GF (2008). Structure of a β₁-adrenergic G-protein-coupled receptor. Nature 454 :486-491. PubMed Id: 18594507.
*β₁ adrenergic receptor (engineered) with bound dobutamine: Meleagris gallopavo (turkey)* E Eukaryota (expressed in Trichoplusia ni), 2.50 Å** With bound dobutamine, 2.65 Å:2Y01 With bound carmoterol, 2.65 Å:2Y02 With bound isoprenaline, 2.85 Å:2Y03 With bound salbutamol, 3.05 Å:2Y04	2Y00	Data File Jmol Viewer 2Y00 2Y03 2Y01 2Y04 2Y02	Warne et al. (2011). Warne T, Moukhametzianov R, Baker JG, Nehmé R, Edwards PC, Leslie AG, Schertler GF, & Tate CG (2011). The structural basis for agonist and partial agonist action on a β₁-adrenergic G-protein-coupled receptor. Nature 469 :241-244. PubMed Id: 21228877.
*β₁ adrenergic receptor (engineered) with bound carazolol (t1118): Meleagris gallopavo (turkey)* E Eukaryota (expressed in Trichoplusia ni), 3.00 Å** With bound cyanopindolol (t148), 3.25 Å:2YCX With bound cyanopindolol (t468), 3.15 Å:2YCY With bound lodocyanopindolol (t756), 3.65 Å:2YCZ	2YCW	Data File Jmol Viewer 2YCW 2YCY 2YCZ 2YCX	Moukhametzianov et al. (2011). Moukhametzianov R, Warne T, Edwards PC, Serrano-Vega MJ, Leslie AG, Tate CG, & Schertler GF (2011). Two distinct conformations of helix 6 observed in antagonist-bound structures of a β₁-adrenergic receptor Proc Natl Acad Sci USA 108 :8228-8232. PubMed Id: 21540331. doi:10.1073/pnas.1100185108.
*β₁ adrenergic receptor (engineered) with bound carvedilol: Meleagris gallopavo (turkey)* E Eukaryota (expressed in Trichoplusia ni), 2.30 Å** With bound bucindolol, 3.20 Å:4AMI	4AMJ	Data File Jmol Viewer 4AMJ 4AMI	Warne et al. (2012). Warne T, Edwards PC, Leslie AG, & Tate CG (2012). Crystal Structures of a Stabilized ?₁-Adrenoceptor Bound to the Biased Agonists Bucindolol and Carvedilol. Structure 20 :841-849. PubMed Id: 22579251. doi:10.1016/j.str.2012.03.014.
*β₁ adrenergic receptor oligomer, basal state: Meleagris gallopavo* E Eukaryota (expressed in Trichoplusia ni), 3.50 Å**	4GPO	Data File Jmol Viewer 4GPO	Huang et al. (2013). Huang J, Chen S, Zhang JJ, & Huang XY (2013). Crystal structure of oligomeric β₁-adrenergic G protein-coupled receptors in ligand-free basal state. Nature Struc Mol Biol 20 :419-425. PubMed Id: 23435379. doi:10.1038/nsmb.2504.
*β₁adrenergic receptor (engineered) with bound agonist isoprenaline & Nb80 nanobody: Meleagris gallopavo* E Eukaryota (expressed in Trichoplusia ni), 2.8 Å** with bound dobutamine & nanobody Nb6B9, 2.7 Å: 6H7L with bound salbutamol and Nb6B9, 2.76 Å: 6H7M with bound cyanopindolol & Nb6B9, 2.8 Å: 6H7O	6H7J	Data File Jmol Viewer 6H7J 6H7L 6H7O 6H7M	Warne et al. (2019). Warne T, Edwards PC, Doré AS, Leslie AGW, & Tate CG (2019). Molecular basis for high-affinity agonist binding in GPCRs. Science 364 6442:775-778. PubMed Id: 31072904. doi:10.1126/science.aau5595.
*β₁ adrenoceptor with bound agonist formoterol coupled to arrestin-2 in lipid nanodisc: Meleagris gallopavo* E Eukaryota (expressed in Trichoplusia ni), 3.30 Å** cryo-EM structure Fomoterol-bound trx-β₁ (x-ray), 2.70 Å: 6IBL	6TKO	Data File Jmol Viewer 6TKO 6IBL	Lee et al. (2020). Lee Y, Warne T, Nehmé R, Pandey S, Dwivedi-Agnihotri H, Chaturvedi M, Edwards PC, García-Nafría J, Leslie AGW, Shukla AK, & Tate CG (2020). Molecular basis of β-arrestin coupling to formoterol-bound β1-adrenoceptor. Nature 583 7818:862-866. PubMed Id: 32555462. doi:10.1038/s41586-020-2419-1.
*β₁ adrenergic receptor-G_s-isoproterenol complex: Meleagris gallopavo* E Eukaryota (expressed in Spodoptera frugiperda), 2.60 Å** cryo-EM structure engineered protein. T4 lysozyme fused to N terminus.	7JJO	Data File Jmol Viewer 7JJO	Su et al. (2020). Su M, Zhu L, Zhang Y, Paknejad N, Dey R, Huang J, Lee MY, Williams D, Jordan KD, Eng ET, Ernst OP, Meyerson JR, Hite RK, Walz T, Liu W, & Huang XY (2020). Structural Basis of the Activation of Heterotrimeric Gs-Protein by Isoproterenol-Bound β₁-Adrenergic Receptor. Mol Cell 80 1:59-71.e4. PubMed Id: 32818430. doi:10.1016/j.molcel.2020.08.001.
*β₁ adrenergic receptor with bound isoproterenol in complex with heterotrimeric G_i protein: Meleagris gallopavo* E Eukaryota (expressed in Spodoptera frugiperda), 2.96 Å** cryo-EM structure in complex with heterotrimeric G_i/s protein, 3.86 Å 7S0G	7S0F	Data File Jmol Viewer 7S0F 7S0G	Alegre et al. (2021). Alegre KO, Paknejad N, Su M, Lou JS, Huang J, Jordan KD, Eng ET, Meyerson JR, Hite RK, & Huang XY (2021). Structural basis and mechanism of activation of two different families of G proteins by the same GPCR. Nat Struct Mol Biol 28 11:936-944. PubMed Id: 34759376. doi:10.1038/s41594-021-00679-2.
*β₁ adrenergic receptor bound to carazolol: Homo sapiens* E Eukaryota (expressed in sf9 cells), 2.50 Å** Engineered protein. See publication. bound to BI-167107 and nanobody 6B9, 2.60 Å: 7BU7 bound to norepinephrine and nanobody 6B9, 2.70 Å: 7BU6 bound to epinephrine and nanobody 6B9, 3.13 Å: 7BTS	7BVQ	Data File Jmol Viewer 7BVQ 7BU6 7BTS 7BU7	Xu et al. (2020). Xu X, Kaindl J, Clark MJ, Hübner H, Hirata K, Sunahara RK, Gmeiner P, Kobilka BK, & Liu X (2020). Binding pathway determines norepinephrine selectivity for the human β₁AR over β₂AR. Cell Res . PubMed Id: 33093660. doi:10.1038/s41422-020-00424-2.
*β₂ adrenergic receptor: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.4/3.7 Å** from β₂AR365-Fab5 complex. From β₂AR24/365-Fab5 complex: 2R4S	2R4R	Data File Jmol Viewer 2R4R 2R4S	Rasmussen et al. (2007). Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, Edwards PC, Burghammer M, Ratnala VR, Sanishvili R, Fischetti RF, Schertler GF, Weis WI, & Kobilka BK (2007). Crystal structure of the human β₂adrenergic G-protein-coupled receptor. Nature 450 :383-387. PubMed Id: 17952055.
*Methylated β₂ adrenergic receptor: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.4 Å** from β₂AR365-Fab5 complex.	3KJ6	Data File Jmol Viewer 3KJ6	Bokoch et al. (2010). Bokoch MP, Zou Y, Rasmussen SG, Liu CW, Nygaard R, Rosenbaum DM, Fung JJ, Choi HJ, Thian FS, Kobilka TS, Puglisi JD, Weis WI, Pardo L, Prosser RS, Mueller L, & Kobilka BK (2010). Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor. Nature 463 :108-112. PubMed Id: 20054398.
*β₂ adrenergic receptor (engineered): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.4 Å** T4 lysozyme replaces third intracellular loop. Reveals close association with cholesterol.	2RH1	Data File Jmol Viewer 2RH1	Cherezov et al. (2007). Cherezov V, Rosenbaum DM, Hanson MA, Rasmussen SG, Thian FS, Kobilka TS, Choi HJ, Kuhn P, Weis WI, Kobilka BK, & Stevens RC (2007). High-resolution crystal structure of an engineered human β₂-adrenergic G protein-coupled receptor. Science 318 :1258-1265. PubMed Id: 17962520.
*β₂ adrenergic receptor (engineered): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.8 Å** T4 lysozyme replaces third intracellular loop. Reveals specific cholesterol binding site.	3D4S	Data File Jmol Viewer 3D4S	Hanson et al. (2008). Hanson MA, Cherezov V, Griffith MT, Roth CB, Jaakola VP, Chien EY, Velasquez J, Kuhn P, & Stevens RC (2008). A Specific Cholesterol Binding Site Is Established by the 2.8 Å Structure of the Human β₂-Adrenergic Receptor. Structure 16 :897-905. PubMed Id: 18547522.
*β₂ adrenergic receptor (engineered) in complex with ICI 118,551: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.84 Å** T4 lysozyme replaces third intracellular loop. In complex with a 'novel inverse agonist', 2.84 Å: 3NY9 In complex with alprenolol, 3.16 Å: 3NYA	3NY8	Data File Jmol Viewer 3NY8 3NY9 3NYA	Wacker et al. (2010). Wacker D, Fenalti G, Brown MA, Katritch V, Abagyan R, Cherezov V, & Stevens RC (2010). Conserved binding mode of human β₂ adrenergic receptor inverse agonists and antagonist revealed by X-ray crystallography. J Am Chem Soc 132 :11443-11445. PubMed Id: 20669948. doi:10.1021/ja105108q.
*β₂ adrenergic receptor (engineered) in nanobody-stabilized active state: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.50 Å** T4 lysozyme replaces third intracellular loop. The nanobody Nb80 is an intact antigen-binding domain of a camelid heavy-chain antibody.	3P0G	Data File Jmol Viewer 3P0G	Rasmussen et al. (2011). Rasmussen SG, Choi HJ, Fung JJ, Pardon E, Casarosa P, Chae PS, Devree BT, Rosenbaum DM, Thian FS, Kobilka TS, Schnapp A, Konetzki I, Sunahara RK, Gellman SH, Pautsch A, Steyaert J, Weis WI, & Kobilka BK (2011). Crystal structure of the human β₂adrenergic G-protein-coupled receptor. Nature 469 :175-180. PubMed Id: 21228869.
*β₂ adrenergic receptor (engineered) with irreversibly-bound agonist: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.50 Å** T4 lysozyme replaces third intracellular loop. The agonist is covalently linked to the receptor by a disulphide bond.	3PDS	Data File Jmol Viewer 3PDS	Rosenbaum et al. (2011). Rosenbaum DM, Zhang C, Lyons JA, Holl R, Aragao D, Arlow DH, Rasmussen SG, Choi HJ, Devree BT, Sunahara RK, Chae PS, Gellman SH, Dror RO, Shaw DE, Weis WI, Caffrey M, Gmeiner P, Kobilka BK (2011). Structure and function of an irreversible agonist-β₂adrenoceptor complex. Nature 469 :236-240. PubMed Id: 21228876.
*β₂ adrenergic receptor-Gs protein complex: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.20 Å** The receptor is engineered; T4 lysozyme at the N-terminus. Nanobody-stabilized active state.	3SN6	Data File Jmol Viewer 3SN6	Rasmussen et al. (2011). Rasmussen SG, Devree BT, Zou Y, Kruse AC, Chung KY, Kobilka TS, Thian FS, Chae PS, Pardon E, Calinski D, Mathiesen JM, Shah ST, Lyons JA, Caffrey M, Gellman SH, Steyaert J, Skiniotis G, Weis WI, Sunahara RK, & Kobilka BK (2011). Crystal structure of the β₂ adrenergic receptor-Gs protein complex. Nature 477 :549-555. PubMed Id: 21772288. doi:10.1038/nature10361.
*β₂ adrenergic receptor (engineered): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.99 Å** T4 lysozyme fused at N-terminal.	4GBR	Data File Jmol Viewer 4GBR	Zou et al. (2012). Zou Y, Weis WI, & Kobilka BK (2012). N-terminal T4 lysozyme fusion facilitates crystallization of a G protein coupled receptor. PLoS ONE 7 10:e46039. PubMed Id: 23056231. doi:10.1371/journal.pone.0046039.
*β₂ adrenergic receptor with a bound positive allosteric modulator: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.2 Å** engineered protein; T4 lysozyme fused at N-terminal	6N48	Data File Jmol Viewer 6N48	Liu et al. (2019). Liu X, Masoudi A, Kahsai AW, Huang LY, Pani B, Staus DP, Shim PJ, Hirata K, Simhal RK, Schwalb AM, Rambarat PK, Ahn S, Lefkowitz RJ, & Kobilka B (2019). Mechanism of β₂ adrenergic receptor regulation by an intracellular positive allosteric modulator. Science 364 6447:1283-1287. PubMed Id: 31249059. doi:10.1126/science.aaw8981.
*β₂ adrenergic receptor fused to a Gs peptide: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.7 Å** engineered protein:T4 lysozyme & Gs inserted in intracellular loop 3 GDP-bound Gs heterotrimer, 2.8 Å: 6EG8	6E67	Data File Jmol Viewer 6E67 6EG8	Liu et al. (2019). Liu X, Xu X, Hilger D, Aschauer P, Tiemann JKS, Du Y, Liu H, Hirata K, Sun X, Guixà-González R, Mathiesen JM, Hildebrand PW, & Kobilka BK (2019). Structural Insights into the Process of GPCR-G Protein Complex Formation. Cell 177 5:1243-1251.e12. PubMed Id: 31080070. doi:10.1016/j.cell.2019.04.021.
*β₂ adrenergic receptor with bound alprenolol: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.8 Å** XFEL structures using transient ligand exchange starting with timolol or alprenolol. with bound carazolol, 3.4 Å: 6PS0 with bound timolol, 3.2 Å: 6PS1 with bound alprenolol, 2.4 Å: 6SP2 with bound carvedilol, 2.5 Å: 6PS3 with bound ICI-118551, 2.6 Å: 6PS4 with bound propranolol, 2.9 Å: 6PS5 with bound timolol, 2.7 Å: 6PS6	6PRZ	Data File Jmol Viewer 6PRZ 6PS3 6PS6 6PS4 6SP2 6PS5 6PS1 6PS0	Ishchenko et al. (2019). Ishchenko A, Stauch B, Han GW, Batyuk A, Shiriaeva A, Li C, Zatsepin N, Weierstall U, Liu W, Nango E, Nakane T, Tanaka R, Tono K, Joti Y, Iwata S, Moraes I, Gati C, & Cherezov V (2019). Toward G protein-coupled receptor structure-based drug design using X-ray lasers. IUCrJ 6 :1106-1119. PubMed Id: 31709066. doi:10.1107/S2052252519013137.
*β₂V₂R-Gs protein subcomplex of a GPCR-G protein-beta-arrestin mega-complex: Homo sapiens* E Eukaryota (expressed in sf-9 cells), 3.8 Å** cryo-EM structure Stabilized beta-arrestin 1-V₂T subcomplex, 4 Å: 6NI2	6NI3	Data File Jmol Viewer 6NI3 6NI2	Nguyen et al. (2019). Nguyen AH, Thomsen ARB, Cahill TJ 3rd, Huang R, Huang LY, Marcink T, Clarke OB, Heissel S, Masoudi A, Ben-Hail D, Samaan F, Dandey VP, Tan YZ, Hong C, Mahoney JP, Triest S, Little J 4th, Chen X, Sunahara R, Steyaert J, Molina H, Yu Z, des Georges A, & Lefkowitz RJ (2019). Structure of an endosomal signaling GPCR-G protein-?-arrestin megacomplex. Nat Struct Mol Biol 26 12:1123-1131. PubMed Id: 31740855. doi:10.1038/s41594-019-0330-y.
*β₂ adrenergic receptor with bound allosteric modulator AS408: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.10 Å** engineered protein: T4 lysozyme replaces third intracellular loop	6OBA	Data File Jmol Viewer 6OBA	Liu et al. (2020). Liu X, Kaindl J, Korczynska M, Stößel A, Dengler D, Stanek M, Hübner H, Clark MJ, Mahoney J, Matt RA, Xu X, Hirata K, Shoichet BK, Sunahara RK, Kobilka BK, & Gmeiner P (2020). An allosteric modulator binds to a conformational hub in the β₂ adrenergic receptor. Nat Chem Biol 16 7:749-755. PubMed Id: 32483378. doi:10.1038/s41589-020-0549-2.
*β₂ adrenergic receptor with bound formoterol and G_s protein: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.82 Å** cryo-EM structure	7BZ2	Data File Jmol Viewer 7BZ2	Zhang et al. (2020). Zhang Y, Yang F, Ling S, Lv P, Zhou Y, Fang W, Sun W, Zhang L, Shi P, & Tian C (2020). Single-particle cryo-EM structural studies of the β₂AR-Gs complex bound with a full agonist formoterol. Cell Discov 6 . PubMed Id: 32655881. doi:10.1038/s41421-020-0176-9.
*β₂ adrenergic receptor with bound carazolol and Cmpd-15: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.7 Å** Engineered protein. T4 lysozyme replaces most of 3rd intracellular loop.	5X7D	Data File Jmol Viewer 5X7D	Liu et al. (2017). Liu X, Ahn S, Kahsai AW, Meng KC, Latorraca NR, Pani B, Venkatakrishnan AJ, Masoudi A, Weis WI, Dror RO, Chen X, Lefkowitz RJ, & Kobilka BK (2017). Mechanism of intracellular allosteric β₂AR antagonist revealed by X-ray crystal structure. Nature 548 :480-484. PubMed Id: 28813418. doi:10.1038/nature23652.
*β₂ adrenergic receptor in full agonist-bound state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), NMR structure**	6KR8	Data File Jmol Viewer 6KR8	Imai et al. (2020). Imai S, Yokomizo T, Kofuku Y, Shiraishi Y, Ueda T, & Shimada I (2020). Structural equilibrium underlying ligand-dependent activation of ?₂-adrenoreceptor. Nat Chem Biol 16 4:430-439. PubMed Id: 31959965. doi:10.1038/s41589-019-0457-5.
*β₂ adrenergic receptor - modified BRIL (mBRIL) construct with bound partial agonist formoterol: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure with bound full agonist olodaterol, 3.20 Å: 8JJL with bound antagonist alprenolol, 3.40 Å: 8JJO	8JJ8	Data File Jmol Viewer 8JJ8 8JJL 8JJO	Guo et al. (2024). Guo Q, He B, Zhong Y, Jiao H, Ren Y, Wang Q, Ge Q, Gao Y, Liu X, Du Y, Hu H, & Tao Y (2024). A method for structure determination of GPCRs in various states. Nat Chem Biol 20 1:74-82. PubMed Id: 37580554. doi:10.1038/s41589-023-01389-0.
*β₃ adrenergic receptor: Canis lupus familiaris* E Eukaryota (expressed in Spodoptera frugiperda), 3.16 Å** cryo-EM structure	7DH5	Data File Jmol Viewer 7DH5	Nagiri et al. (2021). Nagiri C, Kobayashi K, Tomita A, Kato M, Kobayashi K, Yamashita K, Nishizawa T, Inoue A, Shihoya W, & Nureki O (2021). Cryo-EM structure of the β3-adrenergic receptor reveals the molecular basis of subtype selectivity. Mol Cell 81 15:3205-3215. PubMed Id: 34314699. doi:10.1016/j.molcel.2021.06.024.
*A₁ adenosine receptor: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.2 Å** Engineered protein. b₅₆₂ (BRIL) inserted into the third intracellular loop between residues 211 & 220.	5UEN	Data File Jmol Viewer 5UEN	Glukhova et al. (2017). Glukhova A, Thal DM, Nguyen AT, Vecchio EA, Jörg M, Scammells PJ, May LT, Sexton PM, & Christopoulos A (2017). Structure of the Adenosine A₁ Receptor Reveals the Basis for Subtype Selectivity. Cell 168 :867-877.e13. PubMed Id: 28235198. doi:10.1016/j.cell.2017.01.042.
*A₁ adenosine receptor in complex with G_i2: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.6 Å** cryo-EM structure	6D9H	Data File Jmol Viewer 6D9H	Draper-Joyce et al. (2018). Draper-Joyce CJ, Khoshouei M, Thal DM, Liang YL, Nguyen ATN, Furness SGB, Venugopal H, Baltos JA, Plitzko JM, Danev R, Baumeister W, May LT, Wootten D, Sexton PM, Glukhova A, & Christopoulos A (2018). Structure of the adenosine-bound human adenosine A₁ receptor-G_i complex. Nature 558 7711:559-563. PubMed Id: 29925945. doi:10.1038/s41586-018-0236-6.
*A₁ adenosine receptor in complex with PSB36: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.3 Å** Engineered protein: Apocytochrome b₅₆₂ replaces loop 3 of wild-type protein	5N2S	Data File Jmol Viewer 5N2S	Cheng et al. (2017). Cheng RKY, Segala E, Robertson N, Deflorian F, Doré AS, Errey JC, Fiez-Vandal C, Marshall FH, & Cooke RM (2017). Structures of Human A1 and A2A Adenosine Receptors with Xanthines Reveal Determinants of Selectivity. Structure 25 :1275-1285.e4. PubMed Id: 28712806. doi:10.1016/j.str.2017.06.012.
*A₁ adenosine receptor - G_i2-protein complex with endogenous agonist and an allosteric ligand: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.20 Å** cryo-EM structure bound to its endogenous agonist, 3.30 Å 7LD4	7LD3	Data File Jmol Viewer 7LD3 7LD4	Draper-Joyce et al. (2021). Draper-Joyce CJ, Bhola R, Wang J, Bhattarai A, Nguyen ATN, Cowie-Kent I, O'Sullivan K, Chia LY, Venugopal H, Valant C, Thal DM, Wootten D, Panel N, Carlsson J, Christie MJ, White PJ, Scammells P, May LT, Sexton PM, Danev R, Miao Y, Glukhova A, Imlach WL, & Christopoulos A (2021). Positive allosteric mechanisms of adenosine A₁ receptor-mediated analgesia. Nature 597 7877:571-576. PubMed Id: 34497422. doi:10.1038/s41586-021-03897-2.
*A_2A adenosine receptor: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.6 Å** In complex with a high-affinity subtype-selective antagonist ZM241385. Engineered protein: T4 lysozyme inserted between TM helices V and VI.	3EML	Data File Jmol Viewer 3EML	Jaakola et al. (2008). Jaakola VP, Griffith MT, Hanson MA, Cherezov V, Chien EY, Lane JR, Ijzerman AP, & Stevens RC (2008). The 2.6 Angstrom Crystal Structure of a Human A_2AAdenosine Receptor Bound to an Antagonist. Science 322 :1211-1217. PubMed Id: 18832607.
*A_2A adenosine receptor with bound agonist (UK-432097): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.71 Å** Reveals structural changes in helices III, V, & VI relative to inactive, antagonist-bound form. Engineered protein: T4 lysozyme inserted between TM helices V and VI.	3QAK	Data File Jmol Viewer 3QAK	Xu et al. (2011). Xu F, Wu H, Katritch V, Han GW, Jacobson KA, Gao ZG, Cherezov V, & Stevens RC (2011). Structure of an agonist-bound human A_2A adenosine receptor Science 332 :322-327. PubMed Id: 21393508. doi:10.1126/science.1202793.
*A_2A adenosine receptor (engineered) with bound adenosine: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.00 Å** With synthetic agonist NECA, 2.6 Å:2YDV	2YDO	Data File Jmol Viewer 2YDO 2YDV	Lebon et al. (2011). Lebon G, Warne T, Edwards PC, Bennett K, Langmead CJ, Leslie AG, & Tate CG (2011). Agonist-bound adenosine A_2A receptor structures reveal common features of GPCR activation Nature 474 :521-525. PubMed Id: 21593763. doi:10.1038/nature10136.
*A_2A adenosine receptor in complex with caffeine: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.60 Å** Engineered protein, designated A_2A-StaR2: A54L, T88A, R107A, K122A, L202A, L235A, V239A, S277A In complex with ZM241385, 3.30 Å: 3PWH In complex with XAC, 3.31 Å: 3REY	3RFM	Data File Jmol Viewer 3RFM 3REY 3PWH	Doré et al. (2011). Doré AS, Robertson N, Errey JC, Ng I, Hollenstein K, Tehan B, Hurrell E, Bennett K, Congreve M, Magnani F, Tate CG, Weir M, & Marshall FH (2011). Structure of the Adenosine A_2A Receptor in Complex with ZM241385 and the Xanthines XAC and Caffeine. Structure 19 :1283-1293. PubMed Id: 21885291. doi:10.1016/j.str.2011.06.014.
*A_2A adenosine receptor in complex inverse-agonist antibody: Homo sapiens* E Eukaryota (expressed in Pichia pastoris), 2.70 Å** The structure was determined with bound mouse Fab2838 in the presence of the antagonist ZM241385. High-occupancy ZM241385 structure, 3.10 Å: 3VGA	3VG9	Data File Jmol Viewer 3VG9 3VGA	Hino et al. (2012). Hino T, Arakawa T, Iwanari H, Yurugi-Kobayashi T, Ikeda-Suno C, Nakada-Nakura Y, Kusano-Arai O, Weyand S, Shimamura T, Nomura N, Cameron AD, Kobayashi T, Hamakubo T, Iwata S, & Murata T (2012). G-protein-coupled receptor inactivation by an allosteric inverse-agonist antibody. Nature 482 :237-240. PubMed Id: 22286059. doi:10.1038/nature10750.
*A_2A adenosine receptor in complex with ZM241385: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 1.80 Å** Engineered protein: Apocytochrome b₅₆₂ replaces loop 3 of wild-type protein. Structure reveals stabilizing cholesterol molecules, 23 ordered lipids, and 57 ordered waters.	4EIY	Data File Jmol Viewer 4EIY	Liu et al. (2012). Liu W, Chun E, Thompson AA, Chubukov P, Xu F, Katritch V, Han GW, Roth CB, Heitman LH, IJzerman AP, Cherezov V, & Stevens RC (2012). Structural basis for allosteric regulation of GPCRs by sodium ions. Science 337 :232-236. PubMed Id: 22798613. doi:10.1126/science.1219218.
*A_2A adenosine receptor (engineered) with bound CGS21680 (P2₁): Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.60 Å** P212121 space group, 2.60 Å: 4UG2	4UHR	Data File Jmol Viewer 4UHR 4UG2	Lebon et al. (2015). Lebon G, Edwards PC, Leslie AG, & Tate CG (2015). Molecular Determinants of CGS21680 Binding to the Human Adenosine A2A Receptor. Mol Pharmacol 87 :907-915. PubMed Id: 25762024. doi:10.1124/mol.114.097360.
*A_2A adenosine receptor with bound engineered G protein: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.4 Å**	5G53	Data File Jmol Viewer 5G53	Carpenter et al. (2016). Carpenter B, Nehmé R, Warne T, Leslie AG, & Tate CG (2016). Structure of the adenosine A_2A receptor bound to an engineered G protein. Nature 536 :104-107. PubMed Id: 27462812. doi:10.1038/nature18966.
*A2A adenosine receptor by by serial millisecond crystallography (SMC): Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.14 Å** by serial femtosecond crystallography (SFX), 1.70 Å: 5NM4 by cryo-EM, 1.95 Å: 5NM2	5NLX	Data File Jmol Viewer 5NLX 5NM2 5NM4	Weinert et al. (2017). Weinert T, Olieric N, Cheng R, Brünle S, James D, Ozerov D, Gashi D, Vera L, Marsh M, Jaeger K, Dworkowski F, Panepucci E, Basu S, Skopintsev P, Doré AS, Geng T, Cooke RM, Liang M, Prota AE, Panneels V, Nogly P, Ermler U, Schertler G, Hennig M, Steinmetz MO, Wang M, & Standfuss J (2017). Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons. Nat Commun 8 1:542. PubMed Id: 28912485. doi:10.1038/s41467-017-00630-4.
*A_2A adenosine receptor with bound miniGs heterotrimer: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 4.11 Å** cryo-EM structure	6GDG	Data File Jmol Viewer 6GDG	García-Nafría et al. (2018). García-Nafría J, Lee Y, Bai X, Carpenter B, & Tate CG (2018). Cryo-EM structure of the adenosine A_2A receptor coupled to an engineered heterotrimeric G protein. Elife 7 . PubMed Id: 29726815. doi:10.7554/eLife.35946.
*A_2A adenosine receptor with bound ZM241385: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 1.85 Å** XFEL structure using transient ligand exchange starting with LUF5843. See also 6PRZ	6PS7	Data File Jmol Viewer 6PS7	Ishchenko et al. (2019). Ishchenko A, Stauch B, Han GW, Batyuk A, Shiriaeva A, Li C, Zatsepin N, Weierstall U, Liu W, Nango E, Nakane T, Tanaka R, Tono K, Joti Y, Iwata S, Moraes I, Gati C, & Cherezov V (2019). Toward G protein-coupled receptor structure-based drug design using X-ray lasers. IUCrJ 6 :1106-1119. PubMed Id: 31709066. doi:10.1107/S2052252519013137.
*A_2A adenosine receptor in complex with ZM241385: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.25 Å** Structure obtained from SFX experiments under atmospheric pressure.	6JZH	Data File Jmol Viewer 6JZH	Shimazu et al. (2019). Shimazu Y, Tono K, Tanaka T, Yamanaka Y, Nakane T, Mori C, Terakado Kimura K, Fujiwara T, Sugahara M, Tanaka R, Doak RB, Shimamura T, Iwata S, Nango E, & Yabashi M (2019). High-viscosity sample-injection device for serial femtosecond crystallography at atmospheric pressure. J Appl Crystallogr 52 :1280-1288. PubMed Id: 31798359. doi:10.1107/S1600576719012846.
*A_2A adenosine receptor with SRP2070_Fab complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.40 Å** Engineered protein: Apocytochrome b₅₆₂ (BRIL) replaces loop 3 of wild-type protein	7C6A	Data File Jmol Viewer 7C6A	Miyagi et al. (2020). Miyagi H, Asada H, Suzuki M, Takahashi Y, Yasunaga M, Suno C, Iwata S, & Saito JI (2020). The discovery of a new antibody for BRIL-fused GPCR structure determination. Sci Rep 10 1:11669. PubMed Id: 32669569. doi:10.1038/s41598-020-68355-x.
*A_2A adenosine receptor with bound UK432097, D52N mutant: Homo sapiens* E Eukaryota (expressed in P. pastoris), 2.60 Å** S91A mutant, 2.90 Å: 5WF6 Engineered protein: T4 lysozyme inserted between TM helices V and VI	5WF5	Data File Jmol Viewer 5WF5 5WF6	White et al. (2018). White KL, Eddy MT, Gao ZG, Han GW, Lian T, Deary A, Patel N, Jacobson KA, Katritch V, & Stevens RC (2018). Structural Connection between Activation Microswitch and Allosteric Sodium Site in GPCR Signaling. Structure 26 :259-269.e5. PubMed Id: 29395784. doi:10.1016/j.str.2017.12.013.
*A_2A adenosine receptor in complex with theophylline: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.0 Å** Engineered protein: Apocytochrome b₅₆₂ replaces loop 3 of wild-type protein in complex with caffeine, 2.1 Å: 5MZP in complex with PSB36, 2.8 Å: 5N2R	5MZJ	Data File Jmol Viewer 5MZJ 5MZP 5N2R	Cheng et al. (2017). Cheng RKY, Segala E, Robertson N, Deflorian F, Doré AS, Errey JC, Fiez-Vandal C, Marshall FH, & Cooke RM (2017). Structures of Human A1 and A2A Adenosine Receptors with Xanthines Reveal Determinants of Selectivity. Structure 25 :1275-1285.e4. PubMed Id: 28712806. doi:10.1016/j.str.2017.06.012.
*A_2A adenosine receptor in complex with Chromone 4d: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 1.92 Å** engineered protein: Apocytochrome bRIL₅₆₂ in intracellular loop 3. in complex with Chromone 5d, 2.13 Å: 6ZDV	6ZDR	Data File Jmol Viewer 6ZDR 6ZDV	Jespers et al. (2020). Jespers W, Verdon G, Azuaje J, Majellaro M, Keränen H, García-Mera X, Congreve M, Deflorian F, de Graaf C, Zhukov A, Doré AS, Mason JS, Åqvist J, Cooke RM, Sotelo E, & Gutiérrez-de-Terán H (2020). X-Ray Crystallography and Free Energy Calculations Reveal the Binding Mechanism of A2A Adenosine Receptor Antagonists. Angew Chem Int Ed Engl 59 :16536-16543. PubMed Id: 32542862. doi:10.1002/anie.202003788.
*A_2A adenosine receptor, structure using XFEL-SFX diffraction: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.0 Å**	6WQA	Data File Jmol Viewer 6WQA	Lee et al. (2020). Lee MY, Geiger J, Ishchenko A, Han GW, Barty A, White TA, Gati C, Batyuk A, Hunter MS, Aquila A, Boutet S, Weierstall U, Cherezov V, & Liu W (2020). Harnessing the power of an X-ray laser for serial crystallography of membrane proteins crystallized in lipidic cubic phase. IUCrJ 7 :976-984. PubMed Id: 33209312. doi:10.1107/S2052252520012701.
*A_2A adenosine receptor in EROCOC17+4, LCP-SFX at 293 K: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 1.80 Å** at 277 K, 1.80 Å: 6LPJ at 100 K, 2.00 Å: 6LPL	6LPK	Data File Jmol Viewer 6LPK 6LPL 6LPJ	Ihara et al. (2020). Ihara K, Hato M, Nakane T, Yamashita K, Kimura-Someya T, Hosaka T, Ishizuka-Katsura Y, Tanaka R, Tanaka T, Sugahara M, Hirata K, Yamamoto M, Nureki O, Tono K, Nango E, Iwata S, & Shirouzu M (2020). Isoprenoid-chained lipid EROCOC17+4: a new matrix for membrane protein crystallization and a crystal delivery medium in serial femtosecond crystallography. Sci Rep 10 1:19305. PubMed Id: 33168855. doi:10.1038/s41598-020-76277-x.
*A_2A adenosine receptor with bound nonriboside partial agonist: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.12 Å** Engineered protein. Nine thermo-stabilizing mutations. Apocytochrome b₅₆₂ inserted in 3rd intracellular loop.	7ARO	Data File Jmol Viewer 7ARO	Amelia et al. (2021). Amelia T, van Veldhoven JPD, Falsini M, Liu R, Heitman LH, van Westen GJP, Segala E, Verdon G, Cheng RKY, Cooke RM, van der Es D, & IJzerman AP (2021). Crystal Structure and Subsequent Ligand Design of a Nonriboside Partial Agonist Bound to the Adenosine A_2A Receptor. J Med Chem 64 7:3827-3842. PubMed Id: 33764785. doi:10.1021/acs.jmedchem.0c01856.
*A_2A adenosine receptor with bound ZM241385: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.79 Å** microED structure	7RM5	Data File Jmol Viewer 7RM5	Martynowycz et al. (2021). Martynowycz MW, Shiriaeva A, Ge X, Hattne J, Nannenga BL, Cherezov V, & Gonen T (2021). MicroED structure of the human adenosine receptor determined from a single nanocrystal in LCP. Proc Natl Acad Sci U S A 118 36:e2106041118. PubMed Id: 34462357. doi:10.1073/pnas.2106041118.
*A_2A adenosine receptor (S91K mutant) in complex with preladenant conjugate PSB-2113: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.25 Å** in complex with preladenant conjugate PSB-2115, 2.60 Å 7PYR	7PX4	Data File Jmol Viewer 7PX4 7PYR	Claff et al. (2022). Claff T, Klapschinski TA, Tiruttani Subhramanyam UK, Vaaβen VJ, Schlegel JG, Vielmuth C, Voß JH, Labahn J, & Müller CE (2022). Single Stabilizing Point Mutation Enables High-Resolution Co-Crystal Structures of the Adenosine A2A Receptor with Preladenant Conjugates. Angew Chem Int Ed Engl :e202115545. PubMed Id: 35174942. doi:10.1002/anie.202115545.
*A_2A adenosine receptor, I92N mutant: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.80 Å** engineered protein: Apocytochrome bRIL₅₆₂ in intracellular loop 3.	7EZC	Data File Jmol Viewer 7EZC	Cui et al. (2022). Cui M, Zhou Q, Xu Y, Weng Y, Yao D, Zhao S, & Song G (2022). Crystal structure of a constitutive active mutant of adenosine A_2A receptor. IUCrJ 9 :333-341. PubMed Id: 35546802. doi:10.1107/S2052252522001907.
*A_2A adenosine receptor with ZM241385_Fab complex: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure	7T32	Data File Jmol Viewer 7T32	Zhang et al. (2022). Zhang K, Wu H, Hoppe N, Manglik A, & Cheng Y (2022). Fusion protein strategies for cryo-EM study of G protein-coupled receptors. Nat Commun 13 1:4366. PubMed Id: 35902590. doi:10.1038/s41467-022-32125-2.
*A_2A adenosine receptor in complex with LJ-4517, A_2AAR-StaR2-S277-bRIL construct: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.80 Å** A_2AAR-StaR2-A277-bRIL construct, 2.05 Å: 8CU7	8CU6	Data File Jmol Viewer 8CU6 8CU7	Shiriaeva et al. (2022). Shiriaeva A, Park D, Kim G, Lee Y, Hou X, Jarhad DB, Kim G, Yu J, Hyun YE, Kim W, Gao ZG, Jacobson KA, Han GW, Stevens RC, Jeong LS, Choi S, & Cherezov V (2022). GPCR Agonist-to-Antagonist Conversion: Enabling the Design of Nucleoside Functional Switches for the A2A Adenosine Receptor. J Med Chem 65 17:11648-11657. PubMed Id: 35977382. doi:10.1021/acs.jmedchem.2c00462.
*A_2A adenosine receptor, A_2AAR-StaR2-bRIL construct, native-SAD structure determined at wavelength 2.75 Å: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.40 Å** X-Ray structure	8PWN	Data File Jmol Viewer 8PWN	El Omari et al. (2023). El Omari K, Duman R, Mykhaylyk V, Orr CM, Latimer-Smith M, Winter G, Grama V, Qu F, Bountra K, Kwong HS, Romano M, Reis RI, Vogeley L, Vecchia L, Owen CD, Wittmann S, Renner M, Senda M, Matsugaki N, Kawano Y, Bowden TA, Moraes I, Grimes JM, Mancini EJ, Walsh MA, Guzzo CR, Owens RJ, Jones EY, Brown DG, Stuart DI, Beis K, & Wagner A (2023). Experimental phasing opportunities for macromolecular crystallography at very long wavelengths. Commun Chem 6 1:219. PubMed Id: 37828292. doi:10.1038/s42004-023-01014-0.
*A_2A adenosine receptor in complex with KW-6356: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.30 Å** in complex with istradefylline (expressed in K. pastrois), 3.20 Å: 8GNG	8GNE	Data File Jmol Viewer 8GNE 8GNG	Ohno et al. (2023). Ohno Y, Suzuki M, Asada H, Kanda T, Saki M, Miyagi H, Yasunaga M, Suno C, Iwata S, Saito JI, & Uchida S (2023). In Vitro Pharmacological Profile of KW-6356, a Novel Adenosine A2A Receptor Antagonist/Inverse Agonist. Mol Pharmacol 103 6:311-324. PubMed Id: 36894319. doi:10.1124/molpharm.122.000633.
*A_2A adenosine receptor in complex with photoresponsive ligand photoNECA (blue): Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.34 Å** X-ray structure	8WDT	Data File Jmol Viewer 8WDT	Araya et al. (2023). Araya T, Matsuba Y, Suzuki H, Doura T, Nuemket N, Nango E, Yamamoto M, Im D, Asada H, Kiyonaka S, & Iwata S (2023). Crystal structure reveals the binding mode and selectivity of a photoswitchable ligand for the adenosine A2A receptor. Biochem Biophys Res Commun 695 :149393. PubMed Id: 38171234. doi:10.1016/j.bbrc.2023.149393.
*A_2A adenosine receptor in 7.10 monoacylglycerol (MAG): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.37 Å** X-ray structure	8RQQ	Data File Jmol Viewer 8RQQ	Krawinski et al. (2024). Krawinski P, Smithers L, van Dalsen L, Boland C, Ostrovitsa N, Pérez J, & Caffrey M (2024). 7.10 MAG. A Novel Host Monoacylglyceride for In Meso (Lipid Cubic Phase) Crystallization of Membrane Proteins. Cryst Growth Des 24 7:2985-3001. PubMed Id: 38585376. doi:10.1021/acs.cgd.4c00087.
*A_2B adenosine receptor - G_s complex with bound BAY 60-6583: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.87 Å** cryo-EM structure with bound adenosine, 3.20 Å: 8HDP	8HDO	Data File Jmol Viewer 8HDO 8HDP	Cai et al. (2022). Cai H, Xu Y, Guo S, He X, Sun J, Li X, Li C, Yin W, Cheng X, Jiang H, Xu HE, Xie X, & Jiang Y (2022). Structures of adenosine receptor A2BR bound to endogenous and synthetic agonists. Cell Discov 8 1:140. PubMed Id: 36575181. doi:10.1038/s41421-022-00503-1.
*CXCR1 chemokine receptor in phospholipid bilayers: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure**	2LNL	Data File Jmol Viewer 2LNL	Park et al. (2012). Park SH, Das BB, Casagrande F, Tian Y, Nothnagel HJ, Chu M, Kiefer H, Maier K, De Angelis AA, Marassi FM, & Opella SJ (2012). Structure of the chemokine receptor CXCR1 in phospholipid bilayers. Nature 491 :779-783. PubMed Id: 23086146. doi:10.1038/nature11580.
*CXCR1 chemokine receptor - G_i complex with bound CXCL8: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.41 Å** cryo-EM structure	8IC0	Data File Jmol Viewer 8IC0	Ishimoto et al. (2023). Ishimoto N, Park JH, Kawakami K, Tajiri M, Mizutani K, Akashi S, Tame JRH, Inoue A, & Park SY (2023). Structural basis of CXC chemokine receptor 1 ligand binding and activation. Nat Commun 14 1:4107. PubMed Id: 37433790. doi:10.1038/s41467-023-39799-2.
*CXCR2 chemokine receptor - G_i complex with bound CXCL8: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.40 Å** cryo-EM structure dimer in complex with G_i, 3.50 Å: 6LFM CXCR2-00767013, by x-ray, 3.20 Å: 6LFL	6LFO	Data File Jmol Viewer 6LFO 6LFM 6LFL	Liu et al. (2020). Liu K, Wu L, Yuan S, Wu M, Xu Y, Sun Q, Li S, Zhao S, Hua T, & Liu ZJ (2020). Structural basis of CXC chemokine receptor 2 activation and signalling. Nature . PubMed Id: 32610344. doi:10.1038/s41586-020-2492-5.
*CCR1 Chemokine receptor-G_i complex, apo form: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure with bound CCL15 (26-92), 2.60 Å 7VL9 with bound CCL15 (27-92), 2.70 Å 7VLA	7VL8	Data File Jmol Viewer 7VL8 7VLA 7VL9	Shao et al. (2022). Shao Z, Shen Q, Yao B, Mao C, Chen LN, Zhang H, Shen DD, Zhang C, Li W, Du X, Li F, Ma H, Chen ZH, Xu HE, Ying S, Zhang Y, & Shen H (2022). Identification and mechanism of G protein-biased ligands for chemokine receptor CCR1. Nat Chem Biol 18 3:264-271. PubMed Id: 34949837. doi:10.1038/s41589-021-00918-z.
*CCR2 Chemokine receptor with ortho- and allosteric antagonists: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.81 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI.	5T1A	Data File Jmol Viewer 5T1A	Zheng et al. (2016). Zheng Y, Qin L, Zacarías NV, de Vries H, Han GW, Gustavsson M, Dabros M, Zhao C, Cherney RJ, Carter P, Stamos D, Abagyan R, Cherezov V, Stevens RC, IJzerman AP, Heitman LH, Tebben A, Kufareva I, & Handel TM (2016). Structure of CC chemokine receptor 2 with orthosteric and allosteric antagonists. Nature 540 :458-461. PubMed Id: 27926736. doi:10.1038/nature20605.
*CCR2 Chemokine receptor-G_i complex with bound CCL2: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.90 Å** cryo-EM structure	7XA3	Data File Jmol Viewer 7XA3	Shao et al. (2022). Shao Z, Tan Y, Shen Q, Hou L, Yao B, Qin J, Xu P, Mao C, Chen LN, Zhang H, Shen DD, Zhang C, Li W, Du X, Li F, Chen ZH, Jiang Y, Xu HE, Ying S, Ma H, Zhang Y, & Shen H (2022). Molecular insights into ligand recognition and activation of chemokine receptors CCR2 and CCR3. Cell Discov 8 1:44. PubMed Id: 35570218. doi:10.1038/s41421-022-00403-4.
*CCR2A Chemokine receptor, full length in complex with MK-0812: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.3 Å** Engineered protein. N-term residues 1-28 and C-term residues 322-374 removed. Rubredoxin inserted into intracellular loop 3. ΔN.C form in complex with MK-0812, 2.7 Å: 6GPX	6GPS	Data File Jmol Viewer 6GPS 6GPX	Apel et al. (2019). Apel AK, Cheng RKY, Tautermann CS, Brauchle M, Huang CY, Pautsch A, Hennig M, Nar H, & Schnapp G (2019). Crystal Structure of CC Chemokine Receptor 2A in Complex with an Orthosteric Antagonist Provides Insights for the Design of Selective Antagonists. Structure 27 3:427-438.e5. PubMed Id: 30581043. doi:10.1016/j.str.2018.10.027.
*CCR3 Chemokine receptor-G_i complex: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.10 Å** cryo-EM structure	7X9Y	Data File Jmol Viewer 7X9Y	Shao et al. (2022). Shao Z, Tan Y, Shen Q, Hou L, Yao B, Qin J, Xu P, Mao C, Chen LN, Zhang H, Shen DD, Zhang C, Li W, Du X, Li F, Chen ZH, Jiang Y, Xu HE, Ying S, Ma H, Zhang Y, & Shen H (2022). Molecular insights into ligand recognition and activation of chemokine receptors CCR2 and CCR3. Cell Discov 8 1:44. PubMed Id: 35570218. doi:10.1038/s41421-022-00403-4.
*Atypical chemokine receptor 3 (ACKR3) in complex with chemokine CXCL12, intracellular Fab, and extracellular Fab: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.80 Å** cryo-EM structure in complex with chemokine mutant CXCL12_LRHQ, intracellular Fab, and extracellular Fab, 3.30 Å: 7SK4 in complex with chemokine CXCL12 and intracellular Fab, 4.00 Å: 7SK5 in complex with chemokine mutant CXCL12_LRHQ and intracellular Fab, 4.00 Å: 7SK6 in complex with chemokine CXCL12, partial agonist CCX662, and extracellular Fab, 3.30 Å: 7SK7 in complex with chemokine CXCL12, partial agonist CCX662, intracellular Fab, and extracellular Fab, 3.30 Å: 7SK8	7SK3	Data File Jmol Viewer 7SK3 7SK5 7SK7 7SK8 7SK6 7SK4	Yen et al. (2022). Yen YC, Schafer CT, Gustavsson M, Eberle SA, Dominik PK, Deneka D, Zhang P, Schall TJ, Kossiakoff AA, Tesmer JJG, & Handel TM (2022). Structures of atypical chemokine receptor 3 reveal the basis for its promiscuity and signaling bias. Sci Adv 8 28:eabn8063. PubMed Id: 35857509. doi:10.1126/sciadv.abn8063.
*CXCR4 chemokine receptor complexed with IT1t antagonist: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.5 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI. P2₁ space group. CXCR4 with IT1t (P1 space group), 3.10 Å: 3OE8 CXCR4 with IT1t (P1 space group), 3.10 Å: 3OE9 CXCR4 with IT1t (I222 space group), 3.20 Å: 3OE6 CXCR4 with cyclic peptide antagonist CVX15 (C2 space group), 2.90 Å: 3OE0	3ODU	Data File Jmol Viewer 3ODU 3OE6 3OE9 3OE8 3OE0	Wu et al. (2010). Wu B, Chien EY, Mol CD, Fenalti G, Liu W, Katritch V, Abagyan R, Brooun A, Wells P, Bi FC, Hamel DJ, Kuhn P, Handel TM, Cherezov V, & Stevens RC (2010). Structures of the CXCR4 Chemokine GPCR with Small-Molecule and Cyclic Peptide Antagonists. Science 330 :1066-1071. PubMed Id: 20929726.
*CXCR4 chemokine receptor complexed with viral chemokine antagonist vMIP-II: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.10 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI.	4RWS	Data File Jmol Viewer 4RWS	Qin et al. (2015). Qin L, Kufareva I, Holden LG, Wang C, Zheng Y, Zhao C, Fenalti G, Wu H, Han GW, Cherezov V, Abagyan R, Stevens RC, & Handel TM (2015). Structural biology. Crystal structure of the chemokine receptor CXCR4 in complex with a viral chemokine. Science 347 6226:1117-1122. PubMed Id: 25612609. doi:10.1126/science.1261064.
*CX3CR1 chemokine receptor in complex with G_i1: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.80 Å** cryo-EM structure in complex with CX3CL1 & G_i1, 3.40 Å 7XBX	7XBW	Data File Jmol Viewer 7XBW 7XBX	Lu et al. (2022). Lu M, Zhao W, Han S, Lin X, Xu T, Tan Q, Wang M, Yi C, Chu X, Yang W, Zhu Y, Wu B, & Zhao Q (2022). Activation of the human chemokine receptor CX3CR1 regulated by cholesterol. Sci Adv 8 26:eabn8048. PubMed Id: 35767622. doi:10.1126/sciadv.abn8048.
*CCR5 chemokine receptor with bound Maraviroc: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.71 Å** Engineered protein: Met1-Glu54 of rubredoxin were inserted between Arg223 & Glu227 after deletion of Cys224-Asn226 in intracellular loop 3 (ICL3).	4MBS	Data File Jmol Viewer 4MBS	Tan et al. (2013). Tan Q, Zhu Y, Li J, Chen Z, Han GW, Kufareva I, Li T, Ma L, Fenalti G, Li J, Zhang W, Xie X, Yang H, Jiang H, Cherezov V, Liu H, Stevens RC, Zhao Q, & Wu B (2013). Structure of the CCR5 chemokine receptor-HIV entry inhibitor maraviroc complex. Science 341 :1387-1390. PubMed Id: 24030490. doi:10.1126/science.1241475.
*CCR5 chemokine receptor in complex with super-agonist and G_i heterotrimer: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.15 Å** cryo-EM structure	7O7F	Data File Jmol Viewer 7O7F	Isaikina et al. (2021). Isaikina P, Tsai CJ, Dietz N, Pamula F, Grahl A, Goldie KN, Guixà-González R, Branco C, Paolini-Bertrand M, Calo N, Cerini F, Schertler GFX, Hartley O, Stahlberg H, Maier T, Deupi X, & Grzesiek S (2021). Structural basis of the activation of the CC chemokine receptor 5 by a chemokine agonist. Sci Adv 7 25:eabg8685. PubMed Id: 34134983. doi:10.1126/sciadv.abg8685.
*CCR5 chemokine receptor in complex with G_i & MIP-1a: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure in complex with RANTES, 3.00 Å: 7F1R apo receptor in complex with G_i, 2.80 Å: 7F1S	7F1Q	Data File Jmol Viewer 7F1Q 7F1R 7F1S	Zhang et al. (2021). Zhang H, Chen K, Tan Q, Shao Q, Han S, Zhang C, Yi C, Chu X, Zhu Y, Xu Y, Zhao Q, & Wu B (2021). Structural basis for chemokine recognition and receptor activation of chemokine receptor CCR5. Nat Commun 12 1:4151. PubMed Id: 34230484. doi:10.1038/s41467-021-24438-5.
*CCR6 chemokine receptor with bound CCL20 and a G_o protein: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.34 Å** cryo-EM structure Engineered protein. N-terminal BRIL fusion.	6WWZ	Data File Jmol Viewer 6WWZ	Wasilko et al. (2020). Wasilko DJ, Johnson ZL, Ammirati M, Che Y, Griffor MC, Han S, & Wu H (2020). Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20. Nat Commun 11 1. PubMed Id: 32541785. doi:10.1038/s41467-020-16820-6.
*CCR7 chemokine receptor in complex with Cmp2105: Homo sapiens* E Eukaryota (expressed in Sf9 cells), 2.1 Å**	6QZH	Data File Jmol Viewer 6QZH	Jaeger et al. (2019). Jaeger K, Bruenle S, Weinert T, Guba W, Muehle J, Miyazaki T, Weber M, Furrer A, Haenggi N, Tetaz T, Huang CY, Mattle D, Vonach JM, Gast A, Kuglstatter A, Rudolph MG, Nogly P, Benz J, Dawson RJP, & Standfuss J (2019). Structural Basis for Allosteric Ligand Recognition in the Human CC Chemokine Receptor 7. Cell 178 5:1222-1230.e10. PubMed Id: 31442409. doi:10.1016/j.cell.2019.07.028.
*Chemokine receptor CCR9 in complex with vercirnon: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.8 Å**	5LWE	Data File Jmol Viewer 5LWE	Oswald et al. (2016). Oswald C, Rappas M, Kean J, Doré AS, Errey JC, Bennett K, Deflorian F, Christopher JA, Jazayeri A, Mason JS, Congreve M, Cooke RM, & Marshall FH (2016). Intracellular allosteric antagonism of the CCR9 receptor. Nature 540 :462-465. PubMed Id: 27926729. doi:10.1038/nature20606.
*Human cytomeglovirius US28 GPCR with bound human cytokine CX3CL1: Cytomeglovirus* V Viruses (expressed in HEK293 cells), 2.89 Å** Additional structure, 3.80 Å: 4XT3	4XT1	Data File Jmol Viewer 4XT1 4XT3	Burg et al. (2015). Burg JS, Ingram JR, Venkatakrishnan AJ, Jude KM, Dukkipati A, Feinberg EN, Angelini A, Waghray D, Dror RO, Ploegh HL, & Garcia KC (2015). Structural biology. Structural basis for chemokine recognition and activation of a viral G protein-coupled receptor. Science 347 6226:1113-1117. PubMed Id: 25745166. doi:10.1126/science.aaa5026.
*Human cytomeglovirius US28 GPCR bound to engineered chemokine CX3CL1.3: betaherpesvirus 5* V Viruses (expressed in HEK293 cells), 3.50 Å** Ligand-free US28 with stabilizing intracellular nanobody, 3.51 Å 5WB1	5WB2	Data File Jmol Viewer 5WB2 5WB1	Miles et al. (2018). Miles TF, Spiess K, Jude KM, Tsutsumi N, Burg JS, Ingram JR, Waghray D, Hjorto GM, Larsen O, Ploegh HL, Rosenkilde MM, & Garcia KC (2018). Viral GPCR US28 can signal in response to chemokine agonists of nearly unlimited structural degeneracy. Elife 7 :e35850. PubMed Id: 29882741. doi:10.7554/eLife.35850.
*Human cytomeglovirus US28 GPCR CX3CL1-US28-G_i-scFv16 in C-state: betaherpesvirus* V Viruses (expressed in Trichoplusia ni, Homo sapiens), 3.50 Å** cryo-EM structure CX3CL1-US28-G_i-scFv16 in OC-state, 3.60 Å 7RKN US27-G_i-scFv16 in CL-state, 7RKX	7RKM	Data File Jmol Viewer 7RKM 7RKN 7RKX	Tsutsumi et al. (2022). Tsutsumi N, Maeda S, Qu Q, Vögele M, Jude KM, Suomivuori CM, Panova O, Waghray D, Kato HE, Velasco A, Dror RO, Skiniotis G, Kobilka BK, & Garcia KC (2022). Atypical structural snapshots of human cytomegalovirus GPCR interactions with host G proteins. Sci Adv 8 3:eabl5442. PubMed Id: 35061538. doi:10.1126/sciadv.abl5442.
*endothelin ET_B receptor with bound endothelin-1: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.8 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI. Thermostabilized. without bound endothelin-1, 2.5 Å: 5GLI	5GLH	Data File Jmol Viewer 5GLH 5GLI	Shihoya et al. (2016). Shihoya W, Nishizawa T, Okuta A, Tani K, Dohmae N, Fujiyoshi Y, Nureki O, & Doi T (2016). Activation mechanism of endothelin ET_B receptor by endothelin-1. Nature 537 :363-368. PubMed Id: 27595334. doi:10.1038/nature19319.
*endothelin ET_B receptor with bound IRL2500: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.7 Å**	6K1Q	Data File Jmol Viewer 6K1Q	Nagiri et al. (2019). Nagiri C, Shihoya W, Inoue A, Kadji FMN, Aoki J, & Nureki O (2019). Crystal structure of human endothelin ETB receptor in complex with peptide inverse agonist IRL2500. Commun Biol 2 . PubMed Id: 31263780. doi:10.1038/s42003-019-0482-7.
*endothelin ET_B receptor in complex with sarafotoxin S6b: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å**	6LRY	Data File Jmol Viewer 6LRY	Izume et al. (2020). Izume T, Miyauchi H, Shihoya W, & Nureki O (2020). Crystal structure of human endothelin ET_B receptor in complex with sarafotoxin S6b. Biochem Biophys Res Commun 528 2:383-388. PubMed Id: 32001000. doi:10.1016/j.bbrc.2019.12.091.
*endothelin ET_B receptor with bound K-8794: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.2 Å** with bound bosentan, 3.6 Å: 5XPR	5X93	Data File Jmol Viewer 5X93 5XPR	Shihoya et al. (2017). Shihoya W, Nishizawa T, Yamashita K, Inoue A, Hirata K, Kadji FMN, Okuta A, Tani K, Aoki J, Fujiyoshi Y, Doi T, & Nureki O (2017). X-ray structures of endothelin ET_B receptor bound to clinical antagonist bosentan and its analog. Nat Struct Mol Biol 24 9:758-764. PubMed Id: 28805809. doi:10.1038/nsmb.3450.
*endothelin ET_B receptor-G_i complex with bound endothelin-1: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.80 Å** cryo-EM structure endothelin ET_B receptor focused refinement, 3.13 Å: 8IY6	8IY5	Data File Jmol Viewer 8IY5 8IY6	Sano et al. (2023). Sano FK, Akasaka H, Shihoya W, & Nureki O (2023). Cryo-EM structure of the endothelin-1-ETB-Gi complex. Elife 12 :85821. PubMed Id: 37096326. doi:10.7554/eLife.85821.
*Formylpeptide receptor FPR1-G_i1 complex with bound fMLF: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.30 Å** cryo-EM structure	7WVU	Data File Jmol Viewer 7WVU	Zhu et al. (2022). Zhu Y, Lin X, Zong X, Han S, Wang M, Su Y, Ma L, Chu X, Yi C, Zhao Q, & Wu B (2022). Structural basis of FPR2 in recognition of Aβ42 and neuroprotection by humanin. Nat Commun 13 1:1775. PubMed Id: 35365641. doi:10.1038/s41467-022-29361-x.
*Formylpeptide receptor FPR1-G_icomplex with bound fMLFII peptide: Homo sapiens* E Eukaryota (expressed in Spodoptera), 3.20 Å** cryo-EM structure in complex with CGEN-855A, 2.90 Å 7T6U	7T6T	Data File Jmol Viewer 7T6T 7T6U	Zhuang et al. (2022). Zhuang Y, Wang L, Guo J, Sun D, Wang Y, Liu W, Xu HE, & Zhang C (2022). Molecular recognition of formylpeptides and diverse agonists by the formylpeptide receptors FPR1 and FPR2. Nat Commun 13 1:1054. PubMed Id: 35217703. doi:10.1038/s41467-022-28586-0.
*Formylpeptide receptor FPR1-G_i complex with bound peptide agonist fMLF: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure with bound peptide agonist fMIFL, 2.80 Å: 7VFX	7EUO	Data File Jmol Viewer 7EUO 7VFX	Chen et al. (2022). Chen G, Wang X, Liao Q, Ge Y, Jiao H, Chen Q, Liu Y, Lyu W, Zhu L, van Zundert GCP, Robertson MJ, Skiniotis G, Du Y, Hu H, & Ye RD (2022). Structural basis for recognition of N-formyl peptides as pathogen-associated molecular patterns. Nat Commun 13 1:5232. PubMed Id: 36064945. doi:10.1038/s41467-022-32822-y.
*Formylpeptide receptor FPR2-G_i complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.17 Å** cryo-EM structure	6OMM	Data File Jmol Viewer 6OMM	Zhuang et al. (2020). Zhuang Y, Liu H, Edward Zhou X, Kumar Verma R, de Waal PW, Jang W, Xu TH, Wang L, Meng X, Zhao G, Kang Y, Melcher K, Fan H, Lambert NA, Eric Xu H, & Zhang C (2020). Structure of formylpeptide receptor 2-G_i complex reveals insights into ligand recognition and signaling. Nat Commun 11 1:885. PubMed Id: 32060286. doi:10.1038/s41467-020-14728-9.
*Formylpeptide receptor FPR2 with bound peptide agonist WKYMVm: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.8 Å** Engineered protein: N-terminal residues M1E2 replaced with apocytochrome b₅₆₂RIL.	6LW5	Data File Jmol Viewer 6LW5	Chen et al. (2020). Chen T, Xiong M, Zong X, Ge Y, Zhang H, Wang M, Won Han G, Yi C, Ma L, Ye RD, Xu Y, Zhao Q, & Wu B (2020). Structural basis of ligand binding modes at the human formyl peptide receptor 2. Nat Commun 11 1:1208. PubMed Id: 32139677. doi:10.1038/s41467-020-15009-1.
*Formylpeptide receptor FPR2-G_i2 complex with bound fM5: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure with bound fM9, 3.10 Å 7WVW with bound fhumanin, 2.80 Å 7WVX with bound Aβ42, 3.00 Å 7WVY	7WVV	Data File Jmol Viewer 7WVV 7WVX 7WVW 7WVY	Zhu et al. (2022). Zhu Y, Lin X, Zong X, Han S, Wang M, Su Y, Ma L, Chu X, Yi C, Zhao Q, & Wu B (2022). Structural basis of FPR2 in recognition of Aβ42 and neuroprotection by humanin. Nat Commun 13 1:1775. PubMed Id: 35365641. doi:10.1038/s41467-022-29361-x.
*Formylpeptide receptor FPR2-G_icomplex with bound fMLFII peptide: Homo sapiens* E Eukaryota (expressed in Spodoptera), 2.90 Å** cryo-EM structure in complex with C43, 3.00 Å 7T6S	7T6V	Data File Jmol Viewer 7T6V 7T6S	Zhuang et al. (2022). Zhuang Y, Wang L, Guo J, Sun D, Wang Y, Liu W, Xu HE, & Zhang C (2022). Molecular recognition of formylpeptides and diverse agonists by the formylpeptide receptors FPR1 and FPR2. Nat Commun 13 1:1054. PubMed Id: 35217703. doi:10.1038/s41467-022-28586-0.
*Dopamine D₁ receptor complexed with G_s protein with bound SKF-81297: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å** cryo-EM structure with bound SKF-83959, 2.90 Å: 7JVP with bound apomorphine, 3.00 Å: 7JVQ	7JV5	Data File Jmol Viewer 7JV5 7JVQ 7JVP	Zhuang et al. (2021). Zhuang Y, Xu P, Mao C, Wang L, Krumm B, Zhou XE, Huang S, Liu H, Cheng X, Huang XP, Shen DD, Xu T, Liu YF, Wang Y, Guo J, Jiang Y, Jiang H, Melcher K, Roth BL, Zhang Y, Zhang C, & Xu HE (2021). Structural insights into the human D1 and D2 dopamine receptor signaling complexes. Cell 184 4:931-942.e18. PubMed Id: 33571431. doi:10.1016/j.cell.2021.01.027.
*Dopamine D₁ receptor complexed with G_s protein with bound Fenoldopam: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.22 Å** cryo-EM structure with bound A77636, 3.54 Å: 7CKX with bound PW0464, 3.20 Å: 7CKY with bound LY3154207, 3.10 Å: 7CKZ with bound SKF83959, 3.30 Å: 7CRH	7CKW	Data File Jmol Viewer 7CKW 7CKZ 7CKY 7CRH 7CKX	Xiao et al. (2021). Xiao P, Yan W, Gou L, Zhong YN, Kong L, Wu C, Wen X, Yuan Y, Cao S, Qu C, Yang X, Yang CC, Xia A, Hu Z, Zhang Q, He YH, Zhang DL, Zhang C, Hou GH, Liu H, Zhu L, Fu P, Yang S, Rosenbaum DM, Sun JP, Du Y, Zhang L, Yu X, & Shao Z (2021). Ligand recognition and allosteric regulation of DRD1-G_s signaling complexes. Cell 184 4:943-956.e18. PubMed Id: 33571432. doi:10.1016/j.cell.2021.01.028.
*Dopamine D₁ receptor complexed with mini G_s protein , SKF-81297-bound, with bound LY3154207: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å** cryo-EM structure LY3154207 binding to dopamine-bound receptor, 3.20 Å 7LJD	7LJC	Data File Jmol Viewer 7LJC 7LJD	Zhuang et al. (2021). Zhuang Y, Krumm B, Zhang H, Zhou XE, Wang Y, Huang XP, Liu Y, Cheng X, Jiang Y, Jiang H, Zhang C, Yi W, Roth BL, Zhang Y, & Xu HE (2021). Mechanism of dopamine binding and allosteric modulation of the human D1 dopamine receptor. Cell Res 31 5:593-596. PubMed Id: 33750903. doi:10.1038/s41422-021-00482-0.
*Dopamine D₁ receptor complexed with mini G_s protein with bound fenoldopam: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure with bound tavapadon, 3.30 Å 7X2D with bound LY3154207, 3.00 Å 7X2F	7X2C	Data File Jmol Viewer 7X2C 7X2F 7X2D	Teng et al. (2022). Teng X, Chen S, Nie Y, Xiao P, Yu X, Shao Z, & Zheng S (2022). Ligand recognition and biased agonism of the D1 dopamine receptor. Nat Commun 13 1:3186. PubMed Id: 35676276. doi:10.1038/s41467-022-30929-w.
*Dopamine D₁ receptor complexed with mini G_s protein, GDP-bound, with bound Nb35: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.13 Å** cryo-EM structure GDP-bound, 3.46 Å: 7F1Z GTP-bound, with bound Nb35, 3.58 Å: 7F23 GTP-bound, 4.16 Å: 7F24	7F1O	Data File Jmol Viewer 7F1O 7F24 7F23 7F1Z	Teng et al. (2022). Teng X, Chen S, Wang Q, Chen Z, Wang X, Huang N, & Zheng S (2022). Structural insights into G protein activation by D1 dopamine receptor. Sci Adv 8 23:eabo4158. PubMed Id: 35687690. doi:10.1126/sciadv.abo4158.
*Dopamine D₁ Receptor-G_s complex with bound rotigotine: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.20 Å** cryo-EM structure	8IRR	Data File Jmol Viewer 8IRR	Xu et al. (2023). Xu P, Huang S, Krumm BE, Zhuang Y, Mao C, Zhang Y, Wang Y, Huang XP, Liu YF, He X, Li H, Yin W, Jiang Y, Zhang Y, Roth BL, & Xu HE (2023). Structural genomics of the human dopamine receptor system. Cell Res 33 8:604-616. PubMed Id: 37221270. doi:10.1038/s41422-023-00808-0.
*Dopamine D₂ receptor complexed with risperidone: Homo sapiens* E Eukaryota (expressed in sf9 cells), 2.87 Å** engineered protein. T4 lysozyme fused into intracellular loop 3. supersedes 6C38	6CM4	Data File Jmol Viewer 6CM4	Wang et al. (2018). Wang S, Che T, Levit A, Shoichet BK, Wacker D, & Roth BL (2018). Structure of the D₂ dopamine receptor bound to the atypical antipsychotic drug risperidone. Nature 555 :269-273. PubMed Id: 29466326. doi:10.1038/nature25758.
*Dopamine D₂ receptor complexed with haloperidol: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.1 Å**	6LUQ	Data File Jmol Viewer 6LUQ	Fan et al. (2020). Fan L, Tan L, Chen Z, Qi J, Nie F, Luo Z, Cheng J, & Wang S (2020). Haloperidol bound D2 dopamine receptor structure inspired the discovery of subtype selective ligands. Nat Commun 11 1. PubMed Id: 32103023. doi:10.1038/s41467-020-14884-y.
*Dopamine D₂ receptor-G_i protein complex in nanodiscs: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.80 Å** cryo-EM structure	6VMS	Data File Jmol Viewer 6VMS	Yin et al. (2020). Yin J, Chen KM, Clark MJ, Hijazi M, Kumari P, Bai XC, Sunahara RK, Barth P, & Rosenbaum DM (2020). Structure of a D2 dopamine receptor-G-protein complex in a lipid membrane. Nature 584 7819:125-129. PubMed Id: 32528175. doi:10.1038/s41586-020-2379-5.
*Dopamine D₂ receptor complexed with spiperone: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.10 Å**	7DFP	Data File Jmol Viewer 7DFP	Im et al. (2020). Im D, Inoue A, Fujiwara T, Nakane T, Yamanaka Y, Uemura T, Mori C, Shiimura Y, Kimura KT, Asada H, Nomura N, Tanaka T, Yamashita A, Nango E, Tono K, Kadji FMN, Aoki J, Iwata S, & Shimamura T (2020). Structure of the dopamine D₂ receptor in complex with the antipsychotic drug spiperone. Nat Commun 11 1. PubMed Id: 33353947. doi:10.1038/s41467-020-20221-0.
*Dopamine D₂ receptor complexed with G_i protein with bound bromocriptine: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.80 Å** cryo-EM structure	7JVR	Data File Jmol Viewer 7JVR	Zhuang et al. (2021). Zhuang Y, Xu P, Mao C, Wang L, Krumm B, Zhou XE, Huang S, Liu H, Cheng X, Huang XP, Shen DD, Xu T, Liu YF, Wang Y, Guo J, Jiang Y, Jiang H, Melcher K, Roth BL, Zhang Y, Zhang C, & Xu HE (2021). Structural insights into the human D1 and D2 dopamine receptor signaling complexes. Cell 184 4:931-942.e18. PubMed Id: 33571431. doi:10.1016/j.cell.2021.01.027.
*Dopamine D₂ receptor-G_i complex with bound rotigotine: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.00 Å** cryo-EM structure	8IRS	Data File Jmol Viewer 8IRS	Xu et al. (2023). Xu P, Huang S, Krumm BE, Zhuang Y, Mao C, Zhang Y, Wang Y, Huang XP, Liu YF, He X, Li H, Yin W, Jiang Y, Zhang Y, Roth BL, & Xu HE (2023). Structural genomics of the human dopamine receptor system. Cell Res 33 8:604-616. PubMed Id: 37221270. doi:10.1038/s41422-023-00808-0.
*Dopamine D₃ receptor complexed with D2/D3-selective antagonist: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.89 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI.	3PBL	Data File Jmol Viewer 3PBL	Chien et al. (2010). Chien EY, Liu W, Zhao Q, Katritch V, Han GW, Hanson MA, Shi L, Newman AH, Javitch JA, Cherezov V, & Stevens RC (2010). Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist. Science 330 :1091-1095. PubMed Id: 21097933.
*Dopamine D₃-G_i in complex with Pramipexole: Homo sapiens* E Eukaryota (expressed in S. frugiperda cells), 3.00 Å** Engineered protein. cryo-EM structure in complex with PD128907, 2.70 Å: 7CMV	7CMU	Data File Jmol Viewer 7CMU 7CMV	Xu et al. (2021). Xu P, Huang S, Mao C, Krumm BE, Zhou XE, Tan Y, Huang XP, Liu Y, Shen DD, Jiang Y, Yu X, Jiang H, Melcher K, Roth BL, Cheng X, Zhang Y, & Xu HE (2021). Structures of the human dopamine D₃ receptor-G_i complexes. Mol Cell 81 6:1147-1159.e4. PubMed Id: 33548201. doi:10.1016/j.molcel.2021.01.003.
*Dopamine D₃ receptor-G_i complex with bound rotigotine: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.70 Å** cryo-EM structure	8IRT	Data File Jmol Viewer 8IRT	Xu et al. (2023). Xu P, Huang S, Krumm BE, Zhuang Y, Mao C, Zhang Y, Wang Y, Huang XP, Liu YF, He X, Li H, Yin W, Jiang Y, Zhang Y, Roth BL, & Xu HE (2023). Structural genomics of the human dopamine receptor system. Cell Res 33 8:604-616. PubMed Id: 37221270. doi:10.1038/s41422-023-00808-0.
*Dopamine D₄ receptor complexed with nemonapride: Homo sapiens* E Eukaryota (expressed in sf9 cells), 1.96 Å** engineered protein: Thermostabilzed with apocytochrome b₅₆₂ replacing 3rd intracellular loop. with bound Na⁺, 2.43 Å: 5WIV	5WIU	Data File Jmol Viewer 5WIU 5WIV	Wang et al. (2017). Wang S, Wacker D, Levit A, Che T, Betz RM, McCorvy JD, Venkatakrishnan AJ, Huang XP, Dror RO, Shoichet BK, & Roth BL (2017). D₄ dopamine receptor high-resolution structures enable the discovery of selective agonists. Science 358 6361:381-386. PubMed Id: 29051383. doi:10.1126/science.aan5468.
*Dopamine D₄ receptor with bound L745870: E Eukaryota (expressed in sf9 cells), 3.5 Å*	6IQL	Data File Jmol Viewer 6IQL	Zhou et al. (2019). Zhou Y, Cao C, He L, Wang X, & Zhang XC (2019). Crystal structure of dopamine receptor D4 bound to the subtype selective ligand, L745870. Elife 8 :e48822. PubMed Id: 31750832. doi:10.7554/eLife.48822.
*Dopamine D₄ receptor-G_i complex with bound rotigotine: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.20 Å** cryo-EM structure	8IRU	Data File Jmol Viewer 8IRU	Xu et al. (2023). Xu P, Huang S, Krumm BE, Zhuang Y, Mao C, Zhang Y, Wang Y, Huang XP, Liu YF, He X, Li H, Yin W, Jiang Y, Zhang Y, Roth BL, & Xu HE (2023). Structural genomics of the human dopamine receptor system. Cell Res 33 8:604-616. PubMed Id: 37221270. doi:10.1038/s41422-023-00808-0.
*Dopamine D₅ receptor-G_s complex with bound rotigotine: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.10 Å** cryo-EM structure	8IRV	Data File Jmol Viewer 8IRV	Xu et al. (2023). Xu P, Huang S, Krumm BE, Zhuang Y, Mao C, Zhang Y, Wang Y, Huang XP, Liu YF, He X, Li H, Yin W, Jiang Y, Zhang Y, Roth BL, & Xu HE (2023). Structural genomics of the human dopamine receptor system. Cell Res 33 8:604-616. PubMed Id: 37221270. doi:10.1038/s41422-023-00808-0.
*Histamine H₁ receptor, complexed with doxepin: Homo sapiens* E Eukaryota (expressed in Pichia pastoris), 3.10 Å**	3RZE	Data File Jmol Viewer 3RZE	Tsujimoto et al. (2011). Shimamura T, Shiroishi M, Weyand S, Tsujimoto H, Winter G, Katritch V, Abagyan R, Cherezov V, Liu W, Han GW, Kobayashi T, Stevens RC, & Iwata S (2011). Structure of the human histamine H₁ receptor complex with doxepin. Nature 475 :65-70. PubMed Id: 21697825. doi:10.1038/nature10236.
*Histamine H₁ receptor-G_q complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.30 Å** cryo-EM structure	7DFL	Data File Jmol Viewer 7DFL	Xia et al. (2021). Xia R, Wang N, Xu Z, Lu Y, Song J, Zhang A, Guo C, & He Y (2021). Cryo-EM structure of the human histamine H₁ receptor/G_q complex. Nat Commun 12 1:2086. PubMed Id: 33828102. doi:10.1038/s41467-021-22427-2.
*Histamine H₁ receptor, apo state, local refinement: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.50 Å** cryo-EM structure with bound mepyramine, 3.20 Å: 8X63 with bound astemizole, 3.00 Å: 8X5Y with bound desloratadine, 3.40 Å: 8X64	8X5X	Data File Jmol Viewer 8X5X 8X64 8X63 8X5Y	Wang et al. (2024). Wang D, Guo Q, Wu Z, Li M, He B, Du Y, Zhang K, & Tao Y (2024). Molecular mechanism of antihistamines recognition and regulation of the histamine H1 receptor. Nat Commun 15 1:84. PubMed Id: 38167898. doi:10.1038/s41467-023-44477-4.
*Histamine H₂ receptor, complexed with famotidine, a modified nanobody Nb6M, and nanobody-binding antibody fragment (NabFab): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.00 Å** cryo-EM structure	7UL3	Data File Jmol Viewer 7UL3	Robertson et al. (2022). Robertson MJ, Papasergi-Scott MM, He F, Seven AB, Meyerowitz JG, Panova O, Peroto MC, Che T, & Skiniotis G (2022). Structure determination of inactive-state GPCRs with a universal nanobody. Nat Struct Mol Biol 29 12:1188-1195. PubMed Id: 36396979. doi:10.1038/s41594-022-00859-8.
*Histamine H₂ receptor - G_s complex in lipid nanodiscs with bound histidine (cell-free synthesis): Homo sapiens* E Eukaryota (expressed in E. coli), 3.40 Å** cryo-EM structure	8POK	Data File Jmol Viewer 8POK	Köck et al. (2024). Köck Z, Schnelle K, Persechino M, Umbach S, Schihada H, Januliene D, Parey K, Pockes S, Kolb P, Dötsch V, Möller A, Hilger D, & Bernhard F (2024). Cryo-EM structure of cell-free synthesized human histamine 2 receptor/Gs complex in nanodisc environment. Nat Commun 15 1:1831. PubMed Id: 38418462. doi:10.1038/s41467-024-46096-z.
*Histamine H₃ receptor (H₃R), complexed with PF03654746: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.60 Å**	7F61	Data File Jmol Viewer 7F61	Peng et al. (2022). Peng X, Yang L, Liu Z, Lou S, Mei S, Li M, Chen Z, & Zhang H (2022). Structural basis for recognition of antihistamine drug by human histamine receptor. Nat Commun 13 1:6105. PubMed Id: 36243875. doi:10.1038/s41467-022-33880-y.
*Histamine H₄ receptor-G_q complex with bound histamine: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.00 Å** cryo-EM structure with bound imetit, 3.10 Å: 7YFD	7YFC	Data File Jmol Viewer 7YFC 7YFD	Im et al. (2023). Im D, Kishikawa JI, Shiimura Y, Hisano H, Ito A, Fujita-Fujiharu Y, Sugita Y, Noda T, Kato T, Asada H, & Iwata S (2023). Structural insights into the agonists binding and receptor selectivity of human histamine H4 receptor. Nat Commun 14 1:6538. PubMed Id: 37863901. doi:10.1038/s41467-023-42260-z.
*Histamine H₄ receptor- G_i complex with bound histamine: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.07 Å** cryo-EM structure with bound agonist clozapine, 3.21 Å: 8JXV with bound agonist VUF6884, 3.01 Å: 8JXW with bound agonist clobenpropit, 3.06 Å: 8JXX	8JXT	Data File Jmol Viewer 8JXT 8JXW 8JXX 8JXV	Xia et al. (2024). Xia R, Shi S, Xu Z, Vischer HF, Windhorst AD, Qian Y, Duan Y, Liang J, Chen K, Zhang A, Guo C, Leurs R, & He Y (2024). Structural basis of ligand recognition and design of antihistamines targeting histamine H4 receptor. Nat Commun 15 1:2493. PubMed Id: 38509098. doi:10.1038/s41467-024-46840-5.
*Sphingosine-1-phosphate receptor 1 (S1PR1): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.35 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI. Structure determined using microdiffraction data assembly, 2.80 Å: 3V2Y	3V2W	Data File Jmol Viewer 3V2W 3V2Y	Hanson et al. (2012). Hanson MA, Roth CB, Jo E, Griffith MT, Scott FL, Reinhart G, Desale H, Clemons B, Cahalan SM, Schuerer SC, Sanna MG, Han GW, Kuhn P, Rosen H, & Stevens RC (2012). Crystal structure of a lipid G protein-coupled receptor. Science 335 :851-855. PubMed Id: 22344443. doi:10.1126/science.1215904.
*Sphingosine-1-phosphate receptor 1 (S1PR1)-G_i with bound siponimod: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.98 Å** cryo-EM structure with bound cenerimod, 3.07 Å 7EVZ with bound ozanimod, 3.42 Å 7EW0 with bound SEW2871, 3.27 Å 7EW7	7EVY	Data File Jmol Viewer 7EVY 7EVZ 7EW0 7EW7	Yuan et al. (2021). Yuan Y, Jia G, Wu C, Wang W, Cheng L, Li Q, Li Z, Luo K, Yang S, Yan W, Su Z, & Shao Z (2021). Structures of signaling complexes of lipid receptors S1PR1 and S1PR5 reveal mechanisms of activation and drug recognition. Cell Res 31 12:1263-1274. PubMed Id: 34526663. doi:10.1038/s41422-021-00566-x.
*Sphingosine-1-phosphate receptor 1 - G_i complex bound to S1P: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å** cryo-EM structure bound to Siponimod, 2.60 Å 7TD4	7TD3	Data File Jmol Viewer 7TD3 7TD4	Liu et al. (2022). Liu S, Paknejad N, Zhu L, Kihara Y, Ray M, Chun J, Liu W, Hite RK, & Huang XY (2022). Differential activation mechanisms of lipid GPCRs by lysophosphatidic acid and sphingosine 1-phosphate. Nat Commun 13 1:731. PubMed Id: 35136060. doi:10.1038/s41467-022-28417-2.
*Sphingosine-1-phosphate receptor 1 (S1PR1)-G_i complex with bound S1P: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.40 Å** cryo-EM structure bound to FTY720p, 2.89 Å 7EO2 bound to BAF312, 2.86 Å 7EO4	7WF7	Data File Jmol Viewer 7WF7 7EO4 7EO2	Xu et al. (2022). Xu Z, Ikuta T, Kawakami K, Kise R, Qian Y, Xia R, Sun MX, Zhang A, Guo C, Cai XH, Huang Z, Inoue A, & He Y (2022). Structural basis of sphingosine-1-phosphate receptor 1 activation and biased agonism. Nat Chem Biol 18 3:281-288. PubMed Id: 34937912. doi:10.1038/s41589-021-00930-3.
*Sphingosine-1-phosphate receptor 2 (S1PR2)- heterotrimeric G₁₃ complex with bound S1P: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.19 Å** cryo-EM structure	7T6B	Data File Jmol Viewer 7T6B	Chen et al. (2022). Chen H, Chen K, Huang W, Staudt LM, Cyster JG, & Li X (2022). Structure of S1PR2-heterotrimeric G13 signaling complex. Sci Adv 8 13:eabn0067. PubMed Id: 35353559. doi:10.1126/sciadv.abn0067.
*Sphingosine-1-phosphate receptor 3 (S1PR3) in complex with natural ligand: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å**	7C4S	Data File Jmol Viewer 7C4S	Maeda et al. (2021). Maeda S, Shiimura Y, Asada H, Hirata K, Luo F, Nango E, Tanaka N, Toyomoto M, Inoue A, Aoki J, Iwata S, & Hagiwara M (2021). Endogenous agonist-bound S1PR3 structure reveals determinants of G protein-subtype bias. Sci Adv 7 24:eabf5325. PubMed Id: 34108205. doi:10.1126/sciadv.abf5325.
*Sphingosine-1-phosphate receptor 3 (S1PR3)-G_i complex with bound S1P: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.10 Å** cryo-EM structure with bound pFTY720, 3.10 Å 7EW2 with bound CYM-5541, 3.20 Å 7EW4	7EW3	Data File Jmol Viewer 7EW3 7EW2 7EW4	Zhao et al. (2022). Zhao C, Cheng L, Wang W, Wang H, Luo Y, Feng Y, Wang X, Fu H, Cai Y, Yang S, Fu P, Yan W, & Shao Z (2022). Structural insights into sphingosine-1-phosphate recognition and ligand selectivity of S1PR3-Gi signaling complexes. Cell Res 32 2:218-221. PubMed Id: 34545189. doi:10.1038/s41422-021-00567-w.
*Sphingosine-1-phosphate receptor 5 (S1PR5)-G_i complex with bound siponimod: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.40 Å** cryo-EM structure	7EW1	Data File Jmol Viewer 7EW1	Yuan et al. (2021). Yuan Y, Jia G, Wu C, Wang W, Cheng L, Li Q, Li Z, Luo K, Yang S, Yan W, Su Z, & Shao Z (2021). Structures of signaling complexes of lipid receptors S1PR1 and S1PR5 reveal mechanisms of activation and drug recognition. Cell Res 31 12:1263-1274. PubMed Id: 34526663. doi:10.1038/s41422-021-00566-x.
*Sphingosine-1-phosphate receptor 5 (S1PR5) in complex with ONO-5430608: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.20 Å** XFEL structure	7YXA	Data File Jmol Viewer 7YXA	Lyapina et al. (2022). Lyapina E, Marin E, Gusach A, Orekhov P, Gerasimov A, Luginina A, Vakhrameev D, Ergasheva M, Kovaleva M, Khusainov G, Khorn P, Shevtsov M, Kovalev K, Bukhdruker S, Okhrimenko I, Popov P, Hu H, Weierstall U, Liu W, Cho Y, Gushchin I, Rogachev A, Bourenkov G, Park S, Park G, Hyun HJ, Park J, Gordeliy V, Borshchevskiy V, Mishin A, & Cherezov V (2022). Structural basis for receptor selectivity and inverse agonism in S1P5 receptors. Nat Commun 13 1:4736. PubMed Id: 35961984. doi:10.1038/s41467-022-32447-1.
*M1 muscarinic acetylcholine receptor with bound tiotropium: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.7 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI	5CXV	Data File Jmol Viewer 5CXV	Thal et al. (2016). Thal DM, Sun B, Feng D, Nawaratne V, Leach K, Felder CC, Bures MG, Evans DA, Weis WI, Bachhawat P, Kobilka TS, Sexton PM, Kobilka BK, & Christopoulos A (2016). Crystal structures of the M1 and M4 muscarinic acetylcholine receptors. Nature 531 :335-340. PubMed Id: 26958838. doi:10.1038/nature17188.
*M1 muscarinic acetylcholine receptor in complex with G11 protein: Homo sapiens* E Eukaryota (expressed in S. frugiperda & Trichoplusia ni), 3.3 Å** cryo-EM	6OIJ	Data File Jmol Viewer 6OIJ	Maeda et al. (2019). Maeda S, Qu Q, Robertson MJ, Skiniotis G, & Kobilka BK (2019). Structures of the M1 and M2 muscarinic acetylcholine receptor/G-protein complexes. Science 364 6440:552-557. PubMed Id: 31073061. doi:10.1126/science.aaw5188.
*M1 muscarinic acetylcholine receptor in complex with muscarinic toxin 7 (MT7): Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.55 Å**	6WJC	Data File Jmol Viewer 6WJC	Maeda et al. (2020). Maeda S, Xu J, N Kadji FM, Clark MJ, Zhao J, Tsutsumi N, Aoki J, Sunahara RK, Inoue A, Garcia KC, & Kobilka BK (2020). Structure and selectivity engineering of the M1 muscarinic receptor toxin complex. Science 369 6500:161-167. PubMed Id: 32646996. doi:10.1126/science.aax2517.
*M1 muscarinic acetylcholine receptor in complex with 77-LH-28-1: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.17 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI in complex with HTL0009936, 2.33 Å 6ZG4 in complex with GSK1034702, 2.50 Å	6ZFZ	Data File Jmol Viewer 6ZFZ 6ZG4	Brown et al. (2021). Brown AJH, Bradley SJ, Marshall FH, Brown GA, Bennett KA, Brown J, Cansfield JE, Cross DM, de Graaf C, Hudson BD, Dwomoh L, Dias JM, Errey JC, Hurrell E, Liptrot J, Mattedi G, Molloy C, Nathan PJ, Okrasa K, Osborne G, Patel JC, Pickworth M, Robertson N, Shahabi S, Bundgaard C, Phillips K, Broad LM, Goonawardena AV, Morairty SR, Browning M, Perini F, Dawson GR, Deakin JFW, Smith RT, Sexton PM, Warneck J, Vinson M, Tasker T, Tehan BG, Teobald B, Christopoulos A, Langmead CJ, Jazayeri A, Cooke RM, Rucktooa P, Congreve MS, Weir M, & Tobin AB (2021). From structure to clinic: Design of a muscarinic M1 receptor agonist with potential to treatment of Alzheimer's disease. Cell 184 24:5886-5901.e22. PubMed Id: 34822784. doi:10.1016/j.cell.2021.11.001.
*M2 muscarinic acetylcholine receptor bound to an antagonist: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.00 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI.	3UON	Data File Jmol Viewer 3UON	Haga et al. (2012). Haga K, Kruse AC, Asada H, Yurugi-Kobayashi T, Shiroishi M, Zhang C, Weis WI, Okada T, Kobilka BK, Haga T, & Kobayashi T (2012). Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist. Nature 482 :547-551. PubMed Id: 22278061. doi:10.1038/nature10753.
*M2 muscarinic acetylcholine receptor bound to the agonist iperoxo: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.50 Å** Stabilized by camelid antibody fragment. with bound iperoxo and allosteric modulator LY2119620, 3.70 Å: 4MQT	4MQS	Data File Jmol Viewer 4MQS 4MQT	Kruse et al. (2013). Kruse AC, Ring AM, Manglik A, Hu J, Hu K, Eitel K, Hübner H, Pardon E, Valant C, Sexton PM, Christopoulos A, Felder CC, Gmeiner P, Steyaert J, Weis WI, Garcia KC, Wess J, & Kobilka BK (2013). Activation and allosteric modulation of a muscarinic acetylcholine receptor. Nature 504 :101-106. PubMed Id: 24256733. doi:10.1038/nature12735.
*M2 muscarinic acetylcholine receptor in complex with Go: Homo sapiens* E Eukaryota (expressed in S. frugiperda & Trichoplusia ni), 3.6 Å** cryo-EM structure	6OIK	Data File Jmol Viewer 6OIK	Maeda et al. (2019). Maeda S, Qu Q, Robertson MJ, Skiniotis G, & Kobilka BK (2019). Structures of the M1 and M2 muscarinic acetylcholine receptor/G-protein complexes. Science 364 6440:552-557. PubMed Id: 31073061. doi:10.1126/science.aaw5188.
*M2 muscarinic acetylcholine receptor-β-arrestin complex in a nanodisc: Homo sapiens & Rattus norvegicus (arrestin)* E Eukaryota (expressed in HEK293 cells), 4 Å** cryo-EM structure	6U1N	Data File Jmol Viewer 6U1N	Staus et al. (2020). Staus DP, Hu H, Robertson MJ, Kleinhenz ALW, Wingler LM, Capel WD, Latorraca NR, Lefkowitz RJ, & Skiniotis G (2020). Structure of the M2 muscarinic receptor-β-arrestin complex in a lipid nanodisc. Nature 579 7798:297-302. PubMed Id: 31945772. doi:10.1038/s41586-020-1954-0.
*M3 muscarinic acetylcholine receptor: Rattus norvegicus* E Eukaryota (expressed in S. frugiperda), 3.40 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI.	4DAJ	Data File Jmol Viewer 4DAJ	Kruse et al. (2012). Kruse AC, Hu J, Pan AC, Arlow DH, Rosenbaum DM, Rosemond E, Green HF, Liu T, Chae PS, Dror RO, Shaw DE, Weis WI, Wess J, & Kobilka BK (2012). Structure and dynamics of the M3 muscarinic acetylcholine receptor. Nature 482 :552-556. PubMed Id: 22358844. doi:10.1038/nature10867.
*M3 muscarinic acetylcholine receptor, disulfide-stabilized T4 lysozyme (dsT4L) with bound tiotropium: Rattus norvegicus* E Eukaryota (expressed in S. frugiperda), 3.57 Å** M3-mT4L receptor with bound tiotropium, 2.80 Å: 4U15 M3-mT4L receptor with bound NMS, 3.70 Å: 4U16	4U14	Data File Jmol Viewer 4U14 4U15 4U16	Thorsen et al. (2014). Thorsen TS, Matt R, Weis WI, & Kobilka BK (2014). Modified T4 Lysozyme Fusion Proteins Facilitate G Protein-Coupled Receptor Crystallogenesis. Structure 22 11:1657-1664. PubMed Id: 25450769. doi:10.1016/j.str.2014.08.022.
*M3 muscarinic acetylcholine receptor-miniG_q protein complex with bound DCZ: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.69 Å** DREADD-based receptor cryo-EM structure with bound CNO, 2.79 Å: 8E9Y with bound Iperoxo, 2.69 Å: 8E9Z with iperoxo (local refinement), 2.56 Å: 8EA0	8E9W	Data File Jmol Viewer 8E9W 8EA0 8E9Z 8E9Y	Zhang et al. (2022). Zhang S, Gumpper RH, Huang XP, Liu Y, Krumm BE, Cao C, Fay JF, & Roth BL (2022). Molecular basis for selective activation of DREADD-based chemogenetics. Nature 612 7939:354-362. PubMed Id: 36450989. doi:10.1038/s41586-022-05489-0.
*M4 muscarinic acetylcholine receptor with bound tiotropium: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.6 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI.	5DSG	Data File Jmol Viewer 5DSG	Thal et al. (2016). Thal DM, Sun B, Feng D, Nawaratne V, Leach K, Felder CC, Bures MG, Evans DA, Weis WI, Bachhawat P, Kobilka TS, Sexton PM, Kobilka BK, & Christopoulos A (2016). Crystal structures of the M1 and M4 muscarinic acetylcholine receptors. Nature 531 :335-340. PubMed Id: 26958838. doi:10.1038/nature17188.
*M4 muscarinic acetylcholine receptor, inactive N449^7.49R mutant: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3 Å**	6KP6	Data File Jmol Viewer 6KP6	Wang et al. (2020). Wang J, Wu M, Wu L, Xu Y, Li F, Wu Y, Popov P, Wang L, Bai F, Zhao S, Liu ZJ, & Hua T (2020). The structural study of mutation-induced inactivation of human muscarinic receptor M4. IUCrJ 7 :294-305. PubMed Id: 32148857. doi:10.1107/S2052252520000597.
*M4 muscarinic acetylcholine receptor - G_i complex with bound compound 110: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.60 Å** cryo-EM structure with bound iperoxo, 3.40 Å 7V69 with bound iperoxo and LY2119620, 3.40 Å 7V68	7V6A	Data File Jmol Viewer 7V6A 7V68 7V69	Wang et al. (2022). Wang J, Wu M, Chen Z, Wu L, Wang T, Cao D, Wang H, Liu S, Xu Y, Li F, Liu J, Chen N, Zhao S, Cheng J, Wang S, & Hua T (2022). The unconventional activation of the muscarinic acetylcholine receptor M4R by diverse ligands. Nat Commun 13 1:2855. PubMed Id: 35606397. doi:10.1038/s41467-022-30595-y.
*M4 muscarinic acetylcholine receptor-miniG_o protein complex with bound DCZ: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.70 Å** DREADD-based receptor cryo-EM structure	8E9X	Data File Jmol Viewer 8E9X	Zhang et al. (2022). Zhang S, Gumpper RH, Huang XP, Liu Y, Krumm BE, Cao C, Fay JF, & Roth BL (2022). Molecular basis for selective activation of DREADD-based chemogenetics. Nature 612 7939:354-362. PubMed Id: 36450989. doi:10.1038/s41586-022-05489-0.
*M4 muscarinic acetylcholine receptor (M4 mAChR) - G_i1 complex with bound xanomeline: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.45 Å** cryo-EM structure	8FX5	Data File Jmol Viewer 8FX5	Burger et al. (2023). Burger WAC, Pham V, Vuckovic Z, Powers AS, Mobbs JI, Laloudakis Y, Glukhova A, Wootten D, Tobin AB, Sexton PM, Paul SM, Felder CC, Danev R, Dror RO, Christopoulos A, Valant C, & Thal DM (2023). Xanomeline displays concomitant orthosteric and allosteric binding modes at the M4 mAChR. Nat Commun 14 1:5440. PubMed Id: 37673901. doi:10.1038/s41467-023-41199-5.
*M5 muscarinic acetylcholine receptor with bound tiotropium: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.54 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI	6OL9	Data File Jmol Viewer 6OL9	Vuckovic et al. (2019). Vuckovic Z, Gentry PR, Berizzi AE, Hirata K, Varghese S, Thompson G, van der Westhuizen ET, Burger WAC, Rahmani R, Valant C, Langmead CJ, Lindsley CW, Baell JB, Tobin AB, Sexton PM, Christopoulos A, & Thal DM (2019). Crystal structure of the M₅ muscarinic acetylcholine receptor. Proc Natl Acad Sci USA 116 51:26001-26007. PubMed Id: 31772027. doi:10.1073/pnas.1914446116.
*κ-opioid receptor in complex with JDTic: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.90 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI.	4DJH	Data File Jmol Viewer 4DJH	Wu et al. (2012). Wu H, Wacker D, Mileni M, Katritch V, Han GW, Vardy E, Liu W, Thompson AA, Huang XP, Carroll FI, Mascarella SW, Westkaemper RB, Mosier PD, Roth BL, Cherezov V, & Stevens RC (2012). Structure of the human κ-opioid receptor in complex with JDTic. Nature 485 :327-332. PubMed Id: 22437504. doi:10.1038/nature10939.
*κ-opioid receptor in complex with JDTic and nanobody Nb6: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.3 Å**	6VI4	Data File Jmol Viewer 6VI4	Che et al. (2020). Che T, English J, Krumm BE, Kim K, Pardon E, Olsen RHJ, Wang S, Zhang S, Diberto JF, Sciaky N, Carroll FI, Steyaert J, Wacker D, & Roth BL (2020). Nanobody-enabled monitoring of kappa opioid receptor states. Nat Commun 11 1. PubMed Id: 32123179. doi:10.1038/s41467-020-14889-7.
*κ-opioid receptor, nanobody-stabilized active state: Homo sapiens* E Eukaryota (expressed in sf9 cells), 3.1 Å** engineered protein: Lacks N-terminal residues 1-53 and C-terminal residues 259-380. Thermostabilzed with apocytochrome b₅₆₂ in place of N-terminus residues.	6B73	Data File Jmol Viewer 6B73	Che et al. (2018). Che T, Majumdar S, Zaidi SA, Ondachi P, McCorvy JD, Wang S, Mosier PD, Uprety R, Vardy E, Krumm BE, Han GW, Lee MY, Pardon E, Steyaert J, Huang XP, Strachan RT, Tribo AR, Pasternak GW, Carroll FI, Stevens RC, Cherezov V, Katritch V, Wacker D, & Roth BL (2018). Structure of the Nanobody-Stabilized Active State of the Kappa Opioid Receptor. Cell 172 :55-67.e15. PubMed Id: 29307491. doi:10.1016/j.cell.2017.12.011.
*κ-opioid receptor-G_i complex with bound dynorphin: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.19 Å** cryo-EM structure	8F7W	Data File Jmol Viewer 8F7W	Wang et al. (2023). Wang Y, Zhuang Y, DiBerto JF, Zhou XE, Schmitz GP, Yuan Q, Jain MK, Liu W, Melcher K, Jiang Y, Roth BL, & Xu HE (2023). Structures of the entire human opioid receptor family. Cell 186 2:413-427.e17. PubMed Id: 36638794. doi:10.1016/j.cell.2022.12.026.
*κ-opioid receptor in complex with nalfurafine and nanobody Nb39: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.30 Å**	7YIT	Data File Jmol Viewer 7YIT	El Daibani et al. (2023). El Daibani A, Paggi JM, Kim K, Laloudakis YD, Popov P, Bernhard SM, Krumm BE, Olsen RHJ, Diberto J, Carroll FI, Katritch V, Wünsch B, Dror RO, & Che T (2023). Molecular mechanism of biased signaling at the kappa opioid receptor. Nat Commun 14 1:1338. PubMed Id: 36906681. doi:10.1038/s41467-023-37041-7.
*κ-opioid receptor-G_i1 complex with bound momSalB: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.71 Å** cryo-EM structure G_oA complex with bound momSalB, 2.82 Å: 8DZQ G_z complex with bound GR89,696, 2.65 Å: 8DZS G_g complex with bound GR89,696, 2.61 Å: 8DZR	8DZP	Data File Jmol Viewer 8DZP 8DZQ 8DZS 8DZR	Han et al. (2023). Han J, Zhang J, Nazarova AL, Bernhard SM, Krumm BE, Zhao L, Lam JH, Rangari VA, Majumdar S, Nichols DE, Katritch V, Yuan P, Fay JF, & Che T (2023). Ligand and G-protein selectivity in the κ-opioid receptor. Nature 617 7960:417-425. PubMed Id: 37138078. doi:10.1038/s41586-023-06030-7.
*μ-opioid receptor bound to a morphinan antagonist: Mus musculus* E Eukaryota (expressed in S. frugiperda), 2.80 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI.	4DKL	Data File Jmol Viewer 4DKL	Manglik et al. (2012). Manglik A, Kruse AC, Kobilka TS, Thian FS, Mathiesen JM, Sunahara RK, Pardo L, Weis WI, Kobilka BK, & Granier S (2012). Crystal structure of the μ-opioid receptor bound to a morphinan antagonist. Nature 485 :321-326. PubMed Id: 22437502. doi:10.1038/nature10954.
*μ-opioid receptor bound to a morphinan antagonist BU72: Mus musculus* E Eukaryota (expressed in S. frugiperda), 2.10 Å**	5C1M	Data File Jmol Viewer 5C1M	Huang et al. (2015). Huang W, Manglik A, Venkatakrishnan AJ, Laeremans T, Feinberg EN, Sanborn AL, Kato HE, Livingston KE, Thorsen TS, Kling RC, Granier S, Gmeiner P, Husbands SM, Traynor JR, Weis WI, Steyaert J, Dror RO, & Kobilka BK (2015). Structural insights into µ-opioid receptor activation. Nature 524 :315-321. PubMed Id: 26245379. doi:10.1038/nature14886.
*μ-opioid receptor bound to a morphinan antagonist BU72, re-refined structure: Mus musculus* E Eukaryota (expressed in S. frugiperda), 2.10 Å** X-Ray Structure This is an alternative structure of the original PDB code, 5C1M	8E0G	Data File Jmol Viewer 8E0G 5C1M	Munro (2023). Munro TA (2023). Reanalysis of a μ opioid receptor crystal structure reveals a covalent adduct with BU72. BMC Biol 21 1:213. PubMed Id: 37817141. doi:10.1186/s12915-023-01689-w.
*μ-opioid receptor-G_i protein complex with scFv-16: Mus musculus* E Eukaryota (expressed in S. frugiperda), 3.5 Å** cryo-EM structure without scFv-16, 3.5 Å: 6DDF	6DDE	Data File Jmol Viewer 6DDE 6DDF	Koehl et al. (2018). Koehl A, Hu H, Maeda S, Zhang Y, Qu Q, Paggi JM, Latorraca NR, Hilger D, Dawson R, Matile H, Schertler GFX, Granier S, Weis WI, Dror RO, Manglik A, Skiniotis G, & Kobilka BK (2018). Structure of the μ-opioid receptor-G_i protein complex. Nature 558 7711:547-552. PubMed Id: 29899455. doi:10.1038/s41586-018-0219-7.
*μ-opioid receptor-G_i protein complex with bound PZM21: Mus musculus* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure with bound FH210, 3.00 Å: 7SCG	7SBF	Data File Jmol Viewer 7SBF 7SCG	Wang et al. (2022). Wang H, Hetzer F, Huang W, Qu Q, Meyerowitz J, Kaindl J, Hübner H, Skiniotis G, Kobilka BK, & Gmeiner P (2022). Structure-Based Evolution of G Protein-Biased μ-Opioid Receptor Agonists. Angew Chem Int Ed Engl 61 26:e202200269. PubMed Id: 35385593. doi:10.1002/anie.202200269.
*μ-opioid receptor-G_i1 protein complex with bound MP: Mus musculus* E Eukaryota (expressed in Spodoptera frugiperda), 2.50 Å** cryo-EM structure with bound LET, 3.20 Å: 7T2H	7T2G	Data File Jmol Viewer 7T2G 7T2H	Qu et al. (2022). Qu Q, Huang W, Aydin D, Paggi JM, Seven AB, Wang H, Chakraborty S, Che T, DiBerto JF, Robertson MJ, Inoue A, Suomivuori CM, Roth BL, Majumdar S, Dror RO, Kobilka BK, & Skiniotis G (2022). Insights into distinct signaling profiles of the µOR activated by diverse agonists. Nat Chem Biol . PubMed Id: 36411392. doi:10.1038/s41589-022-01208-y.
*μ-opioid receptor bound to an alvimopan and megabody Mb6: Mus musculus* E Eukaryota (expressed in S. frugiperda), 2.80 Å** cryo-EM structure	7UL4	Data File Jmol Viewer 7UL4	Robertson et al. (2022). Robertson MJ, Papasergi-Scott MM, He F, Seven AB, Meyerowitz JG, Panova O, Peroto MC, Che T, & Skiniotis G (2022). Structure determination of inactive-state GPCRs with a universal nanobody. Nat Struct Mol Biol 29 12:1188-1195. PubMed Id: 36396979. doi:10.1038/s41594-022-00859-8.
*μ-opioid receptor-G_i protein complex with bound C5 guano and scFv16: Mus musculus* E Eukaryota (expressed in S. frugiperda), 3.20 Å** cryo-EM structure with bound C6 guano, 3.30 Å: 7U2K	7U2L	Data File Jmol Viewer 7U2L 7U2K	Faouzi et al. (2023). Faouzi A, Wang H, Zaidi SA, DiBerto JF, Che T, Qu Q, Robertson MJ, Madasu MK, El Daibani A, Varga BR, Zhang T, Ruiz C, Liu S, Xu J, Appourchaux K, Slocum ST, Eans SO, Cameron MD, Al-Hasani R, Pan YX, Roth BL, McLaughlin JP, Skiniotis G, Katritch V, Kobilka BK, & Majumdar S (2023). Structure-based design of bitopic ligands for the µ-opioid receptor. Nature 613 7945:767-774. PubMed Id: 36450356. doi:10.1038/s41586-022-05588-y.
*μ-opioid receptor-G_i complex with bound fentanyl: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.30 Å** cryo-EM structure with bound morphine, 3.20 Å: 8EF6 with bound DAMGO, 3.30 Å: 8EFQ with bound SR17018, 3.20 Å: 8EFL with bound PZM21, 2.80 Å: 8EFO with bound TRV130 (oliceridine), 3.20 Å: 8EFB	8EF5	Data File Jmol Viewer 8EF5 8EF6 8EFO 8EFQ 8EFL 8EFB	Zhuang et al. (2022). Zhuang Y, Wang Y, He B, He X, Zhou XE, Guo S, Rao Q, Yang J, Liu J, Zhou Q, Wang X, Liu M, Liu W, Jiang X, Yang D, Jiang H, Shen J, Melcher K, Chen H, Jiang Y, Cheng X, Wang MW, Xie X, & Xu HE (2022). Molecular recognition of morphine and fentanyl by the human μ-opioid receptor. Cell 185 23:4361-4375.e19. PubMed Id: 36368306. doi:10.1016/j.cell.2022.09.041.
*μ-opioid receptor-G_i complex with bound β-endorphin: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.22 Å** cryo-EM structure with bound endomorphin, 3.28 Å: 8F7R	8F7Q	Data File Jmol Viewer 8F7Q 8F7R	Wang et al. (2023). Wang Y, Zhuang Y, DiBerto JF, Zhou XE, Schmitz GP, Yuan Q, Jain MK, Liu W, Melcher K, Jiang Y, Roth BL, & Xu HE (2023). Structures of the entire human opioid receptor family. Cell 186 2:413-427.e17. PubMed Id: 36638794. doi:10.1016/j.cell.2022.12.026.
*δ-opioid receptor in complex with naltrindol: Mus musculus* E Eukaryota (expressed in S. frugiperda), 3.40 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI.	4EJ4	Data File Jmol Viewer 4EJ4	Granier et al. (2012). Granier S, Manglik A, Kruse AC, Kobilka TS, Thian FS, Weis WI, & Kobilka BK (2012). Structure of the δ-opioid receptor bound to naltrindole. Nature 485 :400-404. PubMed Id: 22596164. doi:10.1038/nature11111.
*δ-opioid receptor in complex with naltrindol: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 1.80 Å** Engineered Protein: apocytochrome b₅₆₂ RIL (BRIL) fused at amino terminal of truncated receptor (residues 36-338).	4N6H	Data File Jmol Viewer 4N6H	Fenalti et al. (2014). Fenalti G, Giguere PM, Katritch V, Huang XP, Thompson AA, Cherezov V, Roth BL, & Stevens RC (2014). Molecular control of δ-opioid receptor signalling. Nature 506 :191-196. PubMed Id: 24413399. doi:10.1038/nature12944.
*δ-opioid receptor with bound antagonist/agonist tetrapeptide DIPP-NH₂: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.70 Å** Free electron laser (XFEL) structure. Engineered Protein: apocytochrome b₅₆₂ RIL (BRIL) fused at amino terminal of truncated receptor (residues 39-338). Synchrotron structure, 3.28 Å: 4RWA	4RWD	Data File Jmol Viewer 4RWD 4RWA	Fenalti et al. (2015). Fenalti G, Zatsepin NA, Betti C, Giguere P, Han GW, Ishchenko A, Liu W, Guillemyn K, Zhang H, James D, Wang D, Weierstall U, Spence JC, Boutet S, Messerschmidt M, Williams GJ, Gati C, Yefanov OM, White TA, Oberthuer D, Metz M, Yoon CH, Barty A, Chapman HN, Basu S, Coe J, Conrad CE, Fromme R, Fromme P, Tourwé D, Schiller PW, Roth BL, Ballet S, Katritch V, Stevens RC, & Cherezov V (2015). Structural basis for bifunctional peptide recognition at human ?-opioid receptor. Nat Struct Mol Biol 22 3:265-268. PubMed Id: 25686086. doi:10.1038/nsmb.2965.
*δ-opioid receptor in complex with the peptide agonist KGCHM07: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.8 Å** Engineered protein: apocytochrome b₅₆₂ RIL (BRIL) fused at amino terminal of truncated receptor. In complex with the small molecule agonist DPI-287, 3.3 Å: 6PT3	6PT2	Data File Jmol Viewer 6PT2 6PT3	Claff et al. (2019). Claff T, Yu J, Blais V, Patel N, Martin C, Wu L, Han GW, Holleran BJ, Van der Poorten O, White KL, Hanson MA, Sarret P, Gendron L, Cherezov V, Katritch V, Ballet S, Liu ZJ, Müller CE, & Stevens RC (2019). Elucidating the active ?-opioid receptor crystal structure with peptide and small-molecule agonists. Sci Adv 5 11. PubMed Id: 31807708. doi:10.1126/sciadv.aax9115.
*δ-opioid receptor-G_i complex with bound deltorphin: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.00 Å** cryo-EM structure	8F7S	Data File Jmol Viewer 8F7S	Wang et al. (2023). Wang Y, Zhuang Y, DiBerto JF, Zhou XE, Schmitz GP, Yuan Q, Jain MK, Liu W, Melcher K, Jiang Y, Roth BL, & Xu HE (2023). Structures of the entire human opioid receptor family. Cell 186 2:413-427.e17. PubMed Id: 36638794. doi:10.1016/j.cell.2022.12.026.
*CB₁ cannabinoid receptor complexed with stabilizing antagonist AM6538: Homo sapiens* E Eukaryota (expressed in HEK293F cells), 2.80 Å** Engineered protein: Y98W Flavodoxin fused to third intracellular loop.	5TGZ	Data File Jmol Viewer 5TGZ	Hua et al. (2016). Hua T, Vemuri K, Pu M, Qu L, Han GW, Wu Y, Zhao S, Shui W, Li S, Korde A, Laprairie RB, Stahl EL, Ho JH, Zvonok N, Zhou H, Kufareva I, Wu B, Zhao Q, Hanson MA, Bohn LM, Makriyannis A, Stevens RC, & Liu ZJ (2016). Crystal Structure of the Human Cannabinoid Receptor CB1. Cell 167 :750-762.e14. PubMed Id: 27768894. doi:10.1016/j.cell.2016.10.004.
*CB₁ cannabinoid receptor with bound ORG27569 (NAM) and CP55940 agonist: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.24 Å** Engineered protein. NAM = negative allosteric modulator	6KQI	Data File Jmol Viewer 6KQI	Shao et al. (2019). Shao Z, Yan W, Chapman K, Ramesh K, Ferrell AJ, Yin J, Wang X, Xu Q, & Rosenbaum DM (2019). Structure of an allosteric modulator bound to the CB1 cannabinoid receptor. Nat Chem Biol 15 12:1199-1205. PubMed Id: 31659318. doi:10.1038/s41589-019-0387-2.
*CB₁ cannabinoid receptor with bound inhibitor taranabant: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.6 Å** Engineered protein: Pyrococcus abysii glycogen synthase replaced the 3rd intracellular loop. N-terminal 89 residues deleted. T210A point mutation.	5U09	Data File Jmol Viewer 5U09	Shao et al. (2016). Shao Z, Yin J, Chapman K, Grzemska M, Clark L, Wang J, & Rosenbaum DM (2016). High-resolution crystal structure of the human CB1 cannabinoid receptor. Nature 540 :602-606. PubMed Id: 27851727. doi:10.1038/nature20613.
*CB₁ cannabinoid receptor with bound MDMB-Fubinaca: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3 Å** cryo-EM structure	6N4B	Data File Jmol Viewer 6N4B	Krishna Kumar et al. (2019). Krishna Kumar K, Shalev-Benami M, Robertson MJ, Hu H, Banister SD, Hollingsworth SA, Latorraca NR, Kato HE, Hilger D, Maeda S, Weis WI, Farrens DL, Dror RO, Malhotra SV, Kobilka BK, & Skiniotis G (2019). Structure of a Signaling Cannabinoid Receptor 1-G Protein Complex. Cell 176 3:448-458.e12. PubMed Id: 30639101. doi:10.1016/j.cell.2018.11.040.
*CB₁ cannabinoid receptor complexed with G protein and AM841: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3 Å** cryo-EM structure	6KPG	Data File Jmol Viewer 6KPG	Hua et al. (2020). Hua T, Li X, Wu L, Iliopoulos-Tsoutsouvas C, Wang Y, Wu M, Shen L, Johnston CA, Nikas SP, Song F, Song X, Yuan S, Sun Q, Wu Y, Jiang S, Grim TW, Benchama O, Stahl EL, Zvonok N, Zhao S, Bohn LM, Makriyannis A, & Liu ZJ (2020). Activation and Signaling Mechanism Revealed by Cannabinoid Receptor-G_i Complex Structures. Cell 180 4:655-665.e18. PubMed Id: 32004463. doi:10.1016/j.cell.2020.01.008.
*CB₁ cannabinoid receptor complexed wih AM11542: Homo sapiens* E Eukaryota (expressed in HEK293F cells), 2.8 Å** Engineered protein: Y98W Flavodoxin fused to third intracellular loop. Truncated residues 1-98, 303-331, & 415-472 in complex with AM841 agonist, 2.95 Å: 5XR8	5XRA	Data File Jmol Viewer 5XRA 5XR8	Hua et al. (2017). Hua T, Vemuri K, Nikas SP, Laprairie RB, Wu Y, Qu L, Pu M, Korde A, Jiang S, Ho JH, Han GW, Ding K, Li X, Liu H, Hanson MA, Zhao S, Bohn LM, Makriyannis A, Stevens RC, & Liu ZJ (2017). Crystal structures of agonist-bound human cannabinoid receptor CB1. Nature 547 :468-471. PubMed Id: 28678776. doi:10.1038/nature23272.
*CB₁ cannabinoid receptor complexed wih CP55940 and ZCZ011: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.70 Å** with bound G_i protein, cryo-EM structure, 3.36 Å: 7WV9	7FEE	Data File Jmol Viewer 7FEE 7WV9	Yang et al. (2022). Yang X, Wang X, Xu Z, Wu C, Zhou Y, Wang Y, Lin G, Li K, Wu M, Xia A, Liu J, Cheng L, Zou J, Yan W, Shao Z, & Yang S (2022). Molecular mechanism of allosteric modulation for the cannabinoid receptor CB1. Nat Chem Biol 18 8:831-840. PubMed Id: 35637350. doi:10.1038/s41589-022-01038-y.
*CB₁-G_i cannabinoid receptor complex with bound AMG315: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.80 Å** cryo-EM structure	8GHV	Data File Jmol Viewer 8GHV	Krishna Kumar et al. (2023). Krishna Kumar K, Robertson MJ, Thadhani E, Wang H, Suomivuori CM, Powers AS, Ji L, Nikas SP, Dror RO, Inoue A, Makriyannis A, Skiniotis G, & Kobilka B (2023). Structural basis for activation of CB1 by an endocannabinoid analog. Nat Commun 14 1:2672. PubMed Id: 37160876. doi:10.1038/s41467-023-37864-4.
*CB₂ cannabinoid receptor complexed with antagonist AM10257: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.8 Å**	5ZTY	Data File Jmol Viewer 5ZTY	Li et al. (2019). Li X, Hua T, Vemuri K, Ho JH, Wu Y, Wu L, Popov P, Benchama O, Zvonok N, Locke K, Qu L, Han GW, Iyer MR, Cinar R, Coffey NJ, Wang J, Wu M, Katritch V, Zhao S, Kunos G, Bohn LM, Makriyannis A, Stevens RC, & Liu ZJ (2019). Crystal Structure of the Human Cannabinoid Receptor CB2. Cell 176 3:459-467.e13. PubMed Id: 30639103. doi:10.1016/j.cell.2018.12.011.
*CB₂ cannabinoid receptor complexed with antagonist AM12033: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.2 Å** complexed with G-protein (cryo-EM structure), 2.9 Å: 6KPF	6KPC	Data File Jmol Viewer 6KPC 6KPF	Hua et al. (2020). Hua T, Li X, Wu L, Iliopoulos-Tsoutsouvas C, Wang Y, Wu M, Shen L, Johnston CA, Nikas SP, Song F, Song X, Yuan S, Sun Q, Wu Y, Jiang S, Grim TW, Benchama O, Stahl EL, Zvonok N, Zhao S, Bohn LM, Makriyannis A, & Liu ZJ (2020). Activation and Signaling Mechanism Revealed by Cannabinoid Receptor-G_i Complex Structures. Cell 180 4:655-665.e18. PubMed Id: 32004463. doi:10.1016/j.cell.2020.01.008.
*CB₂-G_i cannabinoid receptor complex: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.2 Å** cryo-EM structure	6PT0	Data File Jmol Viewer 6PT0	Xing et al. (2020). Xing C, Zhuang Y, Xu TH, Feng Z, Zhou XE, Chen M, Wang L, Meng X, Xue Y, Wang J, Liu H, McGuire TF, Zhao G, Melcher K, Zhang C, Xu HE, & Xie XQ (2020). Cryo-EM Structure of the Human Cannabinoid Receptor CB2-G_i Signaling Complex. Cell 180 4:645-654.e13. PubMed Id: 32004460. doi:10.1016/j.cell.2020.01.007.
*CB₂-G_i cannabinoid receptor complex with bound LEI-102: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.98 Å** cryo-EM structure with bound APD371, 3.08 Å: 8GUQ with bound HU308, 2.97 Å: 8GUS with bound CP55,940, 2.84 Å: 8GUR	8GUT	Data File Jmol Viewer 8GUT 8GUS 8GUQ 8GUR	Li et al. (2023). Li X, Chang H, Bouma J, de Paus LV, Mukhopadhyay P, Paloczi J, Mustafa M, van der Horst C, Kumar SS, Wu L, Yu Y, van den Berg RJBHN, Janssen APA, Lichtman A, Liu ZJ, Pacher P, van der Stelt M, Heitman LH, & Hua T (2023). Structural basis of selective cannabinoid CB2 receptor activation. Nat Commun 14 1:1447. PubMed Id: 36922494. doi:10.1038/s41467-023-37112-9.
*Nociceptin/orphanin FQ (N/OFQ) receptor with bound peptide: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.01 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI.	4EA3	Data File Jmol Viewer 4EA3	Thompson et al. (2012). Thompson AA, Liu W, Chun E, Katritch V, Wu H, Vardy E, Huang XP, Trapella C, Guerrini R, Calo G, Roth BL, Cherezov V, & Stevens RC (2012). Structure of the nociceptin/orphanin FQ receptor in complex with a peptide mimetic. Nature 485 :395-399. PubMed Id: 22596163. doi:10.1038/nature11085.
*Nociceptin/orphanin FQ (N/OFQ) receptor with bound C-35: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.0 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI. with bound SB-612111, 3.0 Å: 5DHH	5DHG	Data File Jmol Viewer 5DHG 5DHH	Miller et al. (2015). Miller RL, Thompson AA, Trapella C, Guerrini R, Malfacini D, Patel N, Han GW, Cherezov V, Caló G, Katritch V, & Stevens RC (2015). The Importance of Ligand-Receptor Conformational Pairs in Stabilization: Spotlight on the N/OFQ G Protein-Coupled Receptor. Structure 23 :2291-2299. PubMed Id: 26526853. doi:10.1016/j.str.2015.07.024.
*Nociceptin/orphanin FQ (N/OFQ) receptor-G_i complex with bound nociceptin peptide: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.28 Å** cryo-EM structure	8F7X	Data File Jmol Viewer 8F7X	Wang et al. (2023). Wang Y, Zhuang Y, DiBerto JF, Zhou XE, Schmitz GP, Yuan Q, Jain MK, Liu W, Melcher K, Jiang Y, Roth BL, & Xu HE (2023). Structures of the entire human opioid receptor family. Cell 186 2:413-427.e17. PubMed Id: 36638794. doi:10.1016/j.cell.2022.12.026.
*NTSR1 neurotensin receptor in complex with neurotensin: Rattus norvegicus* E Eukaryota (expressed in Trichoplusia ni), 2.80 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI.	4GRV	Data File Jmol Viewer 4GRV	White et al. (2012). White JF, Noinaj N, Shibata Y, Love J, Kloss B, Xu F, Gvozdenovic-Jeremic J, Shah P, Shiloach J, Tate CG, & Grisshammer R (2012). Structure of the agonist-bound neurotensin receptor. Nature 490 :508-513. PubMed Id: 23051748. doi:10.1038/nature11558.
*NTSR1 neurotensin receptor produced by direct evolution, agonist bound (TM86V-ΔIC3B mutant): Rattus norvegicus* E Eukaryota (expressed in E. coli), 2.75 Å** These proteins are not stabilized by a T4 lysozyme insertion. TM86V-ΔIC3A mutant, 3.00 Å: 3ZEV OGG7-ΔIC3A mutant, 3.10 Å: 4BV0 HTHGH4-ΔIC3 mutant, 3.57 Å: 4BWB	4BUO	Data File Jmol Viewer 4BUO 4BV0 3ZEV 4BWB	Egloff et al. (2014). Egloff P, Hillenbrand M, Klenk C, Batyuk A, Heine P, Balada S, Schlinkmann KM, Scott DJ, Schütz M, & Plückthun A (2014). Structure of signaling-competent neurotensin receptor 1 obtained by directed evolution in Escherichia coli. Proc Natl Acad Sci USA 111 :E655–E662. PubMed Id: 24453215. doi:10.1073/pnas.1317903111.
*NTSR1 neurotensin receptor in active-like state: Rattus norvegicus* E Eukaryota (expressed in Trichoplusia ni), 2.90 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI, 2.60 Å: 4XES	4XEE	Data File Jmol Viewer 4XEE 4XES	Krumm et al. (2015). Krumm BE, White JF, Shah P, & Grisshammer R (2015). Structural prerequisites for G-protein activation by the neurotensin receptor. Nat Commun 6 :7895. PubMed Id: 26205105. doi:10.1038/ncomms8895.
*NTSR1 neurotensin receptor, NTSR1-EL constitutively active mutant: Rattus norvegicus* E Eukaryota (expressed in Trichoplusia ni), 3.3 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI plus six thermostabilizing mutations.	5T04	Data File Jmol Viewer 5T04	Krumm et al. (2016). Krumm BE, Lee S, Bhattacharya S, Botos I, White CF, Du H, Vaidehi N, & Grisshammer R (2016). Structure and dynamics of a constitutively active neurotensin receptor. Sci Rep 6 :38564. PubMed Id: 27924846. doi:10.1038/srep38564.
*NTSR1 neurotensin receptor in complex with the peptide full agonist NTS8-13: Rattus norvegicus* E Eukaryota (expressed in E. coli), 2.46 Å** Engineered protein. See publication. in complex with the small-molecule full agonist SRI-9829, 2.80 Å: 6Z8N in complex with the small-molecule partial agonist RTI-3a, 2.72 Å: 6ZA8 in complex with the small molecule inverse agonist SR48692, 2.64 Å: 6ZIN in complex with the small-molecule inverse agonist SR142948A, 2.92 Å: 6Z4Q NTSR1-H4bmx construct in complex with NTS8-13, 2.60 Å: 6Z4V	6YVR	Data File Jmol Viewer 6YVR 6Z4Q 6ZA8 6Z8N 6Z4V 6ZIN	Deluigi et al. (2021). Deluigi M, Klipp A, Klenk C, Merklinger L, Eberle SA, Morstein L, Heine P, Mittl PRE, Ernst P, Kamenecka TM, He Y, Vacca S, Egloff P, Honegger A, & Plückthun A (2021). Complexes of the neurotensin receptor 1 with small-molecule ligands reveal structural determinants of full, partial, and inverse agonism. Sci Adv 7 5:eabe5504. PubMed Id: 33571132. doi:10.1126/sciadv.abe5504.
*NTSR1 neurotensin receptor G_i complex in lipid nanodisc (canonical state, no AHD): Rattus norvegicus* E Eukaryota (expressed in Spodoptera frugiperda), 4.10 Å** cryo-EM structure canonical state, with AHD, 4.30 Å: 7L0Q noncanonical state, without AHD, 4.20 Å: 7L0R noncanonical state, with AHD, 4.50 Å: 7L0S	7L0P	Data File Jmol Viewer 7L0P 7L0Q 7L0S 7L0R	Zhang et al. (2021). Zhang M, Gui M, Wang ZF, Gorgulla C, Yu JJ, Wu H, Sun ZJ, Klenk C, Merklinger L, Morstein L, Hagn F, Plückthun A, Brown A, Nasr ML, & Wagner G (2021). Cryo-EM structure of an activated GPCR-G protein complex in lipid nanodiscs. Nat Struct Mol Biol 28 3:258-267. PubMed Id: 33633398. doi:10.1038/s41594-020-00554-6.
*NTSR1 neurotensin receptor - G_oA complex: Rattus norvegicus* E Eukaryota (expressed in S. frugiperda), 2.88 Å** cryo-EM structure G_oA complex with bound SBI-553, 2.89 Å: 8FN0 G_q complex, 2.59 Å: 8FMZ	8FN1	Data File Jmol Viewer 8FN1 8FN0 8FMZ	Krumm et al. (2023). Krumm BE, DiBerto JF, Olsen RHJ, Kang HJ, Slocum ST, Zhang S, Strachan RT, Huang XP, Slosky LM, Pinkerton AB, Barak LS, Caron MG, Kenakin T, Fay JF, & Roth BL (2023). Neurotensin Receptor Allosterism Revealed in Complex with a Biased Allosteric Modulator. Biochemistry 62 7:1233-1248. PubMed Id: 36917754. doi:10.1021/acs.biochem.3c00029.
*NTSR1 neurotensin receptor in complex with G_i1 hetero trimer, canonical conformation (C state): Homo sapiens* E Eukaryota (expressed in S. frugiperda (NTSR1) and Trichoplusia ni (G_i1)), 3 Å** cryo-EM structure non-canonical (NC) state, 3 Å: 6OSA	6OS9	Data File Jmol Viewer 6OS9 6OSA	Kato et al. (2019). Kato HE, Zhang Y, Hu H, Suomivuori CM, Kadji FMN, Aoki J, Krishna Kumar K, Fonseca R, Hilger D, Huang W, Latorraca NR, Inoue A, Dror RO, Kobilka BK, & Skiniotis G (2019). Conformational transitions of a neurotensin receptor 1-G_i1 complex. Nature 572 7767:80-85. PubMed Id: 31243364. doi:10.1038/s41586-019-1337-6.
*NTSR1 neurotensin receptor in complex with Arrestin-2: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 4.9 Å** cryo-EM structure	6PWC	Data File Jmol Viewer 6PWC	Yin et al. (2019). Yin W, Li Z, Jin M, Yin YL, de Waal PW, Pal K, Yin Y, Gao X, He Y, Gao J, Wang X, Zhang Y, Zhou H, Melcher K, Jiang Y, Cong Y, Edward Zhou X, Yu X, & Eric Xu H (2019). A complex structure of arrestin-2 bound to a G protein-coupled receptor. Cell Res 29 12:971-983. PubMed Id: 31776446. doi:10.1038/s41422-019-0256-2.
*NTSR1 neurotensin receptor in complex with β-arrestin1: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 4.2 Å** Cryo-EM structure	6UP7	Data File Jmol Viewer 6UP7	Huang et al. (2020). Huang W, Masureel M, Qu Q, Janetzko J, Inoue A, Kato HE, Robertson MJ, Nguyen KC, Glenn JS, Skiniotis G, & Kobilka BK (2020). Structure of the neurotensin receptor 1 in complex with β-arrestin 1. Nature 579 7798:303-308. PubMed Id: 31945771. doi:10.1038/s41586-020-1953-1.
*NTSR1 neurotensin receptor in complex with SR48692 and nanobody Nb6: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.40 Å** cryo-EM structure	7UL2	Data File Jmol Viewer 7UL2	Robertson et al. (2022). Robertson MJ, Papasergi-Scott MM, He F, Seven AB, Meyerowitz JG, Panova O, Peroto MC, Che T, & Skiniotis G (2022). Structure determination of inactive-state GPCRs with a universal nanobody. Nat Struct Mol Biol 29 12:1188-1195. PubMed Id: 36396979. doi:10.1038/s41594-022-00859-8.
*Neuropeptide Y Y₁ receptor with bound UR-MK299: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.7 Å** with bound BMS-193885, 3 Å: 5ZBH	5ZBQ	Data File Jmol Viewer 5ZBQ 5ZBH	Yang et al. (2018). Yang Z, Han S, Keller M, Kaiser A, Bender BJ, Bosse M, Burkert K, Kögler LM, Wifling D, Bernhardt G, Plank N, Littmann T, Schmidt P, Yi C, Li B, Ye S, Zhang R, Xu B, Larhammar D, Stevens RC, Huster D, Meiler J, Zhao Q, Beck-Sickinger AG, Buschauer A, & Wu B (2018). Structural basis of ligand binding modes at the neuropeptide Y Y1 receptor. Nature 556 7702:520-524. PubMed Id: 29670288. doi:10.1038/s41586-018-0046-x.
*Neuropeptide Y Y₁ - G Protein complex with bound peptide-agonist Neuropeptide Y (NPY): Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** cryo-EM structure	7VGX	Data File Jmol Viewer 7VGX	Park et al. (2022). Park C, Kim J, Ko SB, Choi YK, Jeong H, Woo H, Kang H, Bang I, Kim SA, Yoon TY, Seok C, Im W, & Choi HJ (2022). Structural basis of neuropeptide Y signaling through Y1 receptor. Nat Commun 13 1:853. PubMed Id: 35165283. doi:10.1038/s41467-022-28510-6.
*Neuropeptide Y Y₁ - G_i Protein complex with bound NPY: homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.20 Å** cryo-EM structure	7X9A	Data File Jmol Viewer 7X9A	Tang et al. (2022). Tang T, Tan Q, Han S, Diemar A, Löbner K, Wang H, Schüß C, Behr V, Mörl K, Wang M, Chu X, Yi C, Keller M, Kofoed J, Reedtz-Runge S, Kaiser A, Beck-Sickinger AG, Zhao Q, & Wu B (2022). Receptor-specific recognition of NPY peptides revealed by structures of NPY receptors. Sci Adv 8 18:eabm1232. PubMed Id: 35507650. doi:10.1126/sciadv.abm1232.
*Neuropeptide Y Y₂ receptor with bound selective antagonist JNJ-31020028: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.80 Å** Engineered protein: 28 AAs (S354-V381) removed at C-terminus. T4 lysozyme fused at N-terminus. Residues S251-N256 in 3rd intracellular loop replaced with flavodoxin.	7DDZ	Data File Jmol Viewer 7DDZ	Tang et al. (2021). Tang T, Hartig C, Chen Q, Zhao W, Kaiser A, Zhang X, Zhang H, Qu H, Yi C, Ma L, Han S, Zhao Q, Beck-Sickinger AG, & Wu B (2021). Structural basis for ligand recognition of the neuropeptide Y Y₂ receptor. Nat Commun 12 1:737. PubMed Id: 33531491. doi:10.1038/s41467-021-21030-9.
*Neuropeptide Y Y₂ - G_i Protein complex with bound NPY: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.40 Å** cryo-EM structure	7X9B	Data File Jmol Viewer 7X9B	Tang et al. (2022). Tang T, Tan Q, Han S, Diemar A, Löbner K, Wang H, Schüß C, Behr V, Mörl K, Wang M, Chu X, Yi C, Keller M, Kofoed J, Reedtz-Runge S, Kaiser A, Beck-Sickinger AG, Zhao Q, & Wu B (2022). Receptor-specific recognition of NPY peptides revealed by structures of NPY receptors. Sci Adv 8 18:eabm1232. PubMed Id: 35507650. doi:10.1126/sciadv.abm1232.
*Neuropeptide Y Y₂ - G_i Protein complex with bound PYY (3-36): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.95 Å** cryo-EM structure with bound NPY, 3.11 Å: 7YOO	7YON	Data File Jmol Viewer 7YON 7YOO	Kang et al. (2023). Kang H, Park C, Choi YK, Bae J, Kwon S, Kim J, Choi C, Seok C, Im W, & Choi HJ (2023). Structural basis for Y2 receptor-mediated neuropeptide Y and peptide YY signaling. Structure 31 1:44-57.e6. PubMed Id: 36525977. doi:10.1016/j.str.2022.11.010.
*Neuropeptide Y Y₄ - G_i Protein complex with bound PP: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.00 Å** cryo-EM structure	7X9C	Data File Jmol Viewer 7X9C	Tang et al. (2022). Tang T, Tan Q, Han S, Diemar A, Löbner K, Wang H, Schüß C, Behr V, Mörl K, Wang M, Chu X, Yi C, Keller M, Kofoed J, Reedtz-Runge S, Kaiser A, Beck-Sickinger AG, Zhao Q, & Wu B (2022). Receptor-specific recognition of NPY peptides revealed by structures of NPY receptors. Sci Adv 8 18:eabm1232. PubMed Id: 35507650. doi:10.1126/sciadv.abm1232.
*Protease-activated receptor 1 (PAR1) bound with antagonist vorapaxar: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.20 Å** Engineered protein: T4 lysozyme inserted between TM helices V and VI.	3VW7	Data File Jmol Viewer 3VW7	Zhang et al. (2012). Zhang C, Srinivasan Y, Arlow DH, Fung JJ, Palmer D, Zheng Y, Green HF, Pandey A, Dror RO, Shaw DE, Weis WI, Coughlin SR, & Kobilka BK (2012). High-resolution crystal structure of human protease-activated receptor 1. Nature 492 :387-392. PubMed Id: 23222541. doi:10.1038/nature11701.
*Protease-activated receptor 2 (PAR2) with bound AZ8838: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.80 Å** with bound AZ3451, 3.60 Å: 5NDZ with bound Fab3949 and AZ7188, 4.00 Å: 5NJ6	5NDD	Data File Jmol Viewer 5NDD 5NDZ 5NJ6	Cheng et al. (2017). Cheng RKY, Fiez-Vandal C, Schlenker O, Edman K, Aggeler B, Brown DG, Brown GA, Cooke RM, Dumelin CE, Doré AS, Geschwindner S, Grebner C, Hermansson NO, Jazayeri A, Johansson P, Leong L, Prihandoko R, Rappas M, Soutter H, Snijder A, Sundström L, Tehan B, Thornton P, Troast D, Wiggin G, Zhukov A, Marshall FH, & Dekker N (2017). Structural insight into allosteric modulation of protease-activated receptor 2. Nature 545 7652:112-115. PubMed Id: 28445455. doi:10.1038/nature22309.
*Apelin receptor (AR) TM helix 1 in DPC micelles: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure** The TM helix includes residues 1-55. structure in SDS micelles, 2LOT structure in LPPG micelles, 2LOV structure in 50% HFIP, 2LOW	2LOU	Data File Jmol Viewer 2LOU 2LOW 2LOT 2LOV	Langelaan et al. (2013). Langelaan DN, Reddy T, Banks AW, Dellaire G, Dupré DJ, & Rainey JK (2013). Structural features of the apelin receptor N-terminal tail and first transmembrane segment implicated in ligand binding and receptor trafficking. Biochim Biophys Acta 1828 :1471-1483. PubMed Id: 23438363. doi:10.1016/j.bbamem.2013.02.005.
*Apelin receptor (angiotensin II protein J receptor [APJR]) in complex with apelin-17 mimetic peptide: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.6 Å**	5VBL	Data File Jmol Viewer 5VBL	Ma et al. (2017). Ma Y, Yue Y, Ma Y, Zhang Q, Zhou Q, Song Y, Shen Y, Li X, Ma X, Li C, Hanson MA, Han GW, Sickmier EA, Swaminath G, Zhao S, Stevens RC, Hu LA, Zhong W, Zhang M, & Xu F (2017). Structural Basis for Apelin Control of the Human Apelin Receptor. Structure 25 :858-866.e4. PubMed Id: 28528775. doi:10.1016/j.str.2017.04.008.
*Apelin receptor (angiotensin II protein J receptor [APJR]) - G_i complex, dimeric APJR, with bound compound 644: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.57 Å** cryo-EM structure monomeric APJR, with bound compound 644, 3.71 Å: 7W0M dimeric APJR, with bound peptide ELA, 4.21 Å 7W0N monomeric APJR, with bound compound 644, 3.78 Å: 7W0O monomeric APJR, F101A mutant, with bound peptide ELA, 3.16 Å, 7W0P x-ray, APJR in complex with compound 644, 2.70 Å: 7SUS	7W0L	Data File Jmol Viewer 7W0L 7SUS 7W0O 7W0M 7W0P	Yue et al. (2022). Yue Y, Liu L, Wu LJ, Wu Y, Wang L, Li F, Liu J, Han GW, Chen B, Lin X, Brouillette RL, Breault É:, Longpré: JM, Shi S, Lei H, Sarret P, Stevens RC, Hanson MA, & Xu F (2022). Structural insight into apelin receptor-G protein stoichiometry. Nat Struct Mol Biol 29 7:688-697. PubMed Id: 35817871. doi:10.1038/s41594-022-00797-5.
*5-HT_1A-G_i serotonin receptor complex, apo state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å** cryo-EM structure with bound Serotonin, 3.00 Å: 7E2Y with bound Aripiprazole, 3.10 Å: 7E2Z	7E2X	Data File Jmol Viewer 7E2X 7E2Y 7E2Z	Xu et al. (2021). Xu P, Huang S, Zhang H, Mao C, Zhou XE, Cheng X, Simon IA, Shen DD, Yen HY, Robinson CV, Harpsøe K, Svensson B, Guo J, Jiang H, Gloriam DE, Melcher K, Jiang Y, Zhang Y, & Xu HE (2021). Structural insights into the lipid and ligand regulation of serotonin receptors. Nature 592 7854:469-473. PubMed Id: 33762731. doi:10.1038/s41586-021-03376-8.
*5-HT_1A-G_i serotonin receptor complex with bound Ulotaront(SEP-363856): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.65 Å** cryo-EM structure	8JSP	Data File Jmol Viewer 8JSP	Xu et al. (2023). Xu Z, Guo L, Yu J, Shen S, Wu C, Zhang W, Zhao C, Deng Y, Tian X, Feng Y, Hou H, Su L, Wang H, Guo S, Wang H, Wang K, Chen P, Zhao J, Zhang X, Yong X, Cheng L, Liu L, Yang S, Yang F, Wang X, Yu X, Xu Y, Sun JP, Yan W, & Shao Z (2023). Ligand recognition and G-protein coupling of trace amine receptor TAAR1. Nature . PubMed Id: 37935376. doi:10.1038/s41586-023-06804-z.
*5-HT_1A-G_i serotonin receptor complex, with bound SEP-363856: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.00 Å** cryo-EM structure	8W8B	Data File Jmol Viewer 8W8B	Liu et al. (2023). Liu H, Zheng Y, Wang Y, Wang Y, He X, Xu P, Huang S, Yuan Q, Zhang X, Wang L, Jiang K, Chen H, Li Z, Liu W, Wang S, Xu HE, & Xu F (2023). Recognition of methamphetamine and other amines by trace amine receptor TAAR1. Nature 624 7992:663-671. PubMed Id: 37935377. doi:10.1038/s41586-023-06775-1.
*5-HT_1B serotonin receptor with bound ergotamine: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.70 Å** Engineered Protein: apocytochrome b₅₆₂ RIL (BRIL) replaces cytoplasmic loop 3 (L240-M305). With bound dihydroergotamine, 2.80 Å: 4IAQ	4IAR	Data File Jmol Viewer 4IAR 4IAQ	Wang et al. (2013). Wang C, Jiang Y, Ma J, Wu H, Wacker D, Katritch V, Han GW, Liu W, Huang XP, Vardy E, McCorvy JD, Gao X, Zhou XE, Melcher K, Zhang C, Bai F, Yang H, Yang L, Jiang H, Roth BL, Cherezov V, Stevens RC, & Xu HE (2013). Structural basis for molecular recognition at serotonin receptors. Science 340 :610-614. PubMed Id: 23519210. doi:10.1126/science.1232807.
*5-HT_1B serotonin receptor with bound donitriptan coupled to heterotrimeric G_o: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.78 Å** cryo-EM structure	6G79	Data File Jmol Viewer 6G79	García-Nafría et al. (2018). García-Nafría J, Nehmé R, Edwards PC, & Tate CG (2018). Cryo-EM structure of the serotonin 5-HT_1B receptor coupled to heterotrimeric G_o. Nature 558 7711:620-623. PubMed Id: 29925951. doi:10.1038/s41586-018-0241-9.
*5-HT_1B serotonin receptor with SRP2070_Fab complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å** Engineered Protein: apocytochrome b₅₆₂ RIL (BRIL) replaces cytoplasmic loop 3 (L240-M305).	7C61	Data File Jmol Viewer 7C61	Miyagi et al. (2020). Miyagi H, Asada H, Suzuki M, Takahashi Y, Yasunaga M, Suno C, Iwata S, & Saito JI (2020). The discovery of a new antibody for BRIL-fused GPCR structure determination. Sci Rep 10 1:11669. PubMed Id: 32669569. doi:10.1038/s41598-020-68355-x.
*5-HT_1D-G_i serotonin receptor complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure	7E32	Data File Jmol Viewer 7E32	Xu et al. (2021). Xu P, Huang S, Zhang H, Mao C, Zhou XE, Cheng X, Simon IA, Shen DD, Yen HY, Robinson CV, Harpsøe K, Svensson B, Guo J, Jiang H, Gloriam DE, Melcher K, Jiang Y, Zhang Y, & Xu HE (2021). Structural insights into the lipid and ligand regulation of serotonin receptors. Nature 592 7854:469-473. PubMed Id: 33762731. doi:10.1038/s41586-021-03376-8.
*5-HT_1E-G_i serotonin receptor complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure	7E33	Data File Jmol Viewer 7E33	Xu et al. (2021). Xu P, Huang S, Zhang H, Mao C, Zhou XE, Cheng X, Simon IA, Shen DD, Yen HY, Robinson CV, Harpsøe K, Svensson B, Guo J, Jiang H, Gloriam DE, Melcher K, Jiang Y, Zhang Y, & Xu HE (2021). Structural insights into the lipid and ligand regulation of serotonin receptors. Nature 592 7854:469-473. PubMed Id: 33762731. doi:10.1038/s41586-021-03376-8.
*5-HT_1F-G_i serotonin receptor complex: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.40 Å** cryo-EM structure	7EXD	Data File Jmol Viewer 7EXD	Huang et al. (2021). Huang S, Xu P, Tan Y, You C, Zhang Y, Jiang Y, & Xu HE (2021). Structural basis for recognition of anti-migraine drug lasmiditan by the serotonin receptor 5-HT1F-G protein complex. Cell Res . PubMed Id: 34239069. doi:10.1038/s41422-021-00527-4.
*5-HT_2A serotonin receptor with bound risperidone: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3 Å** with bound zotepine, 2.9 Å: 6A94	6A93	Data File Jmol Viewer 6A93 6A94	Kimura et al. (2019). Kimura KT, Asada H, Inoue A, Kadji FMN, Im D, Mori C, Arakawa T, Hirata K, Nomura Y, Nomura N, Aoki J, Iwata S, & Shimamura T (2019). Structures of the 5-HT_2A receptor in complex with the antipsychotics risperidone and zotepine. Nat Struct Mol Biol 26 2:121-128. PubMed Id: 30723326. doi:10.1038/s41594-018-0180-z.
*5-HT_2A serotonin receptor complexed with G_αq and hallucinogen: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.36 Å** cryo-EM structure x-ray: 5-HT_2A with hallucinogenic agonist, 3.40 Å: 6WGT x-ray: 5-HT_2A with inverse agonist, 3.40 Å: 6WH4	6WHA	Data File Jmol Viewer 6WHA 6WH4 6WGT	Kim et al. (2020). Kim K, Che T, Panova O, DiBerto JF, Lyu J, Krumm BE, Wacker D, Robertson MJ, Seven AB, Nichols DE, Shoichet BK, Skiniotis G, & Roth BL (2020). Structure of a Hallucinogen-Activated Gq-Coupled 5-HT2A Serotonin Receptor. Cell 182 6:1574-1588.e19. PubMed Id: 32946782. doi:10.1016/j.cell.2020.08.024.
*5-HT_2A serotonin receptor with bound cariprazine: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.30 Å** with bound aripiprazole, 2.90 Å 7VOE	7VOD	Data File Jmol Viewer 7VOD 7VOE	Chen et al. (2022). Chen Z, Fan L, Wang H, Yu J, Lu D, Qi J, Nie F, Luo Z, Liu Z, Cheng J, & Wang S (2022). Structure-based design of a novel third-generation antipsychotic drug lead with potential antidepressant properties. Nat Neurosci 25 1:39-49. PubMed Id: 34887590. doi:10.1038/s41593-021-00971-w.
*5-HT_2A serotonin receptor in complex with serotonin: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** in complex with psilocin, 3.20 Å 7WC5 in complex with LSD, 2.60 Å 7WC6 in complex with lisuride, 2.60 Å 7WC7 in complex with lumateperone, 2.45 Å 7WC8 in complex with non-hallucinogenic psychedelic analog, 2.50 Å 7WC9	7WC4	Data File Jmol Viewer 7WC4 7WC5 7WC7 7WC8 7WC9 7WC6	Cao et al. (2022). Cao D, Yu J, Wang H, Luo Z, Liu X, He L, Qi J, Fan L, Tang L, Chen Z, Li J, Cheng J, & Wang S (2022). Structure-based discovery of nonhallucinogenic psychedelic analogs. Science 375 6579:403-411. PubMed Id: 35084960. doi:10.1126/science.abl8615.
*5-HT_2A serotonin receptor complexed with miniG_q and agonist (R)-69: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.45 Å** cryo-EM structure	7RAN	Data File Jmol Viewer 7RAN	Kaplan et al. (2022). Kaplan AL, Confair DN, Kim K, Barros-Álvarez X, Rodriguiz RM, Yang Y, Kweon OS, Che T, McCorvy JD, Kamber DN, Phelan JP, Martins LC, Pogorelov VM, DiBerto JF, Slocum ST, Huang XP, Kumar JM, Robertson MJ, Panova O, Seven AB, Wetsel AQ, Wetsel WC, Irwin JJ, Skiniotis G, Shoichet BK, Roth BL, & Ellman JA (2022). Bespoke library docking for 5-HT2A receptor agonists with antidepressant activity. Nature 610 7932:582-591. PubMed Id: 36171289. doi:10.1038/s41586-022-05258-z.
*5-HT_2A serotonin receptor - G_i complex: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.10 Å** cryo-EM structure	7X5H	Data File Jmol Viewer 7X5H	Tan et al. (2022). Tan Y, Xu P, Huang S, Yang G, Zhou F, He X, Ma H, Xu HE, & Jiang Y (2022). Structural insights into the ligand binding and Gi coupling of serotonin receptor 5-HT5A. Cell Discov 8 1:50. PubMed Id: 35610220. doi:10.1038/s41421-022-00412-3.
*5-HT_2B serotonin receptor with bound ergotamine: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.70 Å** Engineered Protein: apocytochrome b₅₆₂ RIL (BRIL) replaces cytoplasmic loop 3 (Y249-V313).	4IB4	Data File Jmol Viewer 4IB4	Wacker et al. (2013). Wacker D, Wang C, Katritch V, Han GW, Huang XP, Vardy E, McCorvy JD, Jiang Y, Chu M, Siu FY, Liu W, Xu HE, Cherezov V, Roth BL, & Stevens RC (2013). Structural features for functional selectivity at serotonin receptors. Science 340 :615-619. PubMed Id: 23519215. doi:10.1126/science.1232808.
*5-HT_2B serotonin receptor: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.80 Å** Structure determined by serial femtosecond crystallography. Engineered Protein: apocytochrome b₅₆₂ RIL (BRIL) replaces cytoplasmic loop 3 (Y249-V313).	4NC3	Data File Jmol Viewer 4NC3	Liu et al. (2013). Liu W, Wacker D, Gati C, Han GW, James D et al. (2013). Serial femtosecond crystallography of G protein-coupled receptors. Science 342 :1521-1524. PubMed Id: 24357322. doi:10.1126/science.1244142.
*5-HT_2B serotonin receptor with bound LSD: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.9 Å** Engineered Protein: apocytochrome b₅₆₂ RIL (BRIL) replaces cytoplasmic loop 3 (Y249-V312)	5TVN	Data File Jmol Viewer 5TVN	Wacker et al. (2017). Wacker D, Wang S, McCorvy JD, Betz RM, Venkatakrishnan AJ, Levit A, Lansu K, Schools ZL, Che T, Nichols DE, Shoichet BK, Dror RO, & Roth BL (2017). Crystal Structure of an LSD-Bound Human Serotonin Receptor. Cell 168 :377-389. PubMed Id: 28129538. doi:10.1016/j.cell.2016.12.033.
*5-HT_2B serotonin receptor with bound methylergonovine: Homo Sapiens* B Bacteria (expressed in Spodoptera frugiperda), 2.92 Å** engineered protein: apocytochrome b562 RIL (BRIL) replaces cytoplasmic loop 3 (Y249-V313) Ala225Gly^5,46 mutant with bound methylsergide, 3.10 Å: 6DRZ with bound lisuride, 3.1 Å: 6DRX with bound LY266097, 3.19 Å: 6DS0	6DRY	Data File Jmol Viewer 6DRY 6DRZ 6DRX 6DS0	McCorvy et al. (2018). McCorvy JD, Wacker D, Wang S, Agegnehu B, Liu J, Lansu K, Tribo AR, Olsen RHJ, Che T, Jin J, & Roth BL (2018). Structural determinants of 5-HT_2B receptor activation and biased agonism. Nat Struct Mol Biol 25 9:787-796. PubMed Id: 30127358. doi:10.1038/s41594-018-0116-7.
*5-HT_2B serotonin receptor - β arrestin-1 complex with bound LSD: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.30 Å** cryo-EM structure mini G_q complex with bound LSD, 2.90 Å: 7SRR with bound LSD, FAB was used as a fiducial marker for cryo-EM, 2.70 Å: 7SRQ	7SRS	Data File Jmol Viewer 7SRS 7SRR 7SRQ	Cao et al. (2022). Cao C, Barros-Álvarez X, Zhang S, Kim K, Dämgen MA, Panova O, Suomivuori CM, Fay JF, Zhong X, Krumm BE, Gumpper RH, Seven AB, Robertson MJ, Krogan NJ, Hüttenhain R, Nichols DE, Dror RO, Skiniotis G, & Roth BL (2022). Signaling snapshots of a serotonin receptor activated by the prototypical psychedelic LSD. Neuron 110 19:3154-3167.e7. PubMed Id: 36087581. doi:10.1016/j.neuron.2022.08.006.
*5-HT_2C serotonin receptor with bound ergotamine: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.00 Å** with bound ritanserin, 2.70 Å: 6BQH	6BQG	Data File Jmol Viewer 6BQG 6BQH	Peng et al. (2018). Peng Y, McCorvy JD, Harpsøe K, Lansu K, Yuan S, Popov P, Qu L, Pu M, Che T, Nikolajsen LF, Huang XP, Wu Y, Shen L, Bjørn-Yoshimoto WE, Ding K, Wacker D, Han GW, Cheng J, Katritch V, Jensen AA, Hanson MA, Zhao S, Gloriam DE, Roth BL, Stevens RC, & Liu ZJ (2018). 5-HT2C Receptor Structures Reveal the Structural Basis of GPCR Polypharmacology. Cell 172 4:719-730.e14. PubMed Id: 29398112. doi:10.1016/j.cell.2018.01.001.
*5-HT_2C serotonin receptor (INI isoform) - G_αq complex, with bound lorcaserin: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.84 Å** cryo-EM structure INI isoform, with bound psilocin, 3.60 Å: 8DPG VGV isoform, with bound lorcaserin, 3.20 Å: 8DPH VSV isoform, with bound lorcaserin, 3.40 Å: 8DPI	8DPF	Data File Jmol Viewer 8DPF 8DPH 8DPG 8DPI	Gumpper et al. (2022). Gumpper RH, Fay JF, & Roth BL (2022). Molecular insights into the regulation of constitutive activity by RNA editing of 5HT2C serotonin receptors. Cell Rep 40 7:111211. PubMed Id: 35977511. doi:10.1016/j.celrep.2022.111211.
*5-HT₄ serotonin receptor G_s-Nb35 complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.10 Å** cryo-EM structure receptor G_s complex, 3.20 Å: 7XT9 G_i-scFv16 complex, 3.20 Å: 7XTA	7XT8	Data File Jmol Viewer 7XT8 7XTA 7XT9	Huang et al. (2022). Huang S, Xu P, Shen DD, Simon IA, Mao C, Tan Y, Zhang H, Harpsøe K, Li H, Zhang Y, You C, Yu X, Jiang Y, Zhang Y, Gloriam DE, & Xu HE (2022). GPCRs steer G_i and G_s selectivity via TM5-TM6 switches as revealed by structures of serotonin receptors. Mol Cell 82 14:2681-2695.e6. PubMed Id: 35714614. doi:10.1016/j.molcel.2022.05.031.
*5-HT_5A serotonin receptor in complex with AS2674723: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.80 Å** in complex with G_o and 5-CT, cryo-EM structure, 2.73 Å: 7UM5 in complex with G_o and lisuride, cryo-EM structure, 2.79 Å: 7UM6 in complex with G_o and methylergometrine, cryo-EM structure, 2.75 Å: 7UM7	7UM4	Data File Jmol Viewer 7UM4 7UM5 7UM7 7UM6	Zhang et al. (2022). Zhang S, Chen H, Zhang C, Yang Y, Popov P, Liu J, Krumm BE, Cao C, Kim K, Xiong Y, Katritch V, Shoichet BK, Jin J, Fay JF, & Roth BL (2022). Inactive and active state structures template selective tools for the human 5-HT5A receptor. Nat Struct Mol Biol 29 7:677-687. PubMed Id: 35835867. doi:10.1038/s41594-022-00796-6.
*5-HT₆ serotonin receptor G_s-Nb35 complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.30 Å** cryo-EM structure	7XTB	Data File Jmol Viewer 7XTB	Huang et al. (2022). Huang S, Xu P, Shen DD, Simon IA, Mao C, Tan Y, Zhang H, Harpsøe K, Li H, Zhang Y, You C, Yu X, Jiang Y, Zhang Y, Gloriam DE, & Xu HE (2022). GPCRs steer G_i and G_s selectivity via TM5-TM6 switches as revealed by structures of serotonin receptors. Mol Cell 82 14:2681-2695.e6. PubMed Id: 35714614. doi:10.1016/j.molcel.2022.05.031.
*5-HT₆ serotonin receptor G_s-scFv16 complex: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.00 Å** cryo-EM structure	7YS6	Data File Jmol Viewer 7YS6	He et al. (2023). He L, Zhao Q, Qi J, Wang Y, Han W, Chen Z, Cong Y, & Wang S (2023). Structural insights into constitutive activity of 5-HT6 receptor. Proc Natl Acad Sci U S A 120 14:e2209917120. PubMed Id: 36989299. doi:10.1073/pnas.2209917120.
*5-HT₇ serotonin receptor G_s-Nb35 complex:: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** cryo-EM structure	7XTC	Data File Jmol Viewer 7XTC	Huang et al. (2022). Huang S, Xu P, Shen DD, Simon IA, Mao C, Tan Y, Zhang H, Harpsøe K, Li H, Zhang Y, You C, Yu X, Jiang Y, Zhang Y, Gloriam DE, & Xu HE (2022). GPCRs steer G_i and G_s selectivity via TM5-TM6 switches as revealed by structures of serotonin receptors. Mol Cell 82 14:2681-2695.e6. PubMed Id: 35714614. doi:10.1016/j.molcel.2022.05.031.
*MT₁ melatonin receptor with bound ramelteon: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.8 Å** XFEL structure with bound 2-phenylmelatonin, 2.9 Å: 6ME3 with bound 2-iodomelatonin, 3.2 Å: 6ME4 with bound agomelatine, 3.2 Å: 6ME5	6ME2	Data File Jmol Viewer 6ME2 6ME3 6ME5 6ME4	Stauch et al. (2019). Stauch B, Johansson LC, McCorvy JD, Patel N, Han GW, Huang XP, Gati C, Batyuk A, Slocum ST, Ishchenko A, Brehm W, White TA, Michaelian N, Madsen C, Zhu L, Grant TD, Grandner JM, Shiriaeva A, Olsen RHJ, Tribo AR, Yous S, Stevens RC, Weierstall U, Katritch V, Roth BL, Liu W, & Cherezov V (2019). Structural basis of ligand recognition at the human MT1 melatonin receptor. Nature 569 7755:284-288. PubMed Id: 31019306. doi:10.1038/s41586-019-1141-3. see DOI 10.1038/s41586-019-1209-0 for corrections
*MT₁ melatonin receptor with bound 2-phenylmelatonin: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.3 Å** XFEL structure using transient ligand exchange starting with agomelatine. See also 6PRZ.	6PS8	Data File Jmol Viewer 6PS8	Ishchenko et al. (2019). Ishchenko A, Stauch B, Han GW, Batyuk A, Shiriaeva A, Li C, Zatsepin N, Weierstall U, Liu W, Nango E, Nakane T, Tanaka R, Tono K, Joti Y, Iwata S, Moraes I, Gati C, & Cherezov V (2019). Toward G protein-coupled receptor structure-based drug design using X-ray lasers. IUCrJ 6 :1106-1119. PubMed Id: 31709066. doi:10.1107/S2052252519013137.
*MT₁-G_i melatonin receptor complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.30 Å** cryo-EM structure	7DB6	Data File Jmol Viewer 7DB6	Okamoto et al. (2021). Okamoto HH, Miyauchi H, Inoue A, Raimondi F, Tsujimoto H, Kusakizako T, Shihoya W, Yamashita K, Suno R, Nomura N, Kobayashi T, Iwata S, Nishizawa T, & Nureki O (2021). Cryo-EM structure of the human MT₁-G_i signaling complex. Nat Struct Mol Biol 28 8:694-701. PubMed Id: 34354246. doi:10.1038/s41594-021-00634-1.
*MT₁ melatonin receptor-G_i complex with bound 2-iodomelatonin: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.10 Å** cryo-EM structure with bound remalteon, 3.30 Å 7VGZ	7VGY	Data File Jmol Viewer 7VGY 7VGZ	Wang et al. (2022). Wang Q, Lu Q, Guo Q, Teng M, Gong Q, Li X, Du Y, Liu Z, & Tao Y (2022). Structural basis of the ligand binding and signaling mechanism of melatonin receptors. Nat Commun 13 1:454. PubMed Id: 35075127. doi:10.1038/s41467-022-28111-3.
*MT₂ melatonin receptor with bound 2-phenylmelatonin: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.8 Å** XFEL structures H208A mutant with bound 2-phenylmelatonin, 3.2 Å: 6ME7 N86D mutant with bound 2-phenylmelatonin, 3.1 Å: 6ME8 with bound ramelteon, 3.3 Å: 6ME9	6ME6	Data File Jmol Viewer 6ME6 6ME7 6ME8 6ME9	Johansson et al. (2019). Johansson LC, Stauch B, McCorvy JD, Han GW, Patel N, Huang XP, Batyuk A, Gati C, Slocum ST, Li C, Grandner JM, Hao S, Olsen RHJ, Tribo AR, Zaare S, Zhu L, Zatsepin NA, Weierstall U, Yous S, Stevens RC, Liu W, Roth BL, Katritch V, & Cherezov V (2019). XFEL structures of the human MT₂ melatonin receptor reveal the basis of subtype selectivity. Nature 569 7755:289-292. PubMed Id: 31019305. doi:10.1038/s41586-019-1144-0.
*MT₂ melatonin receptor-G_icomplex with bound remalteon: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.46 Å** cryo-EM structure	7VH0	Data File Jmol Viewer 7VH0	Wang et al. (2022). Wang Q, Lu Q, Guo Q, Teng M, Gong Q, Li X, Du Y, Liu Z, & Tao Y (2022). Structural basis of the ligand binding and signaling mechanism of melatonin receptors. Nat Commun 13 1:454. PubMed Id: 35075127. doi:10.1038/s41467-022-28111-3.
*P2Y₁₂ receptor in complex with an antithrombotic drug: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.62 Å** Engineered Protein: apocytochrome b₅₆₂ RIL (BRIL) replaces cytoplasmic loop 3	4NTJ	Data File Jmol Viewer 4NTJ	Zhang et al. (2014). Zhang K, Zhang J, Gao ZG, Zhang D, Zhu L, Han GW, Moss SM, Paoletta S, Kiselev E, Lu W, Fenalti G, Zhang W, Müller CE, Yang H, Jiang H, Cherezov V, Katritch V, Jacobson KA, Stevens RC, Wu B, & Zhao Q (2014). Structure of the human P2Y12 receptor in complex with an antithrombotic drug. Nature 509 :115-118. PubMed Id: 24670650. doi:10.1038/nature13083.
*P2Y₁₂ receptor with bound agonist 2MeSADP: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.50 Å** Engineered Protein: apocytochrome b₅₆₂ RIL (BRIL) replaces cytoplasmic loop 3 with bound 2MeSATP, 3.10 Å: 4PY0	4PXZ	Data File Jmol Viewer 4PXZ 4PY0	Zhang et al. (2014). Zhang J, Zhang K, Gao ZG, Paoletta S, Zhang D, Han GW, Li T, Ma L, Zhang W, Müller CE, Yang H, Jiang H, Cherezov V, Katritch V, Jacobson KA, Stevens RC, Wu B, & Zhao Q (2014). Agonist-bound structure of the human P2Y₁₂ receptor. Nature 509 :119-122. PubMed Id: 24784220. doi:10.1038/nature13288.
*P2Y₁₂ receptor with bound inverse agonist selatogrel: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.78 Å**	7PP1	Data File Jmol Viewer 7PP1	Pons et al. (2022). Pons V, Garcia C, Tidten-Luksch N, Mac Sweeney A, Caroff E, Galés C, & Riederer MA (2022). Inverse agonist efficacy of selatogrel blunts constitutive P2Y12 receptor signaling by inducing the inactive receptor conformation. Biochem Pharmacol 206 :115291. PubMed Id: 36306820. doi:10.1016/j.bcp.2022.115291.
*P2Y₁ receptor in complex with BPTU: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.20 Å** Engineered protein. Rubredoxin inserted into the ICL3 domain between residues 247K and 253P, replacing residues 248N to 252S. in complex with MRS2500, 2.70 Å: 4XNW	4XNV	Data File Jmol Viewer 4XNV 4XNW	Zhang et al. (2015). Zhang D, Gao ZG, Zhang K, Kiselev E, Crane S, Wang J, Paoletta S, Yi C, Ma L, Zhang W, Han GW, Liu H, Cherezov V, Katritch V, Jiang H, Stevens RC, Jacobson KA, Zhao Q, & Wu B (2015). Two disparate ligand-binding sites in the human P2Y₁ receptor. Nature 520 7547:317-321. PubMed Id: 25822790. doi:10.1038/nature14287.
*Leukotriene B₄ receptor BLT1 with bound antagonist BIIL260, inactive state: Cavia porcellus* E Eukaryota (expressed in HEK293 cells), 3.7 Å**	5X33	Data File Jmol Viewer 5X33	Hori et al. (2018). Hori T, Okuno T, Hirata K, Yamashita K, Kawano Y, Yamamoto M, Hato M, Nakamura M, Shimizu T, Yokomizo T, Miyano M, & Yokoyama S (2018). Na⁺-mimicking ligands stabilize the inactive state of leukotriene B4receptor BLT1. Nat Chem Biol 14 :262-269. PubMed Id: 29309055. doi:10.1038/nchembio.2547.
*Leukotriene B₄ receptor BLT1 in Complex with Selective Antagonist MK-D-046: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.88 Å**	7K15	Data File Jmol Viewer 7K15	Michaelian et al. (2021). Michaelian N, Sadybekov A, Besserer-Offroy É, Han GW, Krishnamurthy H, Zamlynny BA, Fradera X, Siliphaivanh P, Presland J, Spencer KB, Soisson SM, Popov P, Sarret P, Katritch V, & Cherezov V (2021). Structural insights on ligand recognition at the human leukotriene B4 receptor 1. Nat Commun 12 1:2971. PubMed Id: 34016973. doi:10.1038/s41467-021-23149-1.
*Leukotriene B₄ receptor BLT1-G_i complex: Homo sapiens* E Eukaryota (expressed in SF9 cells), 2.90 Å** cryo-EM structure	7VKT	Data File Jmol Viewer 7VKT	Wang et al. (2022). Wang N, He X, Zhao J, Jiang H, Cheng X, Xia Y, Eric Xu H, & He Y (2022). Structural basis of leukotriene B4 receptor 1 activation. Nat Commun 13 1:1156. PubMed Id: 35241677. doi:10.1038/s41467-022-28820-9.
*cysteinyl leukotriene receptor 1 (CysLT₁) in complex with pranlukast: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.7 Å** in complex with zafirlukast using XFEL, 2.53 Å: 6RZ5	6RZ4	Data File Jmol Viewer 6RZ4 6RZ5	Luginina et al. (2019). Luginina A, Gusach A, Marin E, Mishin A, Brouillette R, Popov P, Shiriaeva A, Besserer-Offroy É, Longpré JM, Lyapina E, Ishchenko A, Patel N, Polovinkin V, Safronova N, Bogorodskiy A, Edelweiss E, Hu H, Weierstall U, Liu W, Batyuk A, Gordeliy V, Han GW, Sarret P, Katritch V, Borshchevskiy V, & Cherezov V (2019). Structure-based mechanism of cysteinyl leukotriene receptor inhibition by antiasthmatic drugs. Sci Adv 5 10. PubMed Id: 31633023. doi:10.1126/sciadv.aax2518.
*cysteinyl leukotriene receptor 2 (CysLT₂) in complex with ONO-2570366 (C222₁) space group: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.43 Å** Engineered protein: b₅₆₂RIL (mutant M7W, H102I, R106L) inserted in ICL3 between E232 and V240 F222 space group, 2.43 Å: 6R7Z in complex with ONO-2080365, 2.7 Å: 6RZ8 in complex with ONO-2770372, 2.73 Å: 6RZ9	6RZ6	Data File Jmol Viewer 6RZ6 6RZ9 6RZ8	Gusach et al. (2019). Gusach A, Luginina A, Marin E, Brouillette RL, Besserer-Offroy É, Longpré JM, Ishchenko A, Popov P, Patel N, Fujimoto T, Maruyama T, Stauch B, Ergasheva M, Romanovskaia D, Stepko A, Kovalev K, Shevtsov M, Gordeliy V, Han GW, Katritch V, Borshchevskiy V, Sarret P, Mishin A, & Cherezov V (2019). Structural basis of ligand selectivity and disease mutations in cysteinyl leukotriene receptors. Nat Commun 10 1:5573. PubMed Id: 31811124. doi:10.1038/s41467-019-13348-2.
*oxytocin receptor: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** Engineered protein. Intracellular loop 3 replaced with Pyrococcus abysii glycogen synthase (PGS).	6TPK	Data File Jmol Viewer 6TPK	Waltenspühl et al. (2020). Waltenspühl Y, Schöppe J, Ehrenmann J, Kummer L, & Plückthun A (2020). Crystal structure of the human oxytocin receptor. Sci Adv 6 29. PubMed Id: 32832646. doi:10.1126/sciadv.abb5419.
*GPR40 free fatty-acid receptor 1 (FFAR1) bound to TAK-875: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.33 Å** Engineered protein: Four point mutations to improve thermostability and T4 lysozyme inserted between TM helices V and VI (intracellular loop 3).	4PHU	Data File Jmol Viewer 4PHU	Srivastava et al. (2014). Srivastava A, Yano J, Hirozane Y, Kefala G, Gruswitz F, Snell G, Lane W, Ivetac A, Aertgeerts K, Nguyen J, Jennings A, & Okada K (2014). High-resolution structure of the human GPR40 receptor bound to allosteric agonist TAK-875. Nature 513 7516:124-127. PubMed Id: 25043059. doi:10.1038/nature13494.
*GPR40 free fatty-acid receptor 1 (FFAR1) - G_q complex with bound DHA: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.39 Å** cryo-EM structure	8T3V	Data File Jmol Viewer 8T3V	Zhang et al. (2024). Zhang X, Guseinov AA, Jenkins L, Li K, Tikhonova IG, Milligan G, & Zhang C (2024). Structural basis for the ligand recognition and signaling of free fatty acid receptors. Sci Adv 10 2:eadj2384. PubMed Id: 38198545. doi:10.1126/sciadv.adj2384.
*GPR43 free fatty-acid receptor 2 (FFAR2) - G_q complex with bound butyrate: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.07 Å** cryo-EM structure	8T3S	Data File Jmol Viewer 8T3S	Zhang et al. (2024). Zhang X, Guseinov AA, Jenkins L, Li K, Tikhonova IG, Milligan G, & Zhang C (2024). Structural basis for the ligand recognition and signaling of free fatty acid receptors. Sci Adv 10 2:eadj2384. PubMed Id: 38198545. doi:10.1126/sciadv.adj2384.
*GPR120 free fatty-acid receptor 4 (FFAR4) - G_iq complex, with bound TUG891: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.64 Å** cryo-EM structure G_i complex, with bound eicosapentaenoic acid, 3.00 Å: 8ID9 G_i complex, with bound 9-hydroxystearic acid, 3.10 Å: 8ID3 G_i complex, with bound linoleic acid, 3.10 Å: 8ID4 G_i complex, with bound TUG891, 3.00 Å: 8ID8 G_i complex, with bound oleic acid, 2.80 Å: 8ID6	8G59	Data File Jmol Viewer 8G59 8ID9 8ID4 8ID6 8ID3 8ID8	Mao et al. (2023). Mao C, Xiao P, Tao XN, Qin J, He QT, Zhang C, Guo SC, Du YQ, Chen LN, Shen DD, Yang ZS, Zhang HQ, Huang SM, He YH, Cheng J, Zhong YN, Shang P, Chen J, Zhang DL, Wang QL, Liu MX, Li GY, Guo Y, Xu HE, Wang C, Zhang C, Feng S, Yu X, Zhang Y, & Sun JP (2023). Unsaturated bond recognition leads to biased signal in a fatty acid receptor. Science 380 6640:eadd6220. PubMed Id: 36862765. doi:10.1126/science.add6220.
*GPR120 free fatty-acid receptor 4 (FFAR4) - G_q complex with bound TUG891: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.06 Å** cryo-EM structure with bound DHA, 3.14 Å: 8T3Q	8T3O	Data File Jmol Viewer 8T3O 8T3Q	Zhang et al. (2024). Zhang X, Guseinov AA, Jenkins L, Li K, Tikhonova IG, Milligan G, & Zhang C (2024). Structural basis for the ligand recognition and signaling of free fatty acid receptors. Sci Adv 10 2:eadj2384. PubMed Id: 38198545. doi:10.1126/sciadv.adj2384.
*LPA₁ Lysophosphatidic Acid Receptor 1 in complex with ONO-9780307: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.00 Å** Engineered Protein: apocytochrome b₅₆₂ RIL (BRIL) replaces cytoplasmic loop 3 in complex with ONO-9910539, 2.90 Å: 4Z35 in complex with ONO-3080573, 2.90 Å: 4Z36	4Z34	Data File Jmol Viewer 4Z34 4Z36 4Z35	Chrencik et al. (2015). Chrencik JE, Roth CB, Terakado M, Kurata H, Omi R, Kihara Y, Warshaviak D, Nakade S, Asmar-Rovira G, Mileni M, Mizuno H, Griffith MT, Rodgers C, Han GW, Velasquez J, Chun J, Stevens RC, & Hanson MA (2015). Crystal Structure of Antagonist Bound Human Lysophosphatidic Acid Receptor 1. Cell 161 :1633-1643. PubMed Id: 26091040. doi:10.1016/j.cell.2015.06.002.
*LPA₁ Lysophosphatidic Acid Receptor 1 -G_i complex bound to LPA: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.83 Å** cryo-EM structure state a, 3.08 Å 7TD1 state a', 3.11 Å 7TD2	7TD0	Data File Jmol Viewer 7TD0 7TD1 7TD2	Liu et al. (2022). Liu S, Paknejad N, Zhu L, Kihara Y, Ray M, Chun J, Liu W, Hite RK, & Huang XY (2022). Differential activation mechanisms of lipid GPCRs by lysophosphatidic acid and sphingosine 1-phosphate. Nat Commun 13 1:731. PubMed Id: 35136060. doi:10.1038/s41467-022-28417-2.
*LPA₁ Lysophosphatidic Acid Receptor 1 -G_i complex with bound ONO-0740556: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.50 Å** cryo-EM structure focused on receptor, 3.70 Å: 7YU4 state 1, 3.70 Å: 7YU5 state 2, 3.90 Å: 7YU6 state 3, 4.50 Å: 7YU7 state 4, 5.60 Å: 7YU8	7YU3	Data File Jmol Viewer 7YU3 7YU8 7YU7 7YU6 7YU4 7YU5	Akasaka et al. (2022). Akasaka H, Tanaka T, Sano FK, Matsuzaki Y, Shihoya W, & Nureki O (2022). Structure of the active Gi-coupled human lysophosphatidic acid receptor 1 complexed with a potent agonist. Nat Commun 13 1:5417. PubMed Id: 36109516. doi:10.1038/s41467-022-33121-2.
*LPA₆ Lysophosphatidic Acid Receptor: Danio rerio* E Eukaryota (expressed in S. frugiperda), 3.2 Å** Engineered protein: T4 lysozyme within extracellular loop 3.	5XSZ	Data File Jmol Viewer 5XSZ	Taniguchi et al. (2017). Taniguchi R, Inoue A, Sayama M, Uwamizu A, Yamashita K, Hirata K, Yoshida M, Tanaka Y, Kato HE, Nakada-Nakura Y, Otani Y, Nishizawa T, Doi T, Ohwada T, Ishitani R, Aoki J, & Nureki O (2017). Structural insights into ligand recognition by the lysophosphatidic acid receptor LPA6. Nature 548 :356-360. PubMed Id: 28792932. doi:10.1038/nature23448.
*Angiotensin II type 1 receptor: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.9 Å** Structure determined using serial femtosecond crystallography (XFEL) Engineered protein: apocytochrome b₅₆₂ RIL (BRIL) fused at amino terminal.	4YAY	Data File Jmol Viewer 4YAY	Zhang et al. (2015). Zhang H, Unal H, Gati C, Han GW, Liu W, Zatsepin NA, James D, Wang D, Nelson G, Weierstall U, Sawaya MR, Xu Q, Messerschmidt M, Williams GJ, Boutet S, Yefanov OM, White TA, Wang C, Ishchenko A, Tirupula KC, Desnoyer R, Coe J, Conrad CE, Fromme P, Stevens RC, Katritch V, Karnik SS, & Cherezov V (2015). Structure of the Angiotensin receptor revealed by serial femtosecond crystallography. Cell 161 :833-844. PubMed Id: 25913193. doi:10.1016/j.cell.2015.04.011.
*Angiotensin II type 1 receptor with bound olmesartan: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.8 Å** Engineered protein: apocytochrome b₅₆₂ RIL (BRIL) fused at amino terminal.	4ZUD	Data File Jmol Viewer 4ZUD	Zhang et al. (2015). Zhang H, Unal H, Desnoyer R, Han GW, Patel N, Katritch V, Karnik SS, Cherezov V, & Stevens RC (2015). Structural Basis for Ligand Recognition and Functional Selectivity at Angiotensin Receptor. J Biol Chem 290 :29127-29139. PubMed Id: 26420482. doi:10.1074/jbc.M115.689000.
*Angiotensin II type 1 receptor in complex with angiotensin II peptide analog: Homo sapiens* E Eukaryota (expressed in Expi293F cells), 2.90 Å** Engineered protein. b562RIL inserted into 3rd intracellular loop.	6DO1	Data File Jmol Viewer 6DO1	Wingler et al. (2019). Wingler LM, McMahon C, Staus DP, Lefkowitz RJ, & Kruse AC (2019). Distinctive Activation Mechanism for Angiotensin Receptor Revealed by a Synthetic Nanobody. Cell 176 3:479-490.e12. PubMed Id: 30639100. doi:10.1016/j.cell.2018.12.006.
*Angiotensin II type 1 receptor with bound angiotensin II: Homo sapiens* E Eukaryota (expressed in Expi293F cells), 2.9 Å** Thermostabilized. Apocytochrome b562RIL (BRIL) inserted in the third intracellular loop between AT1R residues 226 and 227. bound to TRV023, 2.79 Å: 6OS1 bound to TRV026, 2.7 Å: 6OS2	6OS0	Data File Jmol Viewer 6OS0 6OS2 6OS1	Wingler et al. (2020). Wingler LM, Skiba MA, McMahon C, Staus DP, Kleinhenz ALW, Suomivuori CM, Latorraca NR, Dror RO, Lefkowitz RJ, & Kruse AC (2020). Angiotensin and biased analogs induce structurally distinct active conformations within a GPCR. Science 367 6480:888-892. PubMed Id: 32079768. doi:10.1126/science.aay9813.
*Angiotensin II type 2 receptor in complex with compound 1 (monoclinic xtals): Homo Sapiens* E Eukaryota (expressed in S. frugiperda), 2.8 Å** in complex with compound 1 (orthorhombic xtals), 2.8 Å: 5UNG in complex with compound 2, 2.9 Å: 5UNH Engineered protein. N-term residues 1-34 truncated; C-terminal residues 336-363 truncated. b₅₆₂RIL fused to N-term.	5UNF	Data File Jmol Viewer 5UNF 5UNG 5UNH	Zhang et al. (2017). Zhang H, Han GW, Batyuk A, Ishchenko A, White KL, Patel N, Sadybekov A, Zamlynny B, Rudd MT, Hollenstein K, Tolstikova A, White TA, Hunter MS, Weierstall U, Liu W, Babaoglu K, Moore EL, Katz RD, Shipman JM, Garcia-Calvo M, Sharma S, Sheth P, Soisson SM, Stevens RC, Katritch V, & Cherezov V (2017). Structural basis for selectivity and diversity in angiotensin II receptors. Nature 544 :327-332. PubMed Id: 28379944. doi:10.1038/nature22035.
*Angiotensin II type 2 receptor in complex with s-AngII: Homo sapiens* E Eukaryota, 3.2 Å** engineered protein, intracellular loop 3 contains thermostabilized apocytochrome b₅₆₂	5XJM	Data File Jmol Viewer 5XJM	Asada et al. (2018). Asada H, Horita S, Hirata K, Shiroishi M, Shiimura Y, Iwanari H, Hamakubo T, Shimamura T, Nomura N, Kusano-Arai O, Uemura T, Suno C, Kobayashi T, & Iwata S (2018). Crystal structure of the human angiotensin II type 2 receptor bound to an angiotensin II analog. Nat Struct Mol Biol 25 7:570-576. PubMed Id: 29967536. doi:10.1038/s41594-018-0079-8.
*Angiotensin II type 2 receptor with bound angiotensin II: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.20 Å** Engineered protein: N-terminal glycosylation sites truncated and replaced with apocytochrome b₅₆₂.	6JOD	Data File Jmol Viewer 6JOD	Asada et al. (2020). Asada H, Inoue A, Ngako Kadji FM, Hirata K, Shiimura Y, Im D, Shimamura T, Nomura N, Iwanari H, Hamakubo T, Kusano-Arai O, Hisano H, Uemura T, Suno C, Aoki J, & Iwata S (2020). The Crystal Structure of Angiotensin II Type 2 Receptor with Endogenous Peptide Hormone. Structure 28 4:418-425.e4. PubMed Id: 31899086. doi:10.1016/j.str.2019.12.003.
*prostaglandin D₂ receptor CRTH2 with bound fevipiprant: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.8 Å** Engineered protein: T4 lysozyme with 8 amino acid linker inserted in intracellular loop 3 with bound CAY10471, 2.74 Å: 6D27	6D26	Data File Jmol Viewer 6D26 6D27	Wang et al. (2018). Wang L, Yao D, Deepak RNVK, Liu H, Xiao Q, Fan H, Gong W, Wei Z, & Zhang C (2018). Structures of the Human PGD₂ Receptor CRTH2 Reveal Novel Mechanisms for Ligand Recognition. Mol Cell 72 1:48-59.e4. PubMed Id: 30220562. doi:10.1016/j.molcel.2018.08.009.
*prostaglandin D₂ receptor CRTH2 in complex with 15R-methyl-PGD₂: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.61 Å**	7M8W	Data File Jmol Viewer 7M8W	Liu et al. (2021). Liu H, Deepak RNVK, Shiriaeva A, Gati C, Batyuk A, Hu H, Weierstall U, Liu W, Wang L, Cherezov V, Fan H, & Zhang C (2021). Molecular basis for lipid recognition by the prostaglandin D₂ receptor CRTH2. Proc Natl Acad Sci U S A 118 32:e2102813118. PubMed Id: 34341104. doi:10.1073/pnas.2102813118.
*prostanoid receptor EP₂-G_s with bound PGE₂: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.80 Å** cryo-EM structure Taprenepag-bound complex, 2.80 Å: 7CX3 Evatanepag-bound complex, 2.90 Å: 7CX4	7CX2	Data File Jmol Viewer 7CX2 7CX4 7CX3	Qu et al. (2021). Qu C, Mao C, Xiao P, Shen Q, Zhong YN, Yang F, Shen DD, Tao X, Zhang H, Yan X, Zhao RJ, He J, Guan Y, Zhang C, Hou G, Zhang PJ, Hou G, Li Z, Yu X, Chai RJ, Guan YF, Sun JP, & Zhang Y (2021). Ligand recognition, unconventional activation, and G protein coupling of the prostaglandin E2 receptor EP2 subtype. Sci Adv 7 14:eabf1268. PubMed Id: 33811074. doi:10.1126/sciadv.abf1268.
*prostaglandin E₂ receptor 3 (EP₃) with bound misoprostol: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.5 Å** Engineered protein. Third intracellular loop replaced with T4-lysozyme, G286A mutation, and C-terminus truncated after L353	6M9T	Data File Jmol Viewer 6M9T	Audet et al. (2019). Audet M, White KL, Breton B, Zarzycka B, Han GW, Lu Y, Gati C, Batyuk A, Popov P, Velasquez J, Manahan D, Hu H, Weierstall U, Liu W, Shui W, Katritch V, Cherezov V, Hanson MA, & Stevens RC (2019). Crystal structure of misoprostol bound to the labor inducer prostaglandin E2 receptor. Nat Chem Biol 15 1:11-17. PubMed Id: 30510194. doi:10.1038/s41589-018-0160-y.
*prostanoid receptor EP₃ with bound PGE₂: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.9 Å** engineered protein. See article.	6AK3	Data File Jmol Viewer 6AK3	Morimoto et al. (2019). Morimoto K, Suno R, Hotta Y, Yamashita K, Hirata K, Yamamoto M, Narumiya S, Iwata S, & Kobayashi T (2019). Crystal structure of the endogenous agonist-bound prostanoid receptor EP3. Nat Chem Biol 15 1:8-10. PubMed Id: 30510192. doi:10.1038/s41589-018-0171-8.
*prostanoid receptor EP₃ - G_i complex with bound PGE₂: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.50 Å** cryo-EM structure	8GDC	Data File Jmol Viewer 8GDC	Huang et al. (2023). Huang SM, Xiong MY, Liu L, Mu J, Wang MW, Jia YL, Cai K, Tie L, Zhang C, Cao S, Wen X, Wang JL, Guo SC, Li Y, Qu CX, He QT, Cai BY, Xue C, Gan S, Xie Y, Cong X, Yang Z, Kong W, Li S, Li Z, Xiao P, Yang F, Yu X, Guan YF, Zhang X, Liu Z, Yang BX, Du Y, & Sun JP (2023). Single hormone or synthetic agonist induces Gs/Gi coupling selectivity of EP receptors via distinct binding modes and propagating paths. Proc Natl Acad Sci U S A 120 30:e2216329120. PubMed Id: 37478163. doi:10.1073/pnas.2216329120.
*prostaglandin EP₄ receptor in complex with agonist ONO-AE3-208: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.2 Å** engineered protein with bound ONO-AE3-208-Br derivative, 4.2 Å: 5YHL	5YWY	Data File Jmol Viewer 5YWY 5YHL	Toyoda et al. (2019). Toyoda Y, Morimoto K, Suno R, Horita S, Yamashita K, Hirata K, Sekiguchi Y, Yasuda S, Shiroishi M, Shimizu T, Urushibata Y, Kajiwara Y, Inazumi T, Hotta Y, Asada H, Nakane T, Shiimura Y, Nakagita T, Tsuge K, Yoshida S, Kuribara T, Hosoya T, Sugimoto Y, Nomura N, Sato M, Hirokawa T, Kinoshita M, Murata T, Takayama K, Yamamoto M, Narumiya S, Iwata S, & Kobayashi T (2019). Ligand binding to human prostaglandin E receptor EP₄ at the lipid-bilayer interface. Nat Chem Biol 15 1:18-26. PubMed Id: 30510193. doi:10.1038/s41589-018-0131-3.
*prostaglandin EP₄-heterotrimeric G_s receptor in complex with PGE₂: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.30 Å** cryo-EM structure	7D7M	Data File Jmol Viewer 7D7M	Nojima et al. (2021). Nojima S, Fujita Y, Kimura KT, Nomura N, Suno R, Morimoto K, Yamamoto M, Noda T, Iwata S, Shigematsu H, & Kobayashi T (2021). Cryo-EM Structure of the Prostaglandin E Receptor EP4 Coupled to G Protein. Structure 29 3:252-260.e6. PubMed Id: 33264604. doi:10.1016/j.str.2020.11.007.
*prostaglandin EP₄ - G_s complex with bound PGE₂: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.10 Å** cryo-EM structure with bound L902688, 3.30 Å: 8GDA with bound rivenprost, 3.20 Å: 8GD9 G_i complex with bound L902688, 3.50 Å: 8GCM G_i complex with bound PGE₂, 3.10 Å: 8GCP	8GDB	Data File Jmol Viewer 8GDB 8GDA 8GD9 8GCP 8GCM	Huang et al. (2023). Huang SM, Xiong MY, Liu L, Mu J, Wang MW, Jia YL, Cai K, Tie L, Zhang C, Cao S, Wen X, Wang JL, Guo SC, Li Y, Qu CX, He QT, Cai BY, Xue C, Gan S, Xie Y, Cong X, Yang Z, Kong W, Li S, Li Z, Xiao P, Yang F, Yu X, Guan YF, Zhang X, Liu Z, Yang BX, Du Y, & Sun JP (2023). Single hormone or synthetic agonist induces Gs/Gi coupling selectivity of EP receptors via distinct binding modes and propagating paths. Proc Natl Acad Sci U S A 120 30:e2216329120. PubMed Id: 37478163. doi:10.1073/pnas.2216329120.
*prostaglandin F2α receptor (FP) - G_q complex with bound PGF2α: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.67 Å** cryo-EM structure with bound latanoprost, 2.78 Å: 8IUL with bound tafluprost acid, 3.14 Å: 8IUM	8IUK	Data File Jmol Viewer 8IUK 8IUM 8IUL	Wu et al. (2023). Wu C, Xu Y, He Q, Li D, Duan J, Li C, You C, Chen H, Fan W, Jiang Y, & Eric Xu H (2023). Ligand-induced activation and G protein coupling of prostaglandin F2α receptor. Nat Commun 14 1:2668. PubMed Id: 37160891. doi:10.1038/s41467-023-38411-x.
*thromboxane A₂ receptor (TP) with bound ramatroban: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.50 Å** engineered protein: b₅₆₂RIL and rubredoxin were fused into the N-terminus and intracellular loop 3, respectively. with bound daltroban, 3.00 Å: 6IIV	6IIU	Data File Jmol Viewer 6IIU 6IIV	Fan et al. (2019). Fan H, Chen S, Yuan X, Han S, Zhang H, Xia W, Xu Y, Zhao Q, & Wu B (2019). Structural basis for ligand recognition of the human thromboxane A₂ receptor. Nat Chem Biol 15 1:27-33. PubMed Id: 30510189. doi:10.1038/s41589-018-0170-9.
*NK1 tachykinin (neurokinin) receptor with bound inhibitor L760735: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.4 Å** engineered protein. Residues 228-237 in intracellular loop 3 were replaced by Pyrococcus abysii glycogen synthase domain. Residues 347-407 at the C-terminus were removed.	6E59	Data File Jmol Viewer 6E59	Yin et al. (2018). Yin J, Chapman K, Clark LD, Shao Z, Borek D, Xu Q, Wang J, & Rosenbaum DM (2018). Crystal structure of the human NK1 tachykinin receptor. Proc Natl Acad Sci USA 115 52:13264-13269. PubMed Id: 30538204. doi:10.1073/pnas.1812717115.
*NK1 tachykinin (neurokinin) receptor with bound CP-99,994: Homo sapiens* E Eukaryota (expressed in sf9 cells), 3.27 Å** with bound aprepitant, 2.40 Å: 6HLO with bound netupitant, 2.20 Å: 6HLP	6HLL	Data File Jmol Viewer 6HLL 6HLO 6HLP	Schöppe et al. (2019). Schöppe J, Ehrenmann J, Klenk C, Rucktooa P, Schütz M, Doré AS, & Pückthun A (2019). Crystal structures of the human neurokinin 1 receptor in complex with clinically used antagonists. Nat Commun 10 1. PubMed Id: 30604743. doi:10.1038/s41467-018-07939-8.
*NK1 tachykinin (neurokinin) receptor in complex with miniG_s/q70: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure Substance P bound to neurokinin 1 receptor in complex with miniG_s399, 3.10 Å 7RMH SP6-11 biased agonist in complex with miniG_s/q70, 7RMI	7RMG	Data File Jmol Viewer 7RMG 7RMI 7RMH	Harris et al. (2022). Harris JA, Faust B, Gondin AB, Dämgen MA, Suomivuori CM, Veldhuis NA, Cheng Y, Dror RO, Thal DM, & Manglik A (2022). Selective G protein signaling driven by substance P-neurokinin receptor dynamics. Nat Chem Biol 18 1:109-115. PubMed Id: 34711980. doi:10.1038/s41589-021-00890-8.
*NK1 tachykinin (neurokinin) receptor - miniG_q complex with bound substance P (SP): Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.71 Å** cryo-EM structure - miniG_s complex with bound substance P (SP), 2.87 Å 7P02	7P00	Data File Jmol Viewer 7P00 7P02	Thom et al. (2021). Thom C, Ehrenmann J, Vacca S, Waltenspühl Y, Schöppe J, Medalia O, & Plückthun A (2021). Structures of neurokinin 1 receptor in complex with G_q and G_s proteins reveal substance P binding mode and unique activation features. Sci Adv 7 50:eabk2872. PubMed Id: 34878828. doi:10.1126/sciadv.abk2872.
*NK3 tachykinin (neurokinin) receptor - G_q complex with bound neurokinin B (NKB): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.80 Å** cryo-EM structure with bound senktide (SP analog), 3.00 Å: 8JBF with bound substance P (SP), 2.90 Å: 8JBH	8JBG	Data File Jmol Viewer 8JBG 8JBF 8JBH	Sun et al. (2023). Sun W, Yang F, Zhang H, Yuan Q, Ling S, Wang Y, Lv P, Li Z, Luo Y, Liu D, Yin W, Shi P, Xu HE, & Tian C (2023). Structural insights into neurokinin 3 receptor activation by endogenous and analogue peptide agonists. Cell Discov 9 1:66. PubMed Id: 37391393. doi:10.1038/s41421-023-00564-w.
*Platelet activating factor complex with bound antagonist SR 27417: Homo sapiens* E Eukaryota (expressed in sf9 cells), 2.81 Å** engineered protein. T4 lysozyme in 3rd intracellular loop with bound inverse agonist ABT-491, 2.9 Å: 5ZKQ	5ZKP	Data File Jmol Viewer 5ZKP 5ZKQ	Cao et al. (2018). Cao C, Tan Q, Xu C, He L, Yang L, Zhou Y, Zhou Y, Qiao A, Lu M, Yi C, Han GW, Wang X, Li X, Yang H, Rao Z, Jiang H, Zhao Y, Liu J, Stevens RC, Zhao Q, Zhang XC, & Wu B (2018). Structural basis for signal recognition and transduction by platelet-activating-factor receptor. Nat Struct Mol Biol 25 6:488-495. PubMed Id: 29808000. doi:10.1038/s41594-018-0068-y.
*succinate receptor SUCNR1 (GPR91): Rattus norvegicus* E Eukaryota (expressed in S. frugiperda), 2.12 Å** humanized form (K18E, K269N), 1.94 Å: 6RNK	6IBB	Data File Jmol Viewer 6IBB 6RNK	Haffke et al. (2019). Haffke M, Fehlmann D, Rummel G, Boivineau J, Duckely M, Gommermann N, Cotesta S, Sirockin F, Freuler F, Littlewood-Evans A, Kaupmann K, & Jaakola VP (2019). Structural basis of species-selective antagonist binding to the succinate receptor. Nature 574 7779:581-585. PubMed Id: 31645725. doi:10.1038/s41586-019-1663-8.
*succinate receptor SUCNR1 (GPR91). Humanized (K18E, K269N mutant) in complex with a Nb and antagonist: Rattus norvegicus* E Eukaryota (expressed in Spodoptera frugiperda), 2.27 Å**	6Z10	Data File Jmol Viewer 6Z10	Velcicky et al. (2020). Velcicky J, Wilcken R, Cotesta S, Janser P, Schlapbach A, Wagner T, Piechon P, Villard F, Bouhelal R, Piller F, Harlfinger S, Stringer R, Fehlmann D, Kaupmann K, Littlewood-Evans A, Haffke M, & Gommermann N (2020). Discovery and Optimization of Novel SUCNR1 Inhibitors: Design of Zwitterionic Derivatives with a Salt Bridge for the Improvement of Oral Exposure. J Med Chem 63 17:9856-9875. PubMed Id: 32856916. doi:10.1021/acs.jmedchem.0c01020.
*Melanocortin-1 Receptor (MC1R) - G_s complex with bound α-MSH: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.00 Å** cryo-EM structure with bound afamelanotide, 2.90 Å 7F4F with bound afamelanotide, 2.70 Å 7F4H with bound SHU9119, 3.10 Å 7F4I	7F4D	Data File Jmol Viewer 7F4D 7F4H 7F4I 7F4F	Ma et al. (2021). Ma S, Chen Y, Dai A, Yin W, Guo J, Yang D, Zhou F, Jiang Y, Wang MW, & Xu HE (2021). Structural mechanism of calcium-mediated hormone recognition and Gβ interaction by the human melanocortin-1 receptor. Cell Res 31 10:1061-1071. PubMed Id: 34453129. doi:10.1038/s41422-021-00557-y.
*Melanocortin-3 Receptor (MC3R) - G_s complex with bound γ-MSH: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.86 Å** cryo-EM structure	8IOC	Data File Jmol Viewer 8IOC	Feng et al. (2023). Feng W, Zhou Q, Chen X, Dai A, Cai X, Liu X, Zhao F, Chen Y, Ye C, Xu Y, Cong Z, Li H, Lin S, Yang D, & Wang MW (2023). Structural insights into ligand recognition and subtype selectivity of the human melanocortin-3 and melanocortin-5 receptors. Cell Discov 9 1:81. PubMed Id: 37524700. doi:10.1038/s41421-023-00586-4.
*Melanocortin-4 Receptor (MC4R) in complex with antagonist SHU9119: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.75 Å**	6W25	Data File Jmol Viewer 6W25	Yu et al. (2020). Yu J, Gimenez LE, Hernandez CC, Wu Y, Wein AH, Han GW, McClary K, Mittal SR, Burdsall K, Stauch B, Wu L, Stevens SN, Peisley A, Williams SY, Chen V, Millhauser GL, Zhao S, Cone RD, & Stevens RC (2020). Determination of the melanocortin-4 receptor structure identifies Ca2+ as a cofactor for ligand binding. Science 368 6489:428-433. PubMed Id: 32327598. doi:10.1126/science.aaz8995.
*Melanocortin-4 Receptor (MC4R)-G_s complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.97 Å** cryo-EM structure	7AUE	Data File Jmol Viewer 7AUE	Israeli et al. (2021). Israeli H, Degtjarik O, Fierro F, Chunilal V, Gill AK, Roth NJ, Botta J, Prabahar V, Peleg Y, Chan LF, Ben-Zvi D, McCormick PJ, Niv MY, & Shalev-Benami M (2021). Structure reveals the activation mechanism of the MC4 receptor to initiate satiation signaling. Science 372 6544:808-814. PubMed Id: 33858992. doi:10.1126/science.abf7958.
*Melanocortin-4 Receptor (MC4R) - G_s complex bound to agonist NDP-alpha-MSH: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.86 Å** cryo-EM structure with bound agonist setmelanotide, 2.58 Å 7PIU	7PIV	Data File Jmol Viewer 7PIV 7PIU	Heyder et al. (2021). Heyder NA, Kleinau G, Speck D, Schmidt A, Paisdzior S, Szczepek M, Bauer B, Koch A, Gallandi M, Kwiatkowski D, Bürger J, Mielke T, Beck-Sickinger AG, Hildebrand PW, Spahn CMT, Hilger D, Schacherl M, Biebermann H, Hilal T, Kühnen P, Kobilka BK, & Scheerer P (2021). Structures of active melanocortin-4 receptor-Gs-protein complexes with NDP-α-MSH and setmelanotide. Cell Res 31 11:1176-1189. PubMed Id: 34561620. doi:10.1038/s41422-021-00569-8.
*Melanocortin-4 Receptor (MC4R) - G_s complex with bound α-MSH: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å** cryo-EM structure with bound afamelanotide, 3.00 Å 7F54 with bound bremelanotide, 3.10 Å 7F55 with bound THIQ, 3.10 Å 7F58	7F53	Data File Jmol Viewer 7F53 7F55 7F58 7F54	Zhang et al. (2021). Zhang H, Chen LN, Yang D, Mao C, Shen Q, Feng W, Shen DD, Dai A, Xie S, Zhou Y, Qin J, Sun JP, Scharf DH, Hou T, Zhou T, Wang MW, & Zhang Y (2021). Structural insights into ligand recognition and activation of the melanocortin-4 receptor. Cell Res 31 11:1163-1175. PubMed Id: 34433901. doi:10.1038/s41422-021-00552-3.
*Melanocortin-5 Receptor (MC5R) - G_s complex with bound α-MSH: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.73 Å** cryo-EM structure with bound PG-901, 2.59 Å: 8IOD	8INR	Data File Jmol Viewer 8INR 8IOD	Feng et al. (2023). Feng W, Zhou Q, Chen X, Dai A, Cai X, Liu X, Zhao F, Chen Y, Ye C, Xu Y, Cong Z, Li H, Lin S, Yang D, & Wang MW (2023). Structural insights into ligand recognition and subtype selectivity of the human melanocortin-3 and melanocortin-5 receptors. Cell Discov 9 1:81. PubMed Id: 37524700. doi:10.1038/s41421-023-00586-4.
*Ghrelin receptor with Fab: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.30 Å** Engineered protein. Residues 1-28 replaced with b₅₆₂RIL. anti-Ghrelin receptor antibody, 1.75 Å: 6KS2	6KO5	Data File Jmol Viewer 6KO5 6KS2	Shiimura et al. (2020). Shiimura Y, Horita S, Hamamoto A, Asada H, Hirata K, Tanaka M, Mori K, Uemura T, Kobayashi T, Iwata S, & Kojima M (2020). Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode. Nat Commun 11 1:4160. PubMed Id: 32814772. doi:10.1038/s41467-020-17554-1.
*Ghrelin receptor in complex with G_q: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure with bound GHRP-6, 3.20 Å 7F9Z	7F9Y	Data File Jmol Viewer 7F9Y 7F9Z	Wang et al. (2021). Wang Y, Guo S, Zhuang Y, Yun Y, Xu P, He X, Guo J, Yin W, Xu HE, Xie X, & Jiang Y (2021). Molecular recognition of an acyl-peptide hormone and activation of ghrelin receptor. Nat Commun 12 1:5064. PubMed Id: 34417468. doi:10.1038/s41467-021-25364-2.
*Ghrelin receptor - G_i complex with bound synthetic agonist: Homo sapiens* E Eukaryota (expressed in Sf9 cells), 2.70 Å** cryo-EM structure with ghrelin and synthetic agonist, 2.70 Å 7NA8	7NA7	Data File Jmol Viewer 7NA7 7NA8	Liu et al. (2021). Liu H, Sun D, Myasnikov A, Damian M, Baneres JL, Sun J, & Zhang C (2021). Structural basis of human ghrelin receptor signaling by ghrelin and the synthetic agonist ibutamoren. Nat Commun 12 1:6410. PubMed Id: 34737341. doi:10.1038/s41467-021-26735-5.
*Ghrelin receptor - G_o complex with bound ghrelin: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.80 Å** cryo-EM structure x-ray: with inverse agonist, 2.94 Å 7F83	7W2Z	Data File Jmol Viewer 7W2Z 7F83	Qin et al. (2022). Qin J, Cai Y, Xu Z, Ming Q, Ji SY, Wu C, Zhang H, Mao C, Shen DD, Hirata K, Ma Y, Yan W, Zhang Y, & Shao Z (2022). Molecular mechanism of agonism and inverse agonism in ghrelin receptor. Nat Commun 13 1:300. PubMed Id: 35027551. doi:10.1038/s41467-022-27975-9.
*bile acids receptor TGR5 in complex with a synthetic agonist 23H: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.90 Å** cryo-EM structure	7BW0	Data File Jmol Viewer 7BW0	Chen et al. (2020). Chen G, Wang X, Ge Y, Ma L, Chen Q, Liu H, Du Y, Ye RD, Hu H, & Ren R (2020). Cryo-EM structure of activated bile acids receptor TGR5 in complex with stimulatory G protein. Signal Transduct Target Ther 5 1:142. PubMed Id: 32747649. doi:10.1038/s41392-020-00262-z.
*bile acids receptor-G_s complex, P395-bound: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å** cryo-EM structure INT-777-bound, 3.00 Å: 7CFN	7CFM	Data File Jmol Viewer 7CFM 7CFN	Yang et al. (2020). Yang F, Mao C, Guo L, Lin J, Ming Q, Xiao P, Wu X, Shen Q, Guo S, Shen DD, Lu R, Zhang L, Huang S, Ping Y, Zhang C, Ma C, Zhang K, Liang X, Shen Y, Nan F, Yi F, Luca VC, Zhou J, Jiang C, Sun JP, Xie X, Yu X, & Zhang Y (2020). Structural basis of GPBAR activation and bile acid recognition. Nature 587 7834:499-504. PubMed Id: 32698187. doi:10.1038/s41586-020-2569-1.
*gonadotropin-releasing hormone receptor GnRH1R in complex with antagonist elagolix: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.79 Å** Engineered protein. P. abysi glycogen synthase domain (PGS) replaces 3rd intracellular loop.	7BR3	Data File Jmol Viewer 7BR3	Yan et al. (2020). Yan W, Cheng L, Wang W, Wu C, Yang X, Du X, Ma L, Qi S, Wei Y, Lu Z, Yang S, & Shao Z (2020). Structure of the human gonadotropin-releasing hormone receptor GnRH1R reveals an unusual ligand binding mode. Nat Commun 11 1. PubMed Id: 33082324. doi:10.1038/s41467-020-19109-w.
*Arginine-vasopressin (AVP) receptor 2-G_s signaling complex: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.80 Å** cryo-EM structure	7KH0	Data File Jmol Viewer 7KH0	Wang et al. (2021). Wang L, Xu J, Cao S, Sun D, Liu H, Lu Q, Liu Z, Du Y, & Zhang C (2021). Cryo-EM structure of the AVP-vasopressin receptor 2-G_s signaling complex. Cell Res . PubMed Id: 33664408. doi:10.1038/s41422-021-00483-z.
*Arginine-vasopressin (AVP) receptor 2-G_s signaling complex, L state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 4.20 Å** cryo-EM structure T state, 4.40 Å: 7BB7	7BB6	Data File Jmol Viewer 7BB6 7BB7	Bous et al. (2021). Bous J, Orcel H, Floquet N, Leyrat C, Lai-Kee-Him J, Gaibelet G, Ancelin A, Saint-Paul J, Trapani S, Louet M, Sounier R, Déméné H, Granier S, Bron P, & Mouillac B (2021). Cryo-electron microscopy structure of the antidiuretic hormone arginine-vasopressin V2 receptor signaling complex. Sci Adv 7 21:eabg5628. PubMed Id: 34020960. doi:10.1126/sciadv.abg5628.
*Arginine-vasopressin (AVP) receptor 2-G_s signaling complex: Homo sapiens, Rattus norvegicus, Bos taurus, synthetic construct* E Eukaryota (expressed in Spodoptera frugiperda), 2.60 Å** cryo-EM structure	7DW9	Data File Jmol Viewer 7DW9	Zhou et al. (2021). Zhou F, Ye C, Ma X, Yin W, Croll TI, Zhou Q, He X, Zhang X, Yang D, Wang P, Xu HE, Wang MW, & Jiang Y (2021). Molecular basis of ligand recognition and activation of human V2 vasopressin receptor. Cell Res 31 8:929-931. PubMed Id: 33742150. doi:10.1038/s41422-021-00480-2.
*arginine-vasopressin (AVP) receptor 2 in complex with arrestin2-ScFv30: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 4.73 Å** cryo-EM structure C-ter-arrestin2-ScFv30 complex, 4.23 Å: 7R0J	7R0C	Data File Jmol Viewer 7R0C 7R0J	Bous et al. (2022). Bous J, Fouillen A, Orcel H, Trapani S, Cong X, Fontanel S, Saint-Paul J, Lai-Kee-Him J, Urbach S, Sibille N, Sounier R, Granier S, Mouillac B, & Bron P (2022). Structure of the vasopressin hormone-V2 receptor-β-arrestin1 ternary complex. Sci Adv 8 35:eabo7761. PubMed Id: 36054364. doi:10.1126/sciadv.abo7761.
*Epstein-Barr virus GPCR BILF1 in complex with human G_i: Homo sapiens & Human gammaherpesvirus 4* E Eukaryota (expressed in Trichoplusia ni), 3.20 Å** cryo-EM structure	7JHJ	Data File Jmol Viewer 7JHJ	Tsutsumi et al. (2021). Tsutsumi N, Qu Q, Mavri M, Baggesen MS, Maeda S, Waghray D, Berg C, Kobilka BK, Rosenkilde MM, Skiniotis G, & Garcia KC (2021). Structural basis for the constitutive activity and immunomodulatory properties of the Epstein-Barr virus-encoded G protein-coupled receptor BILF1. Immunity 54 7:1405-1416.e7. PubMed Id: 34216564. doi:10.1016/j.immuni.2021.06.001.
*Cholecystokinin A receptor (CCKAR or CCK1R) - G_i complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** cryo-EM structure G_s complex, 3.10 Å 7EZK G_q complex, 2.90 Å 7EZM	7EZH	Data File Jmol Viewer 7EZH 7EZM 7EZK	Liu et al. (2021). Liu Q, Yang D, Zhuang Y, Croll TI, Cai X, Dai A, He X, Duan J, Yin W, Ye C, Zhou F, Wu B, Zhao Q, Xu HE, Wang MW, & Jiang Y (2021). Ligand recognition and G-protein coupling selectivity of cholecystokinin A receptor. Nat Chem Biol 17 12:1238-1244. PubMed Id: 34556862. doi:10.1038/s41589-021-00841-3.
*Cholecystokinin A receptor (CCKAR or CCK1R) in complex with lintitript: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.80 Å** in complex with devazepide, 2.50 Å 7F8Y in complex with NN9056, 3.00 Å 7F8X cryo-EM structures: in complex with gastrin-17 and G_q, 3.10 Å 7F8W in complex with gastrin-17 and G_i, 3.30 Å 7F8V	7F8U	Data File Jmol Viewer 7F8U 7F8V 7F8Y 7F8X	Zhang et al. (2021). Zhang X, He C, Wang M, Zhou Q, Yang D, Zhu Y, Feng W, Zhang H, Dai A, Chu X, Wang J, Yang Z, Jiang Y, Sensfuss U, Tan Q, Han S, Reedtz-Runge S, Xu HE, Zhao S, Wang MW, Wu B, & Zhao Q (2021). Structures of the human cholecystokinin receptors bound to agonists and antagonists. Nat Chem Biol 17 12:1230-1237. PubMed Id: 34556863. doi:10.1038/s41589-021-00866-8.
*Cholecystokinin A receptor (CCKAR or CCK1R) - G_s complex: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 1.95 Å** cryo-EM structure G_q chimera (mG_sqi) complex, 2.44 Å 7MBY	7MBX	Data File Jmol Viewer 7MBX 7MBY	Mobbs et al. (2021). Mobbs JI, Belousoff MJ, Harikumar KG, Piper SJ, Xu X, Furness SGB, Venugopal H, Christopoulos A, Danev R, Wootten D, Thal DM, Miller LJ, & Sexton PM (2021). Structures of the human cholecystokinin 1 (CCK1) receptor bound to G_s and G_q mimetic proteins provide insight into mechanisms of G protein selectivity. PLoS Biol 19 6:3001295. PubMed Id: 34086670. doi:10.1371/journal.pbio.3001295.
*Cholecystokinin A receptor (CCKAR or CCK1R) - G_s complex with bound CCK-8: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** cryo-EM structure with bound SR146131, 3.00 Å 7XOV	7XOU	Data File Jmol Viewer 7XOU 7XOV	Ding et al. (2022). Ding Y, Zhang H, Liao YY, Chen LN, Ji SY, Qin J, Mao C, Shen DD, Lin L, Wang H, Zhang Y, & Li XM (2022). Structural insights into human brain-gut peptide cholecystokinin receptors. Cell Discov 8 1:55. PubMed Id: 35672283. doi:10.1038/s41421-022-00420-3.
*cholecystokinin B receptor (CCKBR or CCK2R) - G_i complex with bound gastrin-17: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.30 Å** cryo-EM structure G_q complex with bound gastrin-17, 3.10 Å 7F8W	7F8V	Data File Jmol Viewer 7F8V 7F8W	Zhang et al. (2021). Zhang X, He C, Wang M, Zhou Q, Yang D, Zhu Y, Feng W, Zhang H, Dai A, Chu X, Wang J, Yang Z, Jiang Y, Sensfuss U, Tan Q, Han S, Reedtz-Runge S, Xu HE, Zhao S, Wang MW, Wu B, & Zhao Q (2021). Structures of the human cholecystokinin receptors bound to agonists and antagonists. Nat Chem Biol 17 12:1230-1237. PubMed Id: 34556863. doi:10.1038/s41589-021-00866-8.
*cholecystokinin B receptor (CCKBR or CCK2R) - G_q complex with bound gastrin-17: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.10 Å** cryo-EM structure with bound CCK-8, 3.10 Å 7XOX	7XOW	Data File Jmol Viewer 7XOW 7XOX	Ding et al. (2022). Ding Y, Zhang H, Liao YY, Chen LN, Ji SY, Qin J, Mao C, Shen DD, Lin L, Wang H, Zhang Y, & Li XM (2022). Structural insights into human brain-gut peptide cholecystokinin receptors. Cell Discov 8 1:55. PubMed Id: 35672283. doi:10.1038/s41421-022-00420-3.
*Bradykinin Receptor, Type 1 (B1R) - G_q in complex with des-Arg10-kallidin: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å** cryo-EM structure	7EIB	Data File Jmol Viewer 7EIB	Yin et al. (2021). Yin YL, Ye C, Zhou F, Wang J, Yang D, Yin W, Wang MW, Xu HE, & Jiang Y (2021). Molecular basis for kinin selectivity and activation of the human bradykinin receptors. Nat Struct Mol Biol 28 9:755-761. PubMed Id: 34518695. doi:10.1038/s41594-021-00645-y.
*Bradykinin Receptor, type 2 (B2R) - G_q complexed with bradykinin: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure	7F2O	Data File Jmol Viewer 7F2O	Yin et al. (2021). Yin YL, Ye C, Zhou F, Wang J, Yang D, Yin W, Wang MW, Xu HE, & Jiang Y (2021). Molecular basis for kinin selectivity and activation of the human bradykinin receptors. Nat Struct Mol Biol 28 9:755-761. PubMed Id: 34518695. doi:10.1038/s41594-021-00645-y.
*Bradykinin Receptor, type 2 (B2R) - G_q complexed with bradykinin: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure in complex with kallidin, 2.80 Å 7F6I	7F6H	Data File Jmol Viewer 7F6H 7F6I	Shen et al. (2022). Shen J, Zhang D, Fu Y, Chen A, Yang X, & Zhang H (2022). Cryo-EM structures of human bradykinin receptor-G_q proteins complexes. Nat Commun 13 1:714. PubMed Id: 35132089. doi:10.1038/s41467-022-28399-1.
*mas-related GPCR (MRGPRX) receptor, G_q-coupled MRGPRX1 with bound BAM 8-14: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.87 Å** cryo-EM structure with bound BAM 8-14 and ML382, 2.71 Å:8DWG with bound compound-16, 3.25 Å: 8DWH	8DWC	Data File Jmol Viewer 8DWC 8DWG 8DWH	Liu et al. (2023). Liu Y, Cao C, Huang XP, Gumpper RH, Rachman MM, Shih SL, Krumm BE, Zhang S, Shoichet BK, Fay JF, & Roth BL (2023). Ligand recognition and allosteric modulation of the human MRGPRX1 receptor. Nat Chem Biol 19 4:416-422. PubMed Id: 36302898. doi:10.1038/s41589-022-01173-6.
*mas-related GPCR (MRGPRX) receptor, G_q-coupled MRGPRX1 with bound peptide agonist BAM 8-22: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.70 Å** cryo-EM structure MRGPRX1-G_i complex with bound peptide agonist CNF-Tx2, 2.84 Å: 8JGB MRGPRX1-G_i complex with bound peptide agonist BAM8-22, 3.00 Å: 8JGG	8JGF	Data File Jmol Viewer 8JGF 8JGG 8JGB	Guo et al. (2023). Guo L, Zhang Y, Fang G, Tie L, Zhuang Y, Xue C, Liu Q, Zhang M, Zhu K, You C, Xu P, Yuan Q, Zhang C, Liu L, Rong N, Peng S, Liu Y, Wang C, Luo X, Lv Z, Kang D, Yu X, Zhang C, Jiang Y, Dong X, Zhou J, Liu Z, Yang F, Eric Xu H, & Sun JP (2023). Ligand recognition and G protein coupling of the human itch receptor MRGPRX1. Nat Commun 14 1:5004. PubMed Id: 37591889. doi:10.1038/s41467-023-40705-z.
*mas-related GPCR (MRGPRX) itch receptor, G_q-coupled MRGPRX2 with bound agonist cortistatin-14: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.45 Å** cryo-EM structure G_i-coupled MRGPRX2 with peptide agonist Cortistatin-14, 2.54 Å 7S8M G_q-coupled MRGPRX2 with bound agonist (R)-Zinc-3573, 2.90 Å 7S8N G_i-coupled MRGPRX2 with small molecule agonist (R)-Zinc-3573, 2.58 Å 7S8O G_q-coupled MRGPRX4 with small molecule agonist MS47134, 2.60 Å 7S8P	7S8L	Data File Jmol Viewer 7S8L 7S8N 7S8M 7S8P 7S8O	Cao et al. (2021). Cao C, Kang HJ, Singh I, Chen H, Zhang C, Ye W, Hayes BW, Liu J, Gumpper RH, Bender BJ, Slocum ST, Krumm BE, Lansu K, McCorvy JD, Kroeze WK, English JG, DiBerto JF, Olsen RHJ, Huang XP, Zhang S, Liu Y, Kim K, Karpiak J, Jan LY, Abraham SN, Jin J, Shoichet BK, Fay JF, & Roth BL (2021). Structure, function and pharmacology of human itch GPCRs. Nature 600 7887:170-175. PubMed Id: 34789874. doi:10.1038/s41586-021-04126-6.
*luteinizing hormone/choriogonadotropin receptor (LHCGR): Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.80 Å** cryo-EM structure in complex with chorionic gonadotropin-G_s, 4.30 Å 7FII S277I mutant of chorionic gonadotropin-G_s complex, 3.90 Å 7FIG S277I mutant of chorionic gonadotropin-G_s complex with Org43553, 3.20 Å 7FIH	7FIJ	Data File Jmol Viewer 7FIJ 7FIH 7FII 7FIG	Duan et al. (2021). Duan J, Xu P, Cheng X, Mao C, Croll T, He X, Shi J, Luan X, Yin W, You E, Liu Q, Zhang S, Jiang H, Zhang Y, Jiang Y, & Xu HE (2021). Structures of full-length glycoprotein hormone receptor signalling complexes. Nature 598 7882:688-692. PubMed Id: 34552239. doi:10.1038/s41586-021-03924-2.
*Mas-related GPCR (MRGPR) MRGPRX2 complex with PAMP-12. state1: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.84 Å** cryo-EM structure with PAMP-12, state2, 2.89 Å 7VUZ with PAMP-12, local, 3.50 Å 7VV0 complex with substance P, 2.98 Å 7VDM complex with circular cortistatin-14, 3.22 Å 7VDL complex with linear cortistatin-14, 2.97 Å 7VV3 complex with linear cortistatin-14, local, 2.97 Å 7VV4 complex with C48/80, state1, 2.76 Å 7VV5 complex with C48/80, state2, 2.90 Å 7VDH complex with C48/80, local, 3.30 Å 7VV6	7VUY	Data File Jmol Viewer 7VUY 7VV0 7VUZ 7VDM 7VDH 7VV3 7VDL 7VV6 7VV4 7VV5	Yang et al. (2021). Yang F, Guo L, Li Y, Wang G, Wang J, Zhang C, Fang GX, Chen X, Liu L, Yan X, Liu Q, Qu C, Xu Y, Xiao P, Zhu Z, Li Z, Zhou J, Yu X, Gao N, & Sun JP (2021). Structure, function and pharmacology of human itch receptor complexes. Nature 600 7887:164-169. PubMed Id: 34789875. doi:10.1038/s41586-021-04077-y.
*somatostatin receptor 2 (SSTR2) - G_i3 complex with bound somatostatin-14: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.50 Å** cryo-EM structure with bound Octreotide, 2.70 Å 7T11	7T10	Data File Jmol Viewer 7T10 7T11	Robertson et al. (2022). Robertson MJ, Meyerowitz JG, Panova O, Borrelli K, & Skiniotis G (2022). Plasticity in ligand recognition at somatostatin receptors. Nat Struct Mol Biol 29 3:210-217. PubMed Id: 35210615. doi:10.1038/s41594-022-00727-5.
*somatostatin receptor 2 (SSTR2) - G_i1 complex with bound somatostatin-14: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.80 Å** cryo-EM structure with bound L-054,264, 2.70 Å 7WIG	7WIC	Data File Jmol Viewer 7WIC 7WIG	Chen et al. (2022). Chen LN, Wang WW, Dong YJ, Shen DD, Guo J, Yu X, Qin J, Ji SY, Zhang H, Shen Q, He Q, Yang B, Zhang Y, Li Q, & Mao C (2022). Structures of the endogenous peptide- and selective non-peptide agonist-bound SSTR2 signaling complexes. Cell Res . PubMed Id: 35578016. doi:10.1038/s41422-022-00669-z.
*somatostatin receptor 2 (SSTR2) - G_i1 complex with bound somatostatin-14: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.72 Å** cryo-EM structure	7WJ5	Data File Jmol Viewer 7WJ5	Heo et al. (2022). Heo Y, Yoon E, Jeon YE, Yun JH, Ishimoto N, Woo H, Park SY, Song JJ, & Lee W (2022). Cryo-EM structure of the human somatostatin receptor 2 complex with its agonist somatostatin delineates the ligand-binding specificity. Elife 11 :76823. PubMed Id: 35446253. doi:10.7554/eLife.76823.
*somatostatin receptor 2 (SSTR2) with bound L-054,522: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.60 Å** with bound peptide antagonist CYN 154806, 2.65 Å: 7XNA G_i1 complex with bound endogeneous peptide ligand SST-14, cryo-EM structure, 3.10 Å: 7XMR	7XN9	Data File Jmol Viewer 7XN9 7XMR 7XNA	Zhao et al. (2022). Zhao W, Han S, Qiu N, Feng W, Lu M, Zhang W, Wang M, Zhou Q, Chen S, Xu W, Du J, Chu X, Yi C, Dai A, Hu L, Shen MY, Sun Y, Zhang Q, Ma Y, Zhong W, Yang D, Wang MW, Wu B, & Zhao Q (2022). Structural insights into ligand recognition and selectivity of somatostatin receptors. Cell Res 32 8:761-772. PubMed Id: 35739238. doi:10.1038/s41422-022-00679-x.
*somatostatin receptor 2 (SSTR2) - G_i complex with bound somatostatin-14: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.85 Å** cryo-EM structure with bound octreotide , 2.97 Å: 7XAU with bound lanreotide, 2.87 Å: 7XAV	7XAT	Data File Jmol Viewer 7XAT 7XAV 7XAU	Bo et al. (2022). Bo Q, Yang F, Li Y, Meng X, Zhang H, Zhou Y, Ling S, Sun D, Lv P, Liu L, Shi P, & Tian C (2022). Structural insights into the activation of somatostatin receptor 2 by cyclic SST analogues. Cell Discov 8 1:47. PubMed Id: 35595746. doi:10.1038/s41421-022-00405-2.
*somatostatin receptor 2 (SSTR2), apo receptor in complex with nanobody Nb6: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.10 Å** cryo-EM structure	7UL5	Data File Jmol Viewer 7UL5	Robertson et al. (2022). Robertson MJ, Papasergi-Scott MM, He F, Seven AB, Meyerowitz JG, Panova O, Peroto MC, Che T, & Skiniotis G (2022). Structure determination of inactive-state GPCRs with a universal nanobody. Nat Struct Mol Biol 29 12:1188-1195. PubMed Id: 36396979. doi:10.1038/s41594-022-00859-8.
*somatostatin receptor 2 (SSTR2) - miniG_o complex with bound octreotide: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.25 Å** cryo-EM structure miniG_q complex with bound octreotide, 3.30 Å: 7Y26 miniG_q complex with bound SST-14, 3.48 Å: 7Y27	7Y24	Data File Jmol Viewer 7Y24 7Y26 7Y27	Chen et al. (2023). Chen S, Teng X, & Zheng S (2023). Molecular basis for the selective G protein signaling of somatostatin receptors. Nat Chem Biol 19 2:133-140. PubMed Id: 36138141. doi:10.1038/s41589-022-01130-3.
*somatostatin receptor 2 (SSTR2) - G_i1 complex with bound octreotide: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.37 Å** cryo-EM structure with bound paltusotine, 3.24 Å: 7YAC	7YAE	Data File Jmol Viewer 7YAE 7YAC	Zhao et al. (2023). Zhao J, Fu H, Yu J, Hong W, Tian X, Qi J, Sun S, Zhao C, Wu C, Xu Z, Cheng L, Chai R, Yan W, Wei X, & Shao Z (2023). Prospect of acromegaly therapy: molecular mechanism of clinical drugs octreotide and paltusotine. Nat Commun 14 1:962. PubMed Id: 36810324. doi:10.1038/s41467-023-36673-z.
*somatostatin receptor 4 (SSTR4) - G_i1 complex with bound SST-14: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure G_i1 complex with bound J-2156, 2.80 Å: 7XMT	7XMS	Data File Jmol Viewer 7XMS 7XMT	Zhao et al. (2022). Zhao W, Han S, Qiu N, Feng W, Lu M, Zhang W, Wang M, Zhou Q, Chen S, Xu W, Du J, Chu X, Yi C, Dai A, Hu L, Shen MY, Sun Y, Zhang Q, Ma Y, Zhong W, Yang D, Wang MW, Wu B, & Zhao Q (2022). Structural insights into ligand recognition and selectivity of somatostatin receptors. Cell Res 32 8:761-772. PubMed Id: 35739238. doi:10.1038/s41422-022-00679-x.
*galanin receptor 1 (GALR1) - G_i complex with bound galanin: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.70 Å** cryo-EM structure	7WQ3	Data File Jmol Viewer 7WQ3	Duan et al. (2022). Duan J, Shen DD, Zhao T, Guo S, He X, Yin W, Xu P, Ji Y, Chen LN, Liu J, Zhang H, Liu Q, Shi Y, Cheng X, Jiang H, Eric Xu H, Zhang Y, Xie X, & Jiang Y (2022). Molecular basis for allosteric agonism and G protein subtype selectivity of galanin receptors. Nat Commun 13 1:1364. PubMed Id: 35292680. doi:10.1038/s41467-022-29072-3.
*galanin receptor 2 (GALR2) - G_q complex with bound galanin: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.60 Å** cryo-EM structure	7WQ4	Data File Jmol Viewer 7WQ4	Duan et al. (2022). Duan J, Shen DD, Zhao T, Guo S, He X, Yin W, Xu P, Ji Y, Chen LN, Liu J, Zhang H, Liu Q, Shi Y, Cheng X, Jiang H, Eric Xu H, Zhang Y, Xie X, & Jiang Y (2022). Molecular basis for allosteric agonism and G protein subtype selectivity of galanin receptors. Nat Commun 13 1:1364. PubMed Id: 35292680. doi:10.1038/s41467-022-29072-3.
*galanin receptor 2 (GALR2) - G_q complex with bound galanin: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.11 Å** cryo-EM structure	7XBD	Data File Jmol Viewer 7XBD	Heo et al. (2022). Heo Y, Ishimoto N, Jeon YE, Yun JH, Ohki M, Anraku Y, Sasaki M, Kita S, Fukuhara H, Ikuta T, Kawakami K, Inoue A, Maenaka K, Tame JRH, Lee W, & Park SY (2022). Structure of the human galanin receptor 2 bound to galanin and Gq reveals the basis of ligand specificity and how binding affects the G-protein interface. PLoS Biol 20 8:e3001714. PubMed Id: 35913979. doi:10.1371/journal.pbio.3001714.
*thyroid-stimulating hormone receptor (TSHR) - Gs complex with bound TSH and ML109: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.96 Å** cryo-EM structure with bound autoantibody M22 and ML109, 2.78 Å: 7XW6 TSHR complexed with inhibitory antibody K1-70, 5.50 Å: 7XW7	7XW5	Data File Jmol Viewer 7XW5 7XW7 7XW6	Duan et al. (2022). Duan J, Xu P, Luan X, Ji Y, He X, Song N, Yuan Q, Jin Y, Cheng X, Jiang H, Zheng J, Zhang S, Jiang Y, & Xu HE (2022). Hormone- and antibody-mediated activation of the thyrotropin receptor. Nature 609 7928:854-859. PubMed Id: 35940204. doi:10.1038/s41586-022-05173-3.
*thyroid-stimulating hormone receptor (TSHR) in complex with miniG_s399: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure with thyrotropin analog TR1402 in complex with miniG_s399, 2.40 Å: 7UTZ with bound M22 Agonist Autoantibody in complex with miniG_s399, 2.90 Å: 7T9N bound by CS-17 Inverse Agonist Fab/Org 274179-0 Antagonist, 3.10 Å: 7TM9	7T9I	Data File Jmol Viewer 7T9I 7TM9 7T9N 7UTZ	Faust et al. (2022). Faust B, Billesbølle CB, Suomivuori CM, Singh I, Zhang K, Hoppe N, Pinto AFM, Diedrich JK, Muftuoglu Y, Szkudlinski MW, Saghatelian A, Dror RO, Cheng Y, & Manglik A (2022). Autoantibody mimicry of hormone action at the thyrotropin receptor. Nature 609 7928:846-853. PubMed Id: 35940205. doi:10.1038/s41586-022-05159-1.
*thyrotropin-releasing hormone receptor (TRHR) - G_q complex with bound TRH: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.01 Å** cryo-EM structure	7WKD	Data File Jmol Viewer 7WKD	Xu et al. (2022). Xu Y, Cai H, You C, He X, Yuan Q, Jiang H, Cheng X, Jiang Y, & Xu HE (2022). Structural insights into ligand binding and activation of the human thyrotropin-releasing hormone receptor. Cell Res 32 9:855-857. PubMed Id: 35365755. doi:10.1038/s41422-022-00641-x.
*Gastrin Releasing Peptide Receptor (GRPR) - G_q complex with bound agonist GRP: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.00 Å** cryo-EM structure with bound agonist Bombesin, 3.00 Å: 7W40 GRPR with bound antagonist PD176252, x-ray structure, 2.95 Å: 7W41	7W3Z	Data File Jmol Viewer 7W3Z 7W41 7W40	Peng et al. (2023). Peng S, Zhan Y, Zhang D, Ren L, Chen A, Chen ZF, & Zhang H (2023). Structures of human gastrin-releasing peptide receptors bound to antagonist and agonist for cancer and itch therapy. Proc Natl Acad Sci U S A 120 6:e2216230120. PubMed Id: 36724251. doi:10.1073/pnas.2216230120.
*Olfactory Receptor OR51E2 - miniG_s399 complex with bound propionate: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.10 Å** cryo-EM structure	8F76	Data File Jmol Viewer 8F76	Billesbølle et al. (2023). Billesbølle CB, de March CA, van der Velden WJC, Ma N, Tewari J, Del Torrent CL, Li L, Faust B, Vaidehi N, Matsunami H, & Manglik A (2023). Structural basis of odorant recognition by a human odorant receptor. Nature 615 7953:742-749. PubMed Id: 36922591. doi:10.1038/s41586-023-05798-y.
*Follicle stimulating hormone repceotr (FSHR) - G_s complex with bound compound 716340: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.80 Å** cryo-EM structure inactive FSHR, 6.00 Å: 8I2H	8I2G	Data File Jmol Viewer 8I2G 8I2H	Duan et al. (2023). Duan J, Xu P, Zhang H, Luan X, Yang J, He X, Mao C, Shen DD, Ji Y, Cheng X, Jiang H, Jiang Y, Zhang S, Zhang Y, & Xu HE (2023). Mechanism of hormone and allosteric agonist mediated activation of follicle stimulating hormone receptor. Nat Commun 14 1:519. PubMed Id: 36720854. doi:10.1038/s41467-023-36170-3.
*Relaxin family peptide receptor 1 (RXFP1) - G_s complex: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure	7TMW	Data File Jmol Viewer 7TMW	Erlandson et al. (2023). Erlandson SC, Rawson S, Osei-Owusu J, Brock KP, Liu X, Paulo JA, Mintseris J, Gygi SP, Marks DS, Cong X, & Kruse AC (2023). The relaxin receptor RXFP1 signals through a mechanism of autoinhibition. Nat Chem Biol 19 8:1013-1021. PubMed Id: 37081311. doi:10.1038/s41589-023-01321-6.
*Relaxin family peptide receptor 4 (RXFP4) - G_i complex with bound insulin-like peptide INSL5: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.19 Å** cryo-EM structure with bound compound 4, 3.03 Å: 7YK6 with bound DC591053, 2.75 Å: 7YK7	7YJ4	Data File Jmol Viewer 7YJ4 7YK6 7YK7	Chen et al. (2023). Chen Y, Zhou Q, Wang J, Xu Y, Wang Y, Yan J, Wang Y, Zhu Q, Zhao F, Li C, Chen CW, Cai X, Bathgate RAD, Shen C, Eric Xu H, Yang D, Liu H, & Wang MW (2023). Ligand recognition mechanism of the human relaxin family peptide receptor 4 (RXFP4). Nat Commun 14 1:492. PubMed Id: 36717591. doi:10.1038/s41467-023-36182-z.
*endothelin ETA receptor - G_q complex, with bound endothelin-1: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.01 Å** cryo-EM structure	8HCQ	Data File Jmol Viewer 8HCQ	Ji et al. (2023). Ji Y, Duan J, Yuan Q, He X, Yang G, Zhu S, Wu K, Hu W, Gao T, Cheng X, Jiang H, Eric Xu H, & Jiang Y (2023). Structural basis of peptide recognition and activation of endothelin receptors. Nat Commun 14 1:1268. PubMed Id: 36882417. doi:10.1038/s41467-023-36998-9.
*endothelin ETB receptor - G_i complex, with bound IRL1620: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.99 Å** cryo-EM structure with bound endothelin-1, 3.50 Å: 8HCX	8HCD	Data File Jmol Viewer 8HCD 8HCX	Ji et al. (2023). Ji Y, Duan J, Yuan Q, He X, Yang G, Zhu S, Wu K, Hu W, Gao T, Cheng X, Jiang H, Eric Xu H, & Jiang Y (2023). Structural basis of peptide recognition and activation of endothelin receptors. Nat Commun 14 1:1268. PubMed Id: 36882417. doi:10.1038/s41467-023-36998-9.
*HCA2 hydroxycarboxylic acid receptor 2 (GPR109A, niacin receptor) - G_i complex with bound MK6892: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure x-ray structure, 2.70 Å: 7ZL9 x-ray structure, expressed in SF9 cells, 2.70 Å: 7ZLY	7XK2	Data File Jmol Viewer 7XK2 7ZL9 7ZLY	Yang et al. (2023). Yang Y, Kang HJ, Gao R, Wang J, Han GW, DiBerto JF, Wu L, Tong J, Qu L, Wu Y, Pileski R, Li X, Zhang XC, Zhao S, Kenakin T, Wang Q, Stevens RC, Peng W, Roth BL, Rao Z, & Liu ZJ (2023). Structural insights into the human niacin receptor HCA2-Gi signalling complex. Nat Commun 14 1:1692. PubMed Id: 36973264. doi:10.1038/s41467-023-37177-6.
*HCA2 hydroxycarboxylic acid receptor 2 (GPR109A, niacin receptor) - G_i complex with bound GSK256073: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.85 Å** cryo-EM structure with bound MK6892, 2.97 Å: 8IHF with bound LUF6283, 3.06 Å: 8IHH with bound acifran, 3.11 Å: 8IHI	8IHB	Data File Jmol Viewer 8IHB 8IHF 8IHH 8IHI	Suzuki et al. (2023). Suzuki S, Tanaka K, Nishikawa K, Suzuki H, Oshima A, & Fujiyoshi Y (2023). Structural basis of hydroxycarboxylic acid receptor signaling mechanisms through ligand binding. Nat Commun 14 1:5899. PubMed Id: 37736747. doi:10.1038/s41467-023-41650-7.
*HCA2 hydroxycarboxylic acid receptor 2 (GPR109A, niacin receptor) - G_i complex, apo state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.28 Å** cryo-EM structure with bound niacin, 2.69 Å: 8IJA with bound acipimox, 3.23 Å: 8IJB with bound agonist MK-6892, 3.25 Å: 8IJD	8IJ3	Data File Jmol Viewer 8IJ3 8IJB 8IJD 8IJA	Pan et al. (2023). Pan X, Ye F, Ning P, Zhang Z, Li X, Zhang B, Wang Q, Chen G, Gao W, Qiu C, Wu Z, Li J, Zhu L, Xia J, Gong K, & Du Y (2023). Structural insights into ligand recognition and selectivity of the human hydroxycarboxylic acid receptor HCAR2. Cell Discov 9 1:118. PubMed Id: 38012147. doi:10.1038/s41421-023-00610-7.
*HCA2 hydroxycarboxylic acid receptor 2 (GPR109A, niacin receptor) - G_i complex with bound niacin: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.01 Å** cryo-EM structure local refinement, 3.43 Å: 8K5B with bound acipimox, 2.77 Å: 8I7V with bound acipimox, local refinement, 3.13 Å: 8K5C with bound GSK256073, 3.39 Å: 8I7W with bound GSK256073, local refinement, 3.74 Å: 8K5D	8H2G	Data File Jmol Viewer 8H2G 8I7V 8K5C 8K5B 8I7W 8K5D	Park et al. (2023). Park JH, Kawakami K, Ishimoto N, Ikuta T, Ohki M, Ekimoto T, Ikeguchi M, Lee DS, Lee YH, Tame JRH, Inoue A, & Park SY (2023). Structural basis for ligand recognition and signaling of hydroxy-carboxylic acid receptor 2. Nat Commun 14 1:7150. PubMed Id: 37932263. doi:10.1038/s41467-023-42764-8.
*HCA2 hydroxycarboxylic acid receptor 2 (GPR109A, niacin receptor) - G_i complex with bound niacin: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.05 Å** cryo-EM structure with bound agonist MK-6892, 2.92 Å: 8J6I with bound agonist GSK256073, 2.80 Å: 8J6L	8J6L	Data File Jmol Viewer 8J6L 8J6I 8J6L	Zhu et al. (2023). Zhu S, Yuan Q, Li X, He X, Shen S, Wang D, Li J, Cheng X, Duan X, Xu HE, & Duan J (2023). Molecular recognition of niacin and lipid-lowering drugs by the human hydroxycarboxylic acid receptor 2. Cell Rep 42 11:113406. PubMed Id: 37952153. doi:10.1016/j.celrep.2023.113406.
*HCA3 hydroxycarboxylic acid receptor 3 (GPR109B, niacin receptor) - G_i complex with bound acifran: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.07 Å** cryo-EM structure local refinement, 3.21 Å: 8IHK	8IHJ	Data File Jmol Viewer 8IHJ 8IHK	Suzuki et al. (2023). Suzuki S, Tanaka K, Nishikawa K, Suzuki H, Oshima A, & Fujiyoshi Y (2023). Structural basis of hydroxycarboxylic acid receptor signaling mechanisms through ligand binding. Nat Commun 14 1:5899. PubMed Id: 37736747. doi:10.1038/s41467-023-41650-7.
*TAAR1 Trace-amine-associated receptor - G_s protein complex with bound T1AM: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.24 Å** cryo-EM structure with bound Ulotaront (SEP-363856), 3.52 Å: 8JLO with bound Ralmitaront (RO-6889450), 3.23 Å: 8JLP with bound Fenoldopam, 2.84 Å: 8JLQ with bound A77636, 3.00 Å: 8JLR with bound AMPH, 3.40 Å: 8JSO	8JLN	Data File Jmol Viewer 8JLN 8JLP 8JLO 8JLR 8JSO 8JLQ	Xu et al. (2023). Xu Z, Guo L, Yu J, Shen S, Wu C, Zhang W, Zhao C, Deng Y, Tian X, Feng Y, Hou H, Su L, Wang H, Guo S, Wang H, Wang K, Chen P, Zhao J, Zhang X, Yong X, Cheng L, Liu L, Yang S, Yang F, Wang X, Yu X, Xu Y, Sun JP, Yan W, & Shao Z (2023). Ligand recognition and G-protein coupling of trace amine receptor TAAR1. Nature . PubMed Id: 37935376. doi:10.1038/s41586-023-06804-z.
*TAAR1 Trace-amine-associated receptor - G_s protein complex with bound methamphetamine: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.80 Å** cryo-EM structure with bound SEP-363856, 2.60 Å: 8W88 with bound β-phenylethylamine, 3.00 Å: 8W89 with bound RO5256390, 2.80 Å: 8W8A	8W87	Data File Jmol Viewer 8W87 8W88 8W89 8W8A	Liu et al. (2023). Liu H, Zheng Y, Wang Y, Wang Y, He X, Xu P, Huang S, Yuan Q, Zhang X, Wang L, Jiang K, Chen H, Li Z, Liu W, Wang S, Xu HE, & Xu F (2023). Recognition of methamphetamine and other amines by trace amine receptor TAAR1. Nature 624 7992:663-671. PubMed Id: 37935377. doi:10.1038/s41586-023-06775-1.
*TAAR1 Trace-amine-associated receptor - G_s protein complex with bound T1AM: Mus musculus* E Eukaryota (expressed in S. frugiperda), 3.10 Å** cryo-EM structure with bound Ulotaront(SEP-363856), 3.22 Å, 8JLK	8JLJ	Data File Jmol Viewer 8JLJ 8JLK	Xu et al. (2023). Xu Z, Guo L, Yu J, Shen S, Wu C, Zhang W, Zhao C, Deng Y, Tian X, Feng Y, Hou H, Su L, Wang H, Guo S, Wang H, Wang K, Chen P, Zhao J, Zhang X, Yong X, Cheng L, Liu L, Yang S, Yang F, Wang X, Yu X, Xu Y, Sun JP, Yan W, & Shao Z (2023). Ligand recognition and G-protein coupling of trace amine receptor TAAR1. Nature . PubMed Id: 37935376. doi:10.1038/s41586-023-06804-z.
G Protein-Coupled Receptors: Class B1
*Corticotropin-releasing factor receptor 1 (CRF1R) in complex with CP-376395 small-molecule antagonist: Homo sapiens* E Eukaryota, 2.98 Å** Engineered protein: T4 lysozyme inserted between TM helices III and IV. Lacks the N-terminal extracellular domain.	4K5Y	Data File Jmol Viewer 4K5Y	Hollenstein et al. (2013). Hollenstein K, Kean J, Bortolato A, Cheng RK, Doré AS, Jazayeri A, Cooke RM, Weir M, & Marshall FH (2013). Structure of class B GPCR corticotropin-releasing factor receptor 1. Nature 499 7459:438-443. PubMed Id: 23863939. doi:10.1038/nature12357.
*Corticotropin-releasing factor 1 (CRF1) receptor in complex with G_s protein and bound Urocortin 1: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3 Å** cryo-EM structure	6PB0	Data File Jmol Viewer 6PB0	Ma et al. (2020). Ma S, Shen Q, Zhao LH, Mao C, Zhou XE, Shen DD, de Waal PW, Bi P, Li C, Jiang Y, Wang MW, Sexton PM, Wootten D, Melcher K, Zhang Y, & Xu HE (2020). Molecular Basis for Hormone Recognition and Activation of Corticotropin-Releasing Factor Receptors. Mol Cell 77 3:669-680.e4. PubMed Id: 32004470. doi:10.1016/j.molcel.2020.01.013.
*corticotropin-releasing factor receptor 1 (CRF1), G_s GPCR protein complex with CRF1 peptide: Homo sapien* E Eukaryota (expressed in Trichoplusia ni), 2.91 Å** cryo-EM structure	6P9X	Data File Jmol Viewer 6P9X	Liang et al. (2020). Liang YL, Belousoff MJ, Zhao P, Koole C, Fletcher MM, Truong TT, Julita V, Christopoulos G, Xu HE, Zhang Y, Khoshouei M, Christopoulos A, Danev R, Sexton PM, & Wootten D (2020). Toward a Structural Understanding of Class B GPCR Peptide Binding and Activation. Mol Cell 77 3:656-668.e5. PubMed Id: 32004469. doi:10.1016/j.molcel.2020.01.012.
*Corticotropin-releasing factor 2 (CRF2) receptor in complex with G_s protein with bound Urocortin 1: Homo sapiens* E Eukaryota, 2.8 Å** cryo-EM structure	6PB1	Data File Jmol Viewer 6PB1	Ma et al. (2020). Ma S, Shen Q, Zhao LH, Mao C, Zhou XE, Shen DD, de Waal PW, Bi P, Li C, Jiang Y, Wang MW, Sexton PM, Wootten D, Melcher K, Zhang Y, & Xu HE (2020). Molecular Basis for Hormone Recognition and Activation of Corticotropin-Releasing Factor Receptors. Mol Cell 77 3:669-680.e4. PubMed Id: 32004470. doi:10.1016/j.molcel.2020.01.013.
*Corticotropin-releasing factor 2 (CRF2) receptor in complex with G_s protein with bound Urocortin 1: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.70 Å** cryo-EM structure bound to Urocortin 1 and coupled with heterotrimeric G_o protein, 2.80 Å: 7TS0	7TRY	Data File Jmol Viewer 7TRY 7TS0	Zhao et al. (2022). Zhao LH, Lin J, Ji SY, Zhou XE, Mao C, Shen DD, He X, Xiao P, Sun J, Melcher K, Zhang Y, Yu X, & Xu HE (2022). Structure insights into selective coupling of G protein subtypes by a class B G protein-coupled receptor. Nat Commun 13 1:6670. PubMed Id: 36335102. doi:10.1038/s41467-022-33851-3.
*Pituitary adenylate cyclase-activating peptide (PAC1) receptor GPCR complex: Homo sapiens* E Eukaryota, 3.01 Å** cryo-EM structure	6P9Y	Data File Jmol Viewer 6P9Y	Liang et al. (2020). Liang YL, Belousoff MJ, Zhao P, Koole C, Fletcher MM, Truong TT, Julita V, Christopoulos G, Xu HE, Zhang Y, Khoshouei M, Christopoulos A, Danev R, Sexton PM, & Wootten D (2020). Toward a Structural Understanding of Class B GPCR Peptide Binding and Activation. Mol Cell 77 3:656-668.e5. PubMed Id: 32004469. doi:10.1016/j.molcel.2020.01.012.
*PAC1 receptor coupled to engineered heterotrimeric G protein: Homo sapiens* E Eukaryota, 3.9 Å** cryo-EM structure	6LPB	Data File Jmol Viewer 6LPB	Kobayashi et al. (2020). Kobayashi K, Shihoya W, Nishizawa T, Kadji FMN, Aoki J, Inoue A, & Nureki O (2020). Cryo-EM structure of the human PAC1 receptor coupled to an engineered heterotrimeric G protein. Nat Struct Mol Biol 27 3:274-280. PubMed Id: 32157248. doi:10.1038/s41594-020-0386-8.
*PAC1-G_s receptor in complex with PACAP38: Homo sapiens* E Eukaryota (expressed in Insect BA phytoplasma), 3.50 Å** cryo-EM structure in complex with maxadilan, 3.60 Å: 6M1H	6M1I	Data File Jmol Viewer 6M1I 6M1H	Wang et al. (2020). Wang J, Song X, Zhang D, Chen X, Li X, Sun Y, Li C, Song Y, Ding Y, Ren R, Harrington EH, Hu LA, Zhong W, Xu C, Huang X, Wang HW, & Ma Y (2020). Cryo-EM structures of PAC1 receptor reveal ligand binding mechanism. Cell Res 30 5:436-445. PubMed Id: 32047270. doi:10.1038/s41422-020-0280-2.
*glucagon receptor (GCGR): Homo sapiens* E Eukaryota, 3.30 Å** Engineered Protein: E. coli apocytochrome b562 RIL (BRIL) fused at residue 123. C-terminus truncated at residue 432.	4L6R	Data File Jmol Viewer 4L6R	Siu et al. (2013). Siu FY, He M, de Graaf C, Han GW, Yang D, Zhang Z, Zhou C, Xu Q, Wacker D, Joseph JS, Liu W, Lau J, Cherezov V, Katritch V, Wang MW, & Stevens RC (2013). Structure of the human glucagon class B G-protein-coupled receptor. Nature 499 7459:444-449. PubMed Id: 23863937. doi:10.1038/nature12393.
*Full-length glucagon receptor (GCGR) in complex with antagonist MK-0893: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.50 Å**	5EE7	Data File Jmol Viewer 5EE7	Jazayeri et al. (2016). Jazayeri A, Doré AS, Lamb D, Krishnamurthy H, Southall SM, Baig AH, Bortolato A, Koglin M, Robertson NJ, Errey JC, Andrews SP, Teobald I, Brown AJ, Cooke RM, Weir M, & Marshall FH (2016). Extra-helical binding site of a glucagon receptor antagonist. Nature 533 7602:274-277. PubMed Id: 27111510. doi:10.1038/nature17414.
*Full-length glucagon receptor (GCGR) in complex with a truncated peptide: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.7 Å**	5NX2	Data File Jmol Viewer 5NX2	Jazayeri et al. (2017). Jazayeri A, Rappas M, Brown AJH, Kean J, Errey JC, Robertson NJ, Fiez-Vandal C, Andrews SP, Congreve M, Bortolato A, Mason JS, Baig AH, Teobald I, Doré AS, Weir M, Cooke RM, & Marshall FH (2017). Crystal structure of the GLP-1 receptor bound to a peptide agonist. Nature 546 :254-258. PubMed Id: 28562585. doi:10.1038/nature22800.
*glucagon receptor (GCGR), full length. XFEL structure: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.0 Å** synchrotron structure, 3.19 Å: 5XF1	5XEZ	Data File Jmol Viewer 5XEZ 5XF1	Zhang et al. (2017). Zhang H, Qiao A, Yang D, Yang L, Dai A, de Graaf C, Reedtz-Runge S, Dharmarajan V, Zhang H, Han GW, Grant TD, Sierra RG, Weierstall U, Nelson G, Liu W, Wu Y, Ma L, Cai X, Lin G, Wu X, Geng Z, Dong Y, Song G, Griffin PR, Lau J, Cherezov V, Yang H, Hanson MA, Stevens RC, Zhao Q, Jiang H, Wang MW, & Wu B (2017). Structure of the full-length glucagon class B G-protein-coupled receptor. Nature 546 :259-264. PubMed Id: 28514451. doi:10.1038/nature22363.
*Full-length glucagon receptor (GCGR) in complex with heterotrimeric G_S protein: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.3 Å** cryo-EM structure	6B3J	Data File Jmol Viewer 6B3J	Liang et al. (2018). Liang YL, Khoshouei M, Glukhova A, Furness SGB, Zhao P, Clydesdale L, Koole C, Truong TT, Thal DM, Lei S, Radjainia M, Danev R, Baumeister W, Wang MW, Miller LJ, Christopoulos A, Sexton PM, & Wootten D (2018). Phase-plate cryo-EM structure of a biased agonist-bound human GLP-1 receptor-Gs complex. Nature 555 :121-125. PubMed Id: 29466332. doi:10.1038/nature25773.
*glucagon receptor (GCGR), full length in complex with glucagon analog NNC1702: Homo sapiens* E Eukaryota (expressed in Sf9 cells), 3.0 Å** Engineered protein. T4 lysozyme fused into 2nd intracellular loop (ICL2). 45 residues were truncated at the C-terminus.	5YQZ	Data File Jmol Viewer 5YQZ	Zhang et al. (2018). Zhang H, Qiao A, Yang L, Van Eps N, Frederiksen KS, Yang D, Dai A, Cai X, Zhang H, Yi C, Cao C, He L, Yang H, Lau J, Ernst OP, Hanson MA, Stevens RC, Wang MW, Reedtz-Runge S, Jiang H, Zhao Q, & Wu B (2018). Structure of the glucagon receptor in complex with a glucagon analogue. Nature 553 :106-110. PubMed Id: 29300013. doi:10.1038/nature25153.
*glucagon receptor (GCGR) in complex with G_s: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.7 Å** cryo-EM structure in complex with G_i1, 3.9 Å: 6LML	6LMK	Data File Jmol Viewer 6LMK 6LML	Qiao et al. (2020). Qiao A, Han S, Li X, Li Z, Zhao P, Dai A, Chang R, Tai L, Tan Q, Chu X, Ma L, Thorsen TS, Reedtz-Runge S, Yang D, Wang MW, Sexton PM, Wootten D, Sun F, Zhao Q, & Wu B (2020). Structural basis of G_s and G_i recognition by the human glucagon receptor. Science 367 6484:1346-1352. PubMed Id: 32193322. doi:10.1126/science.aaz5346.
*Full-length glucagon receptor (GCGR) in complex with P15-GCGR-G_s: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.40 Å** cryo-EM structure	6WHC	Data File Jmol Viewer 6WHC	Chang et al. (2020). Chang R, Zhang X, Qiao A, Dai A, Belousoff MJ, Tan Q, Shao L, Zhong L, Lin G, Liang YL, Ma L, Han S, Yang D, Danev R, Wang MW, Wootten D, Wu B, & Sexton PM (2020). Cryo-electron microscopy structure of the glucagon receptor with a dual-agonist peptide. J Biol Chem 295 28:9313-9325. PubMed Id: 32371397. doi:10.1074/jbc.RA120.013793.
*Glucagon receptor-G_s complex bound to a designed glucagon derivative: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure	6WPW	Data File Jmol Viewer 6WPW	Hilger et al. (2020). Hilger D, Kumar KK, Hu H, Pedersen MF, O'Brien ES, Giehm L, Jennings C, Eskici G, Inoue A, Lerch M, Mathiesen JM, Skiniotis G, & Kobilka BK (2020). Structural insights into differences in G protein activation by family A and family B GPCRs. Science 369 6503:523. PubMed Id: 32732395. doi:10.1126/science.aba3373.
*Glucagon receptor (GCGR)-Gs complex with bound GIPR/GLP-1R/GCGR triagonist peptide 20: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.50 Å** cryo-EM structure	7V35	Data File Jmol Viewer 7V35	Zhao et al. (2022). Zhao F, Zhou Q, Cong Z, Hang K, Zou X, Zhang C, Chen Y, Dai A, Liang A, Ming Q, Wang M, Chen LN, Xu P, Chang R, Feng W, Xia T, Zhang Y, Wu B, Yang D, Zhao L, Xu HE, & Wang MW (2022). Structural insights into multiplexed pharmacological actions of tirzepatide and peptide 20 at the GIP, GLP-1 or glucagon receptors. Nat Commun 13 1:1057. PubMed Id: 35217653. doi:10.1038/s41467-022-28683-0.
*glucagon receptor (GCGR) - β-arrestin 1 complex, ligand-free state: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.50 Å** cryo-EM structure with bound glucagon, 3.30 Å: 8JRV	8JRU	Data File Jmol Viewer 8JRU 8JRV	Chen et al. (2023). Chen K, Zhang C, Lin S, Yan X, Cai H, Yi C, Ma L, Chu X, Liu Y, Zhu Y, Han S, Zhao Q, & Wu B (2023). Tail engagement of arrestin at the glucagon receptor. Nature 620 7975:904-910. PubMed Id: 37558880. doi:10.1038/s41586-023-06420-x.
*glucagon receptor (GCGR)- G_s complex, apo form: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.71 Å** cryo-EM structure	8WG8	Data File Jmol Viewer 8WG8	Cong et al. (2024). Cong Z, Zhao F, Li Y, Luo G, Mai Y, Chen X, Chen Y, Lin S, Cai X, Zhou Q, Yang D, & Wang MW (2024). Molecular features of the ligand-free GLP-1R, GCGR and GIPR in complex with Gs proteins. Cell Discov 10 1:18. PubMed Id: 38346960. doi:10.1038/s41421-024-00649-0.
*Activated glucagon-like receptor (GLP-1) in complex with a G protein: Oryctolagus cuniculus* E Eukaryota, 4.1 Å** cryo-EM structure	5VAI	Data File Jmol Viewer 5VAI	Zhang et al. (2017). Zhang Y, Sun B, Feng D, Hu H, Chu M, Qu Q, Tarrasch JT, Li S, Sun Kobilka T, Kobilka BK, & Skiniotis G (2017). Cryo-EM structure of the activated GLP-1 receptor in complex with a G protein. Nature 546 :248-253. PubMed Id: 28538729. doi:10.1038/nature22394.
*Glucagon-like peptide-1 receptor (GLP-1R) in complex with PF-06372222: Homo sapiens* E Eukaryota, 2.7 Å** in complex with NNC0640, 3.0 Å: 5VEX	5VEW	Data File Jmol Viewer 5VEW 5VEX	Song et al. (2017). Song G, Yang D, Wang Y, de Graaf C, Zhou Q, Jiang S, Liu K, Cai X, Dai A, Lin G, Liu D, Wu F, Wu Y, Zhao S, Ye L, Han GW, Lau J, Wu B, Hanson MA, Liu ZJ, Wang MW, & Stevens RC (2017). Human GLP-1 receptor transmembrane domain structure in complex with allosteric modulators. Nature 546 :312-315. PubMed Id: 28514449. doi:10.1038/nature22378.
*GLP-1 receptor membrane domain, thermostabilized (M10): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.8 Å** M8 (8 mutations), 2.8 Å: 6KK1 M6 (6 mutations), 3.1 Å: 6KK7	6KJV	Data File Jmol Viewer 6KJV 6KK7 6KK1	Xu et al. (2019). Xu Y, Wang Y, Wang Y, Liu K, Peng Y, Yao D, Tao H, Liu H, & Song G (2019). Mutagenesis facilitated crystallization of GLP-1R. IUCrJ 6 :996-1006. PubMed Id: 31709055. doi:10.1107/S2052252519013496.
*GLP-1 receptor in complex with TT-OAD2 non-peptide agonist: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3 Å** cryo-EM structure	6ORV	Data File Jmol Viewer 6ORV	Zhao et al. (2020). Zhao P, Liang YL, Belousoff MJ, Deganutti G, Fletcher MM, Willard FS, Bell MG, Christe ME, Sloop KW, Inoue A, Truong TT, Clydesdale L, Furness SGB, Christopoulos A, Wang MW, Miller LJ, Reynolds CA, Danev R, Sexton PM, & Wootten D (2020). Activation of the GLP-1 receptor by a non-peptidic agonist. Nature 577 7790:432-436. PubMed Id: 31915381. doi:10.1038/s41586-019-1902-z.
*Full-length GLP-1 receptor (GLP-1R) without orthosteric ligands: Homo sapiens* E Eukaryota (expressed in CHO-S cells), 3.2 Å** engineered protein, rubredoxin inserted into intracellular loop 2	6LN2	Data File Jmol Viewer 6LN2	Wu et al. (2020). Wu F, Yang L, Hang K, Laursen M, Wu L, Han GW, Ren Q, Roed NK, Lin G, Hanson MA, Jiang H, Wang MW, Reedtz-Runge S, Song G, & Stevens RC (2020). Full-length human GLP-1 receptor structure without orthosteric ligands. Nat Commun 11 1:1272. PubMed Id: 32152292. doi:10.1038/s41467-020-14934-5.
*GLP-1R-G_s complex with bound small-molecule agonist: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 4.20 Å** cryo-EM structure	7C2E	Data File Jmol Viewer 7C2E	Ma et al. (2020). Ma H, Huang W, Wang X, Zhao L, Jiang Y, Liu F, Guo W, Sun X, Zhong W, Yuan D, & Xu HE (2020). Structural insights into the activation of GLP-1R by a small molecule agonist. Cell Res . PubMed Id: 32724086. doi:10.1038/s41422-020-0384-8.
*GLP-1R-G_s complex with GLP-1 peptide and a positive allosteric modulator: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.30 Å** cryo-EM structure	6VCB	Data File Jmol Viewer 6VCB	Bueno et al. (2020). Bueno AB, Sun B, Willard FS, Feng D, Ho JD, Wainscott DB, Showalter AD, Vieth M, Chen Q, Stutsman C, Chau B, Ficorilli J, Agejas FJ, Cumming GR, Jiménez A, Rojo I, Kobilka TS, Kobilka BK, & Sloop KW (2020). Structural insights into probe-dependent positive allosterism of the GLP-1 receptor. Nat Chem Biol 16 10:1105-1110. PubMed Id: 32690941. doi:10.1038/s41589-020-0589-7.
*GLP-1 receptor in complex with GLP-1 peptide hormone: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.10 Å** cryo-EM structure with Non peptide agonist CHU-128, 2.10 Å: 6X19 with Non peptide agonist PF-06882961, 2.50 Å: 6X1A	6X18	Data File Jmol Viewer 6X18 6X1A 6X19	Zhang et al. (2020). Zhang X, Belousoff MJ, Zhao P, Kooistra AJ, Truong TT, Ang SY, Underwood CR, Egebjerg T, Šenel P, Stewart GD, Liang YL, Glukhova A, Venugopal H, Christopoulos A, Furness SGB, Miller LJ, Reedtz-Runge S, Langmead CJ, Gloriam DE, Danev R, Sexton PM, & Wootten D (2020). Differential GLP-1R Binding and Activation by Peptide and Non-peptide Agonists. Mol Cell 80 3:485-500.e7. PubMed Id: 33027691. doi:10.1016/j.molcel.2020.09.020.
*GLP-1 receptor in complex with LY3502970 nonpeptide agonist: Hom sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.10 Å** cryo-EM structure	6XOX	Data File Jmol Viewer 6XOX	Kawai et al. (2020). Kawai T, Sun B, Yoshino H, Feng D, Suzuki Y, Fukazawa M, Nagao S, Wainscott DB, Showalter AD, Droz BA, Kobilka TS, Coghlan MP, Willard FS, Kawabe Y, Kobilka BK, & Sloop KW (2020). Structural basis for GLP-1 receptor activation by LY3502970, an orally active nonpeptide agonist. Proc Natl Acad Sci U S A 117 47:29959-29967. PubMed Id: 33177239. doi:10.1073/pnas.2014879117.
*GLP-1 receptor-G_s complex with bound Semaglutide: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.50 Å** cryo-EM structure with bound Taspoglutide, 2.50 Å: 7KI1	7KI0	Data File Jmol Viewer 7KI0 7KI1	Zhang et al. (2021). Zhang X, Belousoff MJ, Liang YL, Danev R, Sexton PM, & Wootten D (2021). Structure and dynamics of semaglutide- and taspoglutide-bound GLP-1R-Gs complexes. Cell Rep 36 2. PubMed Id: 34260945. doi:10.1016/j.celrep.2021.109374.
*glucagon-like receptor (GLP-1)-G_s with bound PF 06882961; 200kV Glacios: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.24 Å** cryo-EM structure 300 kV Titan Krios, 3.82 Å 7LCJ	7LCK	Data File Jmol Viewer 7LCK 7LCJ	Zhang et al. (2021). Zhang X, Johnson RM, Drulyte I, Yu L, Kotecha A, Danev R, Wootten D, Sexton PM, & Belousoff MJ (2021). Evolving cryo-EM structural approaches for GPCR drug discovery. Structure 29 9:963-974.e6. PubMed Id: 33957078. doi:10.1016/j.str.2021.04.008.
*glucagon-like receptor (GLP-1)-G_s complex with bound compound 2: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.30 Å** cryo-EM structure with bound compound 2 and GLP-1, 2.50 Å: 7DUQ with bound compound 2, 2.50 Å: 7EVM with bound compound 2 and LY3502970, 2.90 Å: 7E14	7DUR	Data File Jmol Viewer 7DUR 7DUQ 7E14 7EVM	Cong et al. (2021). Cong Z, Chen LN, Ma H, Zhou Q, Zou X, Ye C, Dai A, Liu Q, Huang W, Sun X, Wang X, Xu P, Zhao L, Xia T, Zhong W, Yang D, Eric Xu H, Zhang Y, & Wang MW (2021). Molecular insights into ago-allosteric modulation of the human glucagon-like peptide-1 receptor. Nat Commun 12 1:3763. PubMed Id: 34145245. doi:10.1038/s41467-021-24058-z.
*GLP-1 receptor (GLP-1R) - G_s complex with bound Peptide-19: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.14 Å** cryo-EM structure	7RTB	Data File Jmol Viewer 7RTB	Johnson et al. (2021). Johnson RM, Zhang X, Piper SJ, Nettleton TJ, Vandekolk TH, Langmead CJ, Danev R, Sexton PM, & Wootten D (2021). Cryo-EM structure of the dual incretin receptor agonist, peptide-19, in complex with the glucagon-like peptide-1 receptor. Biochem Biophys Res Commun 578 :84-90. PubMed Id: 34547628. doi:10.1016/j.bbrc.2021.09.016.
*GLP-1R-G_s protein complex with bound oxyntomodulin: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.30 Å** cryo-EM structure with bound exendin-4, 3.70 Å 7LLL	7LLY	Data File Jmol Viewer 7LLY 7LLL	Deganutti et al. (2022). Deganutti G, Liang YL, Zhang X, Khoshouei M, Clydesdale L, Belousoff MJ, Venugopal H, Truong TT, Glukhova A, Keller AN, Gregory KJ, Leach K, Christopoulos A, Danev R, Reynolds CA, Zhao P, Sexton PM, & Wootten D (2022). Dynamics of GLP-1R peptide agonist engagement are correlated with kinetics of G protein activation. Nat Commun 13 1:92. PubMed Id: 35013280. doi:10.1038/s41467-021-27760-0.
*Glucagon-like peptide-1 receptor (GLP-1R)-G protein complex with bound Ex4-D-Ala, conformer 1: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.41 Å** cryo-EM structure conformer 2, 2.51 Å 7S3I	7S1M	Data File Jmol Viewer 7S1M 7S3I	Cary et al. (2022). Cary BP, Deganutti G, Zhao P, Truong TT, Piper SJ, Liu X, Belousoff MJ, Danev R, Sexton PM, Wootten D, & Gellman SH (2022). Structural and functional diversity among agonist-bound states of the GLP-1 receptor. Nat Chem Biol 18 3:256-263. PubMed Id: 34937906. doi:10.1038/s41589-021-00945-w.
*Glucagon-like peptide-1 receptor (GLP-1R)-G_s complex with bound tirzepatide (LY3298176): Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.40 Å** cryo-EM structure with bound non-acylated tirzepatide (LY3298176), 3.00 Å 7VBI with bound GIPR/GLP-1R/GCGR triagonist peptide 20, 3.00 Å 7VBH	7FIM	Data File Jmol Viewer 7FIM 7VBH 7VBI	Zhao et al. (2022). Zhao F, Zhou Q, Cong Z, Hang K, Zou X, Zhang C, Chen Y, Dai A, Liang A, Ming Q, Wang M, Chen LN, Xu P, Chang R, Feng W, Xia T, Zhang Y, Wu B, Yang D, Zhao L, Xu HE, & Wang MW (2022). Structural insights into multiplexed pharmacological actions of tirzepatide and peptide 20 at the GIP, GLP-1 or glucagon receptors. Nat Commun 13 1:1057. PubMed Id: 35217653. doi:10.1038/s41467-022-28683-0.
*Glucagon-like peptide-1 receptor (GLP-1R)-G_s complex with bound Boc5: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.61 Å** cryo-EM structure with bound WB4-24, 3.09 Å 7X8S	7X8R	Data File Jmol Viewer 7X8R 7X8S	Cong et al. (2022). Cong Z, Zhou Q, Li Y, Chen LN, Zhang ZC, Liang A, Liu Q, Wu X, Dai A, Xia T, Wu W, Zhang Y, Yang D, & Wang MW (2022). Structural basis of peptidomimetic agonism revealed by small- molecule GLP-1R agonists Boc5 and WB4-24. Proc Natl Acad Sci U S A 119 20:e2200155119. PubMed Id: 35561211. doi:10.1073/pnas.2200155119.
*Glucagon-like peptide-1 receptor (GLP-1R) in complex with PF-06882961: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.80 Å** cryo-EM structure	7S15	Data File Jmol Viewer 7S15	Griffith et al. (2022). Griffith DA, Edmonds DJ, Fortin JP, Kalgutkar AS, Kuzmiski JB, Loria PM, Saxena AR, Bagley SW, Buckeridge C, Curto JM, Derksen DR, Dias JM, Griffor MC, Han S, Jackson VM, Landis MS, Lettiere D, Limberakis C, Liu Y, Mathiowetz AM, Patel JC, Piotrowski DW, Price DA, Ruggeri RB, & Tess DA (2022). A Small-Molecule Oral Agonist of the Human Glucagon-like Peptide-1 Receptor. J Med Chem 65 12:8208-8226. PubMed Id: 35647711. doi:10.1021/acs.jmedchem.1c01856.
*Glucagon-like peptide-1 receptor (GLP-1R)-G_s complex, apo form: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.54 Å** cryo-EM structure	8WG7	Data File Jmol Viewer 8WG7	Cong et al. (2024). Cong Z, Zhao F, Li Y, Luo G, Mai Y, Chen X, Chen Y, Lin S, Cai X, Zhou Q, Yang D, & Wang MW (2024). Molecular features of the ligand-free GLP-1R, GCGR and GIPR in complex with Gs proteins. Cell Discov 10 1:18. PubMed Id: 38346960. doi:10.1038/s41421-024-00649-0.
*GLP-2R-G_s complex with GLP-2 peptide: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å** cryo-EM structure	7D68	Data File Jmol Viewer 7D68	Sun et al. (2020). Sun W, Chen LN, Zhou Q, Zhao LH, Yang D, Zhang H, Cong Z, Shen DD, Zhao F, Zhou F, Cai X, Chen Y, Zhou Y, Gadgaard S, van der Velden WJC, Zhao S, Jiang Y, Rosenkilde MM, Xu HE, Zhang Y, & Wang MW (2020). A unique hormonal recognition feature of the human glucagon-like peptide-2 receptor. Cell Res 30 12:1098-1108. PubMed Id: 33239759. doi:10.1038/s41422-020-00442-0.
*GIPR glucose-dependent insulinotropic polypeptide receptor: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.98 Å** Cryo-EM structure	7DTY	Data File Jmol Viewer 7DTY	Zhao et al. (2021). Zhao F, Zhang C, Zhou Q, Hang K, Zou X, Chen Y, Wu F, Rao Q, Dai A, Yin W, Shen DD, Zhang Y, Xia T, Stevens RC, Xu HE, Yang D, Zhao L, & Wang MW (2021). Structural insights into hormone recognition by the human glucose-dependent insulinotropic polypeptide receptor. Elife 10 :e68719. PubMed Id: 34254582. doi:10.7554/eLife.68719.
*GIPR glucose-dependent insulinotropic polypeptide receptor-G_s complex with bound tirzepatide: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.40 Å** cryo-EM structure with bound non-acylated tirzepatide (LY3298176), 3.20 Å 7VAB with bound GIPR/GLP-1R/GCGR triagonist peptide 20, 3.10 Å 7FIN	7FIY	Data File Jmol Viewer 7FIY 7VAB 7FIN	Zhao et al. (2022). Zhao F, Zhou Q, Cong Z, Hang K, Zou X, Zhang C, Chen Y, Dai A, Liang A, Ming Q, Wang M, Chen LN, Xu P, Chang R, Feng W, Xia T, Zhang Y, Wu B, Yang D, Zhao L, Xu HE, & Wang MW (2022). Structural insights into multiplexed pharmacological actions of tirzepatide and peptide 20 at the GIP, GLP-1 or glucagon receptors. Nat Commun 13 1:1057. PubMed Id: 35217653. doi:10.1038/s41467-022-28683-0.
*GIPR glucose-dependent insulinotropic polypeptide receptor - G_s complex, splice variant 1 (SV1): Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.23 Å** cryo-EM structure splice variant 2 (SV2), 3.13 Å: 8ITM	8ITL	Data File Jmol Viewer 8ITL 8ITM	Zhao et al. (2023). Zhao F, Hang K, Zhou Q, Shao L, Li H, Li W, Lin S, Dai A, Cai X, Liu Y, Xu Y, Feng W, Yang D, & Wang MW (2023). Molecular basis of signal transduction mediated by the human GIPR splice variants. Proc Natl Acad Sci U S A 120 41:e2306145120. PubMed Id: 37792509. doi:10.1073/pnas.2306145120.
*GIPR glucose-dependent insulinotropic polypeptide receptor-G_s complex, apo form: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.86 Å** cryo-EM structure	8WA3	Data File Jmol Viewer 8WA3	Cong et al. (2024). Cong Z, Zhao F, Li Y, Luo G, Mai Y, Chen X, Chen Y, Lin S, Cai X, Zhou Q, Yang D, & Wang MW (2024). Molecular features of the ligand-free GLP-1R, GCGR and GIPR in complex with Gs proteins. Cell Discov 10 1:18. PubMed Id: 38346960. doi:10.1038/s41421-024-00649-0.
*Calcitonin receptor-heterotrimeric G_s protein complex: Homo sapiens* E Eukaryota, 4.1 Å** Phase-plate cryo-EM structure.	5UZ7	Data File Jmol Viewer 5UZ7	Liang et al. (2017). Liang YL, Khoshouei M, Radjainia M, Zhang Y, Glukhova A, Tarrasch J, Thal DM, Furness SGB, Christopoulos G, Coudrat T, Danev R, Baumeister W, Miller LJ, Christopoulos A, Kobilka BK, Wootten D, Skiniotis G, & Sexton PM (2017). Phase-plate cryo-EM structure of a class B GPCR-G-protein complex. Nature 546 7656:118-123. PubMed Id: 28437792. doi:10.1038/nature22327.
*Calcitonin receptor-heterotrimeric G_s bound to endogenous peptide and canonical transducer: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.3 Å** Volta phase-plate cryo-EM structure	6E3Y	Data File Jmol Viewer 6E3Y	Liang et al. (2018). Liang YL, Khoshouei M, Deganutti G, Glukhova A, Koole C, Peat TS, Radjainia M, Plitzko JM, Baumeister W, Miller LJ, Hay DL, Christopoulos A, Reynolds CA, Wootten D, & Sexton PM (2018). Cryo-EM structure of the active, Gs-protein complexed, human CGRP receptor. Nature 561 7724:492-497. PubMed Id: 30209400. doi:10.1038/s41586-018-0535-y.
*Calcitonin receptor-heterotrimeric G_s protein complex: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.34 Å** cryo-EM structure	6NIY	Data File Jmol Viewer 6NIY	Dal Maso et al. (2019). Dal Maso E, Glukhova A, Zhu Y, Garcia-Nafria J, Tate CG, Atanasio S, Reynolds CA, Ramírez-Aportela E, Carazo JM, Hick CA, Furness SGB, Hay DL, Liang YL, Miller LJ, Christopoulos A, Wang MW, Wootten D, & Sexton PM (2019). The Molecular Control of Calcitonin Receptor Signaling. ACS Pharmacol Transl Sci 2 1:31-51. PubMed Id: 32219215. doi:10.1021/acsptsci.8b00056.
*Calcitonin gene-related peptide receptor (GPCR), apo form: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.15 Å** cryo-EM structure with bound CGRP peptide, 3.49 Å: 7KNU	7KNT	Data File Jmol Viewer 7KNT 7KNU	Josephs et al. (2021). Josephs TM, Belousoff MJ, Liang YL, Piper SJ, Cao J, Garama DJ, Leach K, Gregory KJ, Christopoulos A, Hay DL, Danev R, Wootten D, & Sexton PM (2021). Structure and dynamics of the CGRP receptor in apo and peptide-bound forms. Science 372 6538:eabf7258. PubMed Id: 33602864. doi:10.1126/science.abf7258.
*Amylin1 Receptor in complex with G_s and rat amylin peptide: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.20 Å** cryo-EM structure Amylin2 Receptor in complex with G_sand human calcitonin peptide, 3.30 Å: 7TYH Calcitonin Receptor in complex with G_s and rat amylin peptide, CT-like state, 3.30 Å: 7TYI Calcitonin Receptor in complex with G_s and rat amylin peptide, bypass motif, 3.30 Å: 7TYL Calcitonin Receptor in complex with G_s and salmon calcitonin peptide, 2.60 Å: 7TYN Calcitonin receptor in complex with G_s and human calcitonin peptide, 2.70 Å: 7TYO Amylin1 Receptor in complex with G_s and salmon calcitonin peptide, 3.00 Å: 7TYW Amylin2 Receptor in complex with G_s and rat amylin peptide, 2.55 Å: 7TYX Human Amylin2 Receptor in complex with G_s and salmon calcitonin peptide, 3.00 Å: 7TYY Human Amylin3 Receptor in complex with G_s and rat amylin peptide, 2.40 Å: 7TZF	7TYF	Data File Jmol Viewer 7TYF 7TYY 7TYN 7TYW 7TYH 7TYX 7TYL 7TZF 7TYI 7TYO	Cao et al. (2022). Cao J, Belousoff MJ, Liang YL, Johnson RM, Josephs TM, Fletcher MM, Christopoulos A, Hay DL, Danev R, Wootten D, & Sexton PM (2022). A structural basis for amylin receptor phenotype. Science 375 6587:eabm9609. PubMed Id: 35324283. doi:10.1126/science.abm9609.
*parathyroid hormone receptor-1 (PTH1R) in complex with a parathyroid hormone analog and G protein, state 1: Homo sapiens* E Eukaryota, 3 Å** cryo-EM structure conformation state 2, 3.5 Å: 6NBH conformation state 3, 4 Å: 6NBI	6NBF	Data File Jmol Viewer 6NBF 6NBI 6NBH	Zhao et al. (2019). Zhao LH, Ma S, Sutkeviciute I, Shen DD, Zhou XE, de Waal PW, Li CY, Kang Y, Clark LJ, Jean-Alphonse FG, White AD, Yang D, Dai A, Cai X, Chen J, Li C, Jiang Y, Watanabe T, Gardella TJ, Melcher K, Wang MW, Vilardaga JP, Xu HE, & Zhang Y (2019). Structure and dynamics of the active human parathyroid hormone receptor-1. Science 364 6436:148-153. PubMed Id: 30975883. doi:10.1126/science.aav7942.
*parathyroid hormone receptor-1 (PTH1R) in complex with a peptide agonist: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.50 Å**	6FJ3	Data File Jmol Viewer 6FJ3	Ehrenmann et al. (2018). Ehrenmann J, Schöppe J, Klenk C, Rappas M, Kummer L, Doré AS, & Plückthun A (2018). High-resolution crystal structure of parathyroid hormone 1 receptor in complex with a peptide agonist. Nat Struct Mol Biol 25 12:1086-1092. PubMed Id: 30455434. doi:10.1038/s41594-018-0151-4.
*parathyroid hormone receptor-1 (PTH1R) - G_s complex with bound intracellular biased agonist PCO371: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure	8GW8	Data File Jmol Viewer 8GW8	Kobayashi et al. (2023). Kobayashi K, Kawakami K, Kusakizako T, Tomita A, Nishimura M, Sawada K, Okamoto HH, Hiratsuka S, Nakamura G, Kuwabara R, Noda H, Muramatsu H, Shimizu M, Taguchi T, Inoue A, Murata T, & Nureki O (2023). Class B1 GPCR activation by an intracellular agonist. Nature 618 7967:1085-1093. PubMed Id: 37286611. doi:10.1038/s41586-023-06169-3.
*parathyroid hormone receptor-1 (PTH1R)—G_s complex with bound Abaloparatide: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure with bound teriparatide, 2.80 Å: 7Y36	7Y35	Data File Jmol Viewer 7Y35 7Y36	Zhai et al. (2022). Zhai X, Mao C, Shen Q, Zang S, Shen DD, Zhang H, Chen Z, Wang G, Zhang C, Zhang Y, & Liu Z (2022). Molecular insights into the distinct signaling duration for the peptide-induced PTH1R activation. Nat Commun 13 1:6276. PubMed Id: 36271004. doi:10.1038/s41467-022-34009-x.
*parathyroid hormone receptor-2 (PTH2R) in complex with a tuberoinfundibular peptide of 39 residues and G protein: Homo sapiens* E Eukaryota (expressed in richoplusia ni), 2.80 Å** cryo-EM structure	7F16	Data File Jmol Viewer 7F16	Wang et al. (2021). Wang X, Cheng X, Zhao L, Wang Y, Ye C, Zou X, Dai A, Cong Z, Chen J, Zhou Q, Xia T, Jiang H, Xu HE, Yang D, & Wang MW (2021). Molecular insights into differentiated ligand recognition of the human parathyroid hormone receptor 2. Proc Natl Acad Sci U S A 118 32:e2101279118. PubMed Id: 34353904. doi:10.1073/pnas.2101279118.
*Adrenomedullin 1 (AM1) receptor G protein complex with adrenomedullin peptide: Homo sapiens* E Eukaryota, 3.00 Å** cryo-EM structure	6UUN	Data File Jmol Viewer 6UUN	Liang et al. (2020). Liang YL, Belousoff MJ, Fletcher MM, Zhang X, Khoshouei M, Deganutti G, Koole C, Furness SGB, Miller LJ, Hay DL, Christopoulos A, Reynolds CA, Danev R, Wootten D, & Sexton PM (2020). Structure and Dynamics of Adrenomedullin Receptors AM1 and AM2 Reveal Key Mechanisms in the Control of Receptor Phenotype by Receptor Activity-Modifying Proteins. ACS Pharmacol Transl Sci 3 2:263-284. PubMed Id: 32296767. doi:10.1021/acsptsci.9b00080.
*Adrenomedullin 2 (AM2) receptor G protein complex with adrenomedullin peptide: Homo sapiens* E Eukaryota, 2.40 Å** cryo-EM structure active Adrenomedullin 2 receptor G protein complex with adrenomedullin 2 peptide, 6UVA	6UUS	Data File Jmol Viewer 6UUS 6UVA	Liang et al. (2020). Liang YL, Belousoff MJ, Fletcher MM, Zhang X, Khoshouei M, Deganutti G, Koole C, Furness SGB, Miller LJ, Hay DL, Christopoulos A, Reynolds CA, Danev R, Wootten D, & Sexton PM (2020). Structure and Dynamics of Adrenomedullin Receptors AM1 and AM2 Reveal Key Mechanisms in the Control of Receptor Phenotype by Receptor Activity-Modifying Proteins. ACS Pharmacol Transl Sci 3 2:263-284. PubMed Id: 32296767. doi:10.1021/acsptsci.9b00080.
*secretin receptor (SecR) in complex with G_s: Homo Sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.30 Å** cryo-EM structure low resolution structure, 4.30 Å: 6WI9	6WZG	Data File Jmol Viewer 6WZG 6WI9	Dong et al. (2020). Dong M, Deganutti G, Piper SJ, Liang YL, Khoshouei M, Belousoff MJ, Harikumar KG, Reynolds CA, Glukhova A, Furness SGB, Christopoulos A, Danev R, Wootten D, Sexton PM, & Miller LJ (2020). Structure and dynamics of the active Gs-coupled human secretin receptor. Nat Commun 11 1:4137. PubMed Id: 32811827. doi:10.1038/s41467-020-17791-4.
*secretin receptor (SecR) in complex with engineered G_s: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure	7D3S	Data File Jmol Viewer 7D3S	Fukuhara et al. (2020). Fukuhara S, Kobayashi K, Kusakizako T, Iida W, Kato M, Shihoya W, & Nureki O (2020). Structure of the human secretin receptor coupled to an engineered heterotrimeric G protein. Biochem Biophys Res Commun 533 4:861-866. PubMed Id: 33008599. doi:10.1016/j.bbrc.2020.08.042.
*Vasoactive intestinal polypeptide 1 (VIP1) receptor-G protein complex (activated): Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** cryo-EM structure	6VN7	Data File Jmol Viewer 6VN7	Duan et al. (2020). Duan J, Shen DD, Zhou XE, Bi P, Liu QF, Tan YX, Zhuang YW, Zhang HB, Xu PY, Huang SJ, Ma SS, He XH, Melcher K, Zhang Y, Xu HE, & Jiang Y (2020). Cryo-EM structure of an activated VIP1 receptor-G protein complex revealed by a NanoBiT tethering strategy. Nat Commun 11 1:4121. PubMed Id: 32807782. doi:10.1038/s41467-020-17933-8.
*Vasoactive intestinal polypeptide 1 (VIP1) receptor-G_s complex with bound PACAP27: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 2.30 Å** cryo-EM structure PAC1R-PACAP27-G_s complex, 2.30 Å: 8E3X VPAC1R-VIP-G_s complex, 2.70 Å: 8E3Z	8E3Y	Data File Jmol Viewer 8E3Y 8E3X 8E3Z	Piper et al. (2022). Piper SJ, Deganutti G, Lu J, Zhao P, Liang YL, Lu Y, Fletcher MM, Hossain MA, Christopoulos A, Reynolds CA, Danev R, Sexton PM, & Wootten D (2022). Understanding VPAC receptor family peptide binding and selectivity. Nat Commun 13 1:7013. PubMed Id: 36385145. doi:10.1038/s41467-022-34629-3.
*Vasoactive intestinal polypeptide 2 (VIP2) receptor-G_s complex with bound PACAP27: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.74 Å** cryo-EM structure 23 residues were truncated at the N-terminus of the VIP2 receptor. 3.42 Å 7WBJ	7VQX	Data File Jmol Viewer 7VQX 7WBJ	Xu et al. (2022). Xu Y, Feng W, Zhou Q, Liang A, Li J, Dai A, Zhao F, Yan J, Chen CW, Li H, Zhao LH, Xia T, Jiang Y, Xu HE, Yang D, & Wang MW (2022). A distinctive ligand recognition mechanism by the human vasoactive intestinal polypeptide receptor 2. Nat Commun 13 1:2272. PubMed Id: 35477937. doi:10.1038/s41467-022-30041-z.
*growth hormone-releasing hormone receptor-G_s protein complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.60 Å** cryo-EM structure	7CZ5	Data File Jmol Viewer 7CZ5	Zhou et al. (2020). Zhou F, Zhang H, Cong Z, Zhao LH, Zhou Q, Mao C, Cheng X, Shen DD, Cai X, Ma C, Wang Y, Dai A, Zhou Y, Sun W, Zhao F, Zhao S, Jiang H, Jiang Y, Yang D, Eric Xu H, Zhang Y, & Wang MW (2020). Structural basis for activation of the growth hormone-releasing hormone receptor. Nat Commun 11 1:5205. PubMed Id: 33060564. doi:10.1038/s41467-020-18945-0.
G Protein-Coupled Receptors: Class B2
*Adhesion receptor GPR133 (ADGRD1)-miniG_s complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.80 Å** cryo-EM structure	7WU2	Data File Jmol Viewer 7WU2	Qu et al. (2022). Qu X, Qiu N, Wang M, Zhang B, Du J, Zhong Z, Xu W, Chu X, Ma L, Yi C, Han S, Shui W, Zhao Q, & Wu B (2022). Structural basis of tethered agonism of the adhesion GPCRs ADGRD1 and ADGRF1. Nature 604 7907:779-785. PubMed Id: 35418679. doi:10.1038/s41586-022-04580-w.
*Adhesion receptor GPR110 (ADGRF1)-miniG_s complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.10 Å** cryo-EM structure miniG_i complex, 3.40 Å: 7WU4 miniG_i complex, H565A/T567A mutant, 3.00 Å: 7WU5	7WU3	Data File Jmol Viewer 7WU3 7WU5 7WU4	Qu et al. (2022). Qu X, Qiu N, Wang M, Zhang B, Du J, Zhong Z, Xu W, Chu X, Ma L, Yi C, Han S, Shui W, Zhao Q, & Wu B (2022). Structural basis of tethered agonism of the adhesion GPCRs ADGRD1 and ADGRF1. Nature 604 7907:779-785. PubMed Id: 35418679. doi:10.1038/s41586-022-04580-w.
*Adhesion receptor GPR110 (ADGRF1) - G_q complex: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.85 Å** cryo-EM structure G_s complex, 2.84 Å: 7WXW G_i complex, 3.09 Å: 7X2V G₁₂ complex, 2.83 Å: 7WZ7 C₁₃ complex, 2.83 Å: 7WY0	7WXU	Data File Jmol Viewer 7WXU 7WZ7 7WXW 7X2V 7WY0	Zhu et al. (2022). Zhu X, Qian Y, Li X, Xu Z, Xia R, Wang N, Liang J, Yin H, Zhang A, Guo C, Wang G, & He Y (2022). Structural basis of adhesion GPCR GPR110 activation by stalk peptide and G-proteins coupling. Nat Commun 13 1:5513. PubMed Id: 36127364. doi:10.1038/s41467-022-33173-4.
*Adhesion receptor GPR56 (ADGRG1)-miniG₁₃ complex with bound tethered agonist: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.70 Å** cryo-EM structure	7SF8	Data File Jmol Viewer 7SF8	Barros-Álvarez et al. (2022). Barros-Álvarez X, Nwokonko RM, Vizurraga A, Matzov D, He F, Papasergi-Scott MM, Robertson MJ, Panova O, Yardeni EH, Seven AB, Kwarcinski FE, Su H, Peroto MC, Meyerowitz JG, Shalev-Benami M, Tall GG, & Skiniotis G (2022). The tethered peptide activation mechanism of adhesion GPCRs. Nature 604 7907:757-762. PubMed Id: 35418682. doi:10.1038/s41586-022-04575-7.
*Adhesion receptor GPR97 (ADGRG3)-G_o complex with bound beclomethasone: Homo sapiens* E Eukaryota, 3.10 Å** cryo-EM structure with bound cortisol, 2.90 Å: 7D77	7D76	Data File Jmol Viewer 7D76 7D77	Ping et al. (2021). Ping YQ, Mao C, Xiao P, Zhao RJ, Jiang Y, Yang Z, An WT, Shen DD, Yang F, Zhang H, Qu C, Shen Q, Tian C, Li ZJ, Li S, Wang GY, Tao X, Wen X, Zhong YN, Yang J, Yi F, Yu X, Xu HE, Zhang Y, & Sun JP (2021). Structures of the glucocorticoid-bound adhesion receptor GPR97-G_o complex. Nature 589 7843:620-626. PubMed Id: 33408414. doi:10.1038/s41586-020-03083-w.
*Adhesion receptor LPHN3 (ADGRL3)-miniG₁₃ complex with bound tethered agonist: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.90 Å** cryo-EM structure	7SF7	Data File Jmol Viewer 7SF7	Barros-Álvarez et al. (2022). Barros-Álvarez X, Nwokonko RM, Vizurraga A, Matzov D, He F, Papasergi-Scott MM, Robertson MJ, Panova O, Yardeni EH, Seven AB, Kwarcinski FE, Su H, Peroto MC, Meyerowitz JG, Shalev-Benami M, Tall GG, & Skiniotis G (2022). The tethered peptide activation mechanism of adhesion GPCRs. Nature 604 7907:757-762. PubMed Id: 35418682. doi:10.1038/s41586-022-04575-7.
*Adhesion receptor LPHN3 (ADGRL3)-G_q complex: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.83 Å** cryo-EM structure G_s complex, 2.83 Å: 7WY8 G_i complex, 2.97 Å: 7WYB G₁₂ complex, 2.93 Å: 7X10	7WY5	Data File Jmol Viewer 7WY5 7WY8 7X10 7WYB	Qian et al. (2022). Qian Y, Ma Z, Liu C, Li X, Zhu X, Wang N, Xu Z, Xia R, Liang J, Duan Y, Yin H, Xiong Y, Zhang A, Guo C, Chen Z, Huang Z, & He Y (2022). Structural insights into adhesion GPCR ADGRL3 activation and G_q, G_s, G_i, and G₁₂ coupling. Mol Cell 82 22:4340-4352.e6. PubMed Id: 36309016. doi:10.1016/j.molcel.2022.10.009.
*Adhesion receptor LPHN3 (ADGRL3) - modified BRIL (mBRIL) construct: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	8JMT	Data File Jmol Viewer 8JMT	Guo et al. (2024). Guo Q, He B, Zhong Y, Jiao H, Ren Y, Wang Q, Ge Q, Gao Y, Liu X, Du Y, Hu H, & Tao Y (2024). A method for structure determination of GPCRs in various states. Nat Chem Biol 20 1:74-82. PubMed Id: 37580554. doi:10.1038/s41589-023-01389-0.
G Protein-Coupled Receptors: Class C
*GABA_B receptor ectodomain GBR1-GBR2 heterodimer, apo form: Homo sapiens* E Eukaryota, 2.35 Å** with bound antagonist 2-hydroxysaclofen, 2.22 Å: 4MQF with bound antagonist CGP54626, 2.15 Å: 4MR7 with bound antagonist CGP35348, 2.15 Å: 4MR8 with bound antagonist SCH50911, 2.35 Å:4MR9 with bound antagonist phaclofen, 2.86 Å: 4MRM with bound antagonist CGP46381, 2.25 Å: 4MS1 with bound endogenous agonist GABA, 2.50 Å: 4MS3 with bound agonist baclofen, 1.90 Å: 4MS4	4MQE	Data File Jmol Viewer 4MQE 4MR7 4MS4 4MR9 4MR8 4MRM 4MQF 4MS1 4MS3	Geng et al. (2013). Geng Y, Bush M, Mosyak L, Wang F, & Fan QR (2013). Structural mechanism of ligand activation in human GABA_B receptor. Nature 504 :254-259. PubMed Id: 24305054. doi:10.1038/nature12725.
*GABA_B receptor KCTD16 oligomerization domain in complex with part of GABA_B2 receptor: Homo sapiens* E Eukaryota (expressed in E. coli), 2.35 Å** KCTD16 T1 domain (form II crystal), 2.8 Å: 6OCT KCTD16 T1 domain (form I crystal), 2.28 Å: 6OCR	6OCP	Data File Jmol Viewer 6OCP 6OCT 6OCR	Zuo et al. (2019). Zuo H, Glaaser I, Zhao Y, Kurinov I, Mosyak L, Wang H, Liu J, Park J, Frangaj A, Sturchler E, Zhou M, McDonald P, Geng Y, Slesinger PA, & Fan QR (2019). Structural basis for auxiliary subunit KCTD16 regulation of the GABA_B receptor. Proc Natl Acad Sci USA 116 17:8370-8379. PubMed Id: 30971491. doi:10.1073/pnas.1903024116.
*GABA_B receptor, baclofen/BHFF-bound in the active state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure CGP54626-bound in inactive state, 2.90 Å: 7C7S	7C7Q	Data File Jmol Viewer 7C7Q 7C7S	Mao et al. (2020). Mao C, Shen C, Li C, Shen DD, Xu C, Zhang S, Zhou R, Shen Q, Chen LN, Jiang Z, Liu J, & Zhang Y (2020). Cryo-EM structures of inactive and active GABA_B receptor. Cell Res 30 7:564-573. PubMed Id: 32494023. doi:10.1038/s41422-020-0350-5.
*GABA_B heterodimeric receptor in an inactive state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	6WIV	Data File Jmol Viewer 6WIV	Park et al. (2020). Park J, Fu Z, Frangaj A, Liu J, Mosyak L, Shen T, Slavkovich VN, Ray KM, Taura J, Cao B, Geng Y, Zuo H, Kou Y, Grassucci R, Chen S, Liu Z, Lin X, Williams JP, Rice WJ, Eng ET, Huang RK, Soni RK, Kloss B, Yu Z, Javitch JA, Hendrickson WA, Slesinger PA, Quick M, Graziano J, Yu H, Fiehn O, Clarke OB, Frank J, & Fan QR (2020). Structure of human GABAB receptor in an inactive state. Nature 584 7820:304-309. PubMed Id: 32581365. doi:10.1038/s41586-020-2452-0.
*GABA_B1 homodimeric receptor in an inactive state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure inactive GABA_B heterodimer, 3.60 Å: 6W2X	6W2Y	Data File Jmol Viewer 6W2Y 6W2X	Papasergi-Scott et al. (2020). Papasergi-Scott MM, Robertson MJ, Seven AB, Panova O, Mathiesen JM, & Skiniotis G (2020). Structures of metabotropic GABA_B receptor. Nature 584 7820:310-314. PubMed Id: 32580208. doi:10.1038/s41586-020-2469-4.
*GABA_B heterodimeric receptor with bound agonist SKF97541 and positive allosteric modulator GS39783: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.63 Å** cryo-EM structure bound to agonist SKF97541 in its intermediate state 2, 4.80 Å: 6UO9 intermediate state 1, 6.30 Å: 6UOA apo state, 3.97 Å: 6JVM	6UO8	Data File Jmol Viewer 6UO8 6JVM 6UOA 6UO9	Shaye et al. (2020). Shaye H, Ishchenko A, Lam JH, Han GW, Xue L, Rondard P, Pin JP, Katritch V, Gati C, & Cherezov V (2020). Structural basis of the activation of a metabotropic GABA receptor. Nature 584 7820:298-303. PubMed Id: 32555460. doi:10.1038/s41586-020-2408-4.
*GABA_B receptor bound to the positive allosteric modulator rac-BHFF: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.50 Å** cryo-EM structure receptor in apo state, 7.60 Å: 7CA5 bound to the antagonist CGP54626, 3.52 Å: 7CUM	7CA3	Data File Jmol Viewer 7CA3 7CA5 7CUM	Kim et al. (2020). Kim Y, Jeong E, Jeong JH, Kim Y, & Cho Y (2020). Structural Basis for Activation of the Heterodimeric GABA_B Receptor. J Mol Biol 432 22:5966-5984. PubMed Id: 33058878. doi:10.1016/j.jmb.2020.09.023.
*GABA_B receptor-G_i complex: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.50 Å** cryo-EM structure	7EB2	Data File Jmol Viewer 7EB2	Shen et al. (2021). Shen C, Mao C, Xu C, Jin N, Zhang H, Shen DD, Shen Q, Wang X, Hou T, Chen Z, Rondard P, Pin JP, Zhang Y, & Liu J (2021). Structural basis of GABA_B receptor-G_i protein coupling. Nature 594 7864:594-598. PubMed Id: 33911284. doi:10.1038/s41586-021-03507-1.
*Metabotropic Glutamate Receptor 1 (mGlu₁) with bound allosteric modulator: Homo sapiens* E Eukaryota, 2.80 Å** Engineered Protein: E. coli apocytochrome b562 RIL (BRIL) fused at N-terminal at I581. C-terminus truncated at residue V860.	4OR2	Data File Jmol Viewer 4OR2	Wu et al. (2014). Wu H, Wang C, Gregory KJ, Han GW, Cho HP, Xia Y, Niswender CM, Katritch V, Meiler J, Cherezov V, Conn PJ, & Stevens RC (2014). Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator. Science 344 :58-64. PubMed Id: 24603153. doi:10.1126/science.1249489.
*Metabotropic Glutamate Receptor 1 (mGlu₁), apo state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.96 Å** cryo-EM structure intermediate state, 3.65 Å, 7DGE	7DGD	Data File Jmol Viewer 7DGD 7DGE	Zhang et al. (2021). Zhang J, Qu L, Wu L, Tang X, Luo F, Xu W, Xu Y, Liu ZJ, & Hua T (2021). Structural insights into the activation initiation of full-length mGlu1. Protein Cell 12 8:662-667. PubMed Id: 33278019. doi:10.1007/s13238-020-00808-5.
*Metabotropic Glutamate Receptor 2 (mGlu₂) with bound G_i: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.50 Å** cryo-EM structure	7E9G	Data File Jmol Viewer 7E9G	Lin et al. (2021). Lin S, Han S, Cai X, Tan Q, Zhou K, Wang D, Wang X, Du J, Yi C, Chu X, Dai A, Zhou Y, Chen Y, Zhou Y, Liu H, Liu J, Yang D, Wang MW, Zhao Q, & Wu B (2021). Structures of Gi-bound metabotropic glutamate receptors mGlu2 and mGlu4. Nature 594 :583-588. PubMed Id: 34135510. doi:10.1038/s41586-021-03495-2.
*Metabotropic Glutamate Receptor 2 (mGlu₂) in inactive-State Bound to Antagonist LY341495: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.65 Å** cryo-Em structure bound to Ago-PAM ADX55164 and Glutamate, 3.30 Å: 7MTR mGlu2-G_i complex, 3.20 Å: 7MTS	7MTQ	Data File Jmol Viewer 7MTQ 7MTR 7MTS	Seven et al. (2021). Seven AB, Barros-Álvarez X, de Lapeyrièe M, Papasergi-Scott MM, Robertson MJ, Zhang C, Nwokonko RM, Gao Y, Meyerowitz JG, Rocher JP, Schelshorn D, Kobilka BK, Mathiesen JM, & Skiniotis G (2021). G-protein activation by a metabotropic glutamate receptor. Nature 595 7867:450-454. PubMed Id: 34194039. doi:10.1038/s41586-021-03680-3.
*Metabotropic Glutamate Receptor 2 (mGlu2) homodimer: Homo sapiens* E Eukaryota (expressed in mammal environmental sample), 3.60 Å** cryo-EM structure mGlu2 homodimer with bound LY354740, 3.10 Å: 7EPB mGlu2-mGlu7 heterodimer (inactive), 3.90 Å: 7EPD mGlu2 bound to NAM597, 2.50 Å: 7EPE mGlu2 bound to NAM597, 2.70 Å: 7EPF	7EPA	Data File Jmol Viewer 7EPA 7EPF 7EPB 7EPE 7EPD	Du et al. (2021). Du J, Wang D, Fan H, Xu C, Tai L, Lin S, Han S, Tan Q, Wang X, Xu T, Zhang H, Chu X, Yi C, Liu P, Wang X, Zhou Y, Pin JP, Rondard P, Liu H, Liu J, Sun F, Wu B, & Zhao Q (2021). Structures of human mGlu2 and mGlu7 homo- and heterodimers. Nature 594 7864:589-593. PubMed Id: 34135509. doi:10.1038/s41586-021-03641-w.
*mGlu₂ - mGlu₃ heterodimer with bound LY341495, dimerization mode I: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.80 Å** cryo-EM structure dimerization mode II, 3.40 Å: 8JCV in presence of LY341495 and NAM563, 3.00 Å: 8JCW in presence of LY341495 and NAM563, dimerization mode II, 3.00 Å: 8JCX in presence of LY341495, NAM563, and LY2389575, 2.90 Å: 8JCY in presence of LY341495, NAM563, and LY2389575, dimerization mode III, 3.00 Å: 8JCZ in presence of NAM563, 3.30 Å: 8JD0 Rco state, 3.70 Å: 8JD1 with bound G_i1, 3.30 Å: 8JD3 G protein-free, Acc state, 2.80 Å: 8JD2	8JCU	Data File Jmol Viewer 8JCU 8JCV 8JCX 8JCZ 8JD2 8JCW 8JCY 8JD3 8JD1 8JD0	Wang et al. (2023). Wang X, Wang M, Xu T, Feng Y, Shao Q, Han S, Chu X, Xu Y, Lin S, Zhao Q, & Wu B (2023). Structural insights into dimerization and activation of the mGlu2-mGlu3 and mGlu2-mGlu4 heterodimers. Cell Res 33 10:762-774. PubMed Id: 37286794. doi:10.1038/s41422-023-00830-2.
*mGlu₂ - mGlu₄ heterodimer, G-protein free: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure with bound G_i1 3.60 Å: 8JD5	8JD4	Data File Jmol Viewer 8JD4 8JD5	Wang et al. (2023). Wang X, Wang M, Xu T, Feng Y, Shao Q, Han S, Chu X, Xu Y, Lin S, Zhao Q, & Wu B (2023). Structural insights into dimerization and activation of the mGlu2-mGlu3 and mGlu2-mGlu4 heterodimers. Cell Res 33 10:762-774. PubMed Id: 37286794. doi:10.1038/s41422-023-00830-2.
*Metabotropic Glutamate Receptor 3 (mGlu₃) with bound LY341495: Homo sapiens* E Eukaryota, 4.17 Å** cryo-EM structure with bound LY341495/NAM, 3.71 Å: 7WI6 with bound LY2794193, 3.68 Å: 7WIH	7WI8	Data File Jmol Viewer 7WI8 7WI6 7WIH	Fang et al. (2022). Fang W, Yang F, Xu C, Ling S, Lin L, Zhou Y, Sun W, Wang X, Liu P, Rondard P, Shi P, Pin JP, Tian C, & Liu J (2022). Structural basis of the activation of metabotropic glutamate receptor 3. Cell Res 32 7:695-698. PubMed Id: 35236939. doi:10.1038/s41422-022-00623-z.
*Metabotropic Glutamate Receptor 4 (mGlu₄) with bound G_i: Homo Sapiens* E Eukaryota (expressed in S. frugiperda), 4.00 Å** cryo-EM structure	7E9H	Data File Jmol Viewer 7E9H	Lin et al. (2021). Lin S, Han S, Cai X, Tan Q, Zhou K, Wang D, Wang X, Du J, Yi C, Chu X, Dai A, Zhou Y, Chen Y, Zhou Y, Liu H, Liu J, Yang D, Wang MW, Zhao Q, & Wu B (2021). Structures of Gi-bound metabotropic glutamate receptors mGlu2 and mGlu4. Nature 594 :583-588. PubMed Id: 34135510. doi:10.1038/s41586-021-03495-2.
*Metabotropic Glutamate Receptor 4 (mGlu₄) with bound G_i1: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure	8JD6	Data File Jmol Viewer 8JD6	Wang et al. (2023). Wang X, Wang M, Xu T, Feng Y, Shao Q, Han S, Chu X, Xu Y, Lin S, Zhao Q, & Wu B (2023). Structural insights into dimerization and activation of the mGlu2-mGlu3 and mGlu2-mGlu4 heterodimers. Cell Res 33 10:762-774. PubMed Id: 37286794. doi:10.1038/s41422-023-00830-2.
*Metabotropic Glutamate Receptor 5 (mGlu₅) with bound negative allosteric modulator: Homo sapiens* E Eukaryota, 2.60 Å** Engineered protein. T4 lysozyme inserted between TM helices V and VI; thermostabilized by five collective mutations in TM3 and TM5.	4OO9	Data File Jmol Viewer 4OO9	Doré et al. (2014). Doré AS, Okrasa K, Patel JC, Serrano-Vega M, Bennett K, Cooke RM, Errey JC, Jazayeri A, Khan S, Tehan B, Weir M, Wiggin GR, & Marshall FH (2014). Structure of class C GPCR metabotropic glutamate receptor 5 transmembrane domain. Nature 511 :557-562. PubMed Id: 25042998. doi:10.1038/nature13396.
*Metabotropic Glutamate Receptor 5 (mGlu₅) with bound compound 14: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.10 Å** with bound compound 25 (HTL14242), 2.60 Å: 5CGD Engineered protein. T4 lysozyme inserted between TM helices V and VI; thermostabilized by six collective mutations in TM3 and TM5.	5CGC	Data File Jmol Viewer 5CGC 5CGD	Christopher et al. (2015). Christopher JA, Aves SJ, Bennett KA, Doré AS, Errey JC, Jazayeri A, Marshall FH, Okrasa K, Serrano-Vega MJ, Tehan BG, Wiggin GR, & Congreve M (2015). Fragment and Structure-Based Drug Discovery for a Class C GPCR: Discovery of the mGlu5 Negative Allosteric Modulator HTL14242 (3-Chloro-5-[6-(5-fluoropyridin-2-yl)pyrimidin-4-yl]benzonitrile). J Med Chem 58 :6653-6664. PubMed Id: 26225459. doi:10.1021/acs.jmedchem.5b00892.
*Metabotropic Glutamate Receptor 5 (mGlu5) apo form: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 4 Å** cryo-EM structure bound to L-quisqualate, 4 Å: 6N51 by x-ray diffraction: apo Form Ligand Binding Domain, 4 Å: 6N4X Extracellular Domain with Nb43, 3.26 Å: 6N4Y Extracellular Domain in Complex with Nb43 and L-quisqualic acid, 3.75 Å: 6N50	6N52	Data File Jmol Viewer 6N52 6N4X 6N50 6N51 6N4Y	Koehl et al. (2019). Koehl A, Hu H, Feng D, Sun B, Zhang Y, Robertson MJ, Chu M, Kobilka TS, Laermans T, Steyaert J, Tarrasch J, Dutta S, Fonseca R, Weis WI, Mathiesen JM, Skiniotis G, & Kobilka BK (2019). Structural insights into the activation of metabotropic glutamate receptors. Nature 566 7742:79-84. PubMed Id: 30675062. doi:10.1038/s41586-019-0881-4.
*Metabotropic Glutamate Receptor 5 (mGlu5) with bound MMPEP: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.20 Å** with bound Fenobam, 2.65 Å: 6FFH	6FFI	Data File Jmol Viewer 6FFI 6FFH	Christopher et al. (2019). Christopher JA, Orgován Z, Congreve M, Doré AS, Errey JC, Marshall FH, Mason JS, Okrasa K, Rucktooa P, Serrano-Vega MJ, Ferenczy GG, & Keserű GM (2019). Structure-Based Optimization Strategies for G Protein-Coupled Receptor (GPCR) Allosteric Modulators: A Case Study from Analyses of New Metabotropic Glutamate Receptor 5 (mGlu5) X-ray Structures. J Med Chem 62 1:207-222. PubMed Id: 29455526. doi:10.1021/acs.jmedchem.7b01722.
*Metabotropic Glutamate Receptor 5 (mGlu₅) with orthosteric antagonist, LY341495: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.00 Å** cryo-EM structure with bound with L-quisqualic acid, 3.80 Å 7FD8 x-ray: thermostabilised 7TM domain bound to photoswitchable ligand alloswitch-1, 2.54 Å 7P2L	7FD9	Data File Jmol Viewer 7FD9 7FD8 7P2L	Nasrallah et al. (2021). Nasrallah C, Cannone G, Briot J, Rottier K, Berizzi AE, Huang CY, Quast RB, Hoh F, Banères JL, Malhaire F, Berto L, Dumazer A, Font-Ingles J, Gómez-Santacana X, Catena J, Kniazeff J, Goudet C, Llebaria A, Pin JP, Vinothkumar KR, & Lebon G (2021). Agonists and allosteric modulators promote signaling from different metabotropic glutamate receptor 5 conformations. Cell Rep 36 9:109648. PubMed Id: 34469715. doi:10.1016/j.celrep.2021.109648.
*Metabotropic Glutamate Receptor 7 (mGlu₇) inactive homodimer: Homo sapiens* E Eukaryota (expressed in mammal environmental sample), 4.00 Å** cryo-EM structure	7EPC	Data File Jmol Viewer 7EPC	Du et al. (2021). Du J, Wang D, Fan H, Xu C, Tai L, Lin S, Han S, Tan Q, Wang X, Xu T, Zhang H, Chu X, Yi C, Liu P, Wang X, Zhou Y, Pin JP, Rondard P, Liu H, Liu J, Sun F, Wu B, & Zhao Q (2021). Structures of human mGlu2 and mGlu7 homo- and heterodimers. Nature 594 7864:589-593. PubMed Id: 34135509. doi:10.1038/s41586-021-03641-w.
*Calcium-Sensing Receptor (CaSR) bound with calcium ions: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.80 Å** cryo-EM structure with bound with L-Trp, 4.40 Å: 7DTU with bound L-Trp and calcium ions, 3.50 Å: 7DTV inactive close-close conformation, 4.50 Å: 7DTW	7DTT	Data File Jmol Viewer 7DTT 7DTW 7DTV 7DTU	Ling et al. (2021). Ling S, Shi P, Liu S, Meng X, Zhou Y, Sun W, Chang S, Zhang X, Zhang L, Shi C, Sun D, Liu L, & Tian C (2021). Structural mechanism of cooperative activation of the human calcium-sensing receptor by Ca²⁺ ions and L-tryptophan. Cell Res 31 4:383-394. PubMed Id: 33603117. doi:10.1038/s41422-021-00474-0.
*Calcium-Sensing Receptor (CaSR) with bound cinacalcet in detergent: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.70 Å** cryo-EM structure in complex with G_q, 3.10 Å: 8WPU	8WPG	Data File Jmol Viewer 8WPG 8WPU	Ling et al. (2023). Ling S, Meng X, Zhang Y, Xia Z, Zhou Y, Yang F, Shi P, Shi C, & Tian C (2023). Structural insights into asymmetric activation of the calcium-sensing receptor-Gq complex. Cell Res . PubMed Id: 37919470. doi:10.1038/s41422-023-00892-2.
*Calcium-Sensing Receptor (CaSR) in complex with NPS-2143: Gallus gallus* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure with bound Ca²⁺ & L-Trp in active state, 3.20 Å: 7DD6 in complex with Evocalcet, 3.20 Å: 7DD7	7DD5	Data File Jmol Viewer 7DD5 7DD6 7DD7	Wen et al. (2021). Wen T, Wang Z, Chen X, Ren Y, Lu X, Xing Y, Lu J, Chang S, Zhang X, Shen Y, & Yang X (2021). Structural basis for activation and allosteric modulation of full-length calcium-sensing receptor. Sci Adv 7 23:eabf5325. PubMed Id: 34088669. doi:10.1126/sciadv.abg1483.
*Calcium-Sensing Receptor (CaSR) homodimer, active state-cinacalcet: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.80 Å** cryo-EM structure homodimer, active state-etelcalcetide-evocalset, 2.50 Å: 7M3G inactive state with NPS2143, 4.10 Å: 7M3J inactive state with NPS2143, Ca²⁺ & Trp, 3.20 Å: 7M3E	7M3F	Data File Jmol Viewer 7M3F 7M3E 7M3G 7M3J	Gao et al. (2021). Gao Y, Robertson MJ, Rahman SN, Seven AB, Zhang C, Meyerowitz JG, Panova O, Hannan FM, Thakker RV, Bräuner-Osborne H, Mathiesen JM, & Skiniotis G (2021). Asymmetric activation of the calcium-sensing receptor homodimer. Nature 595 7867:455-459. PubMed Id: 34194040. doi:10.1038/s41586-021-03691-0.
*Calcium-Sensing Receptor (CaSR) homodimer in complex with NB2D11, inactive: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 6.00 Å** cryo-EM structure TNCA-bound, 3.00 Å 7E6T	7E6U	Data File Jmol Viewer 7E6U 7E6T	Chen et al. (2021). Chen X, Wang L, Cui Q, Ding Z, Han L, Kou Y, Zhang W, Wang H, Jia X, Dai M, Shi Z, Li Y, Li X, & Geng Y (2021). Structural insights into the activation of human calcium-sensing receptor. Elife 10 :e68578. PubMed Id: 34467854. doi:10.7554/eLife.68578.
*Calcium-Sensing Receptor (CaSR) homodimer, active with bound positive allosteric modulator: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.70 Å** cryo-EM structure positive allosteric modulator-free state, 2.70 Å 7SIM negative allosteric modulator-bound inactive, 5.90 Å 7SIN	7SIL	Data File Jmol Viewer 7SIL 7SIM 7SIN	Park et al. (2021). Park J, Zuo H, Frangaj A, Fu Z, Yen LY, Zhang Z, Mosyak L, Slavkovich VN, Liu J, Ray KM, Cao B, Vallese F, Geng Y, Chen S, Grassucci R, Dandey VP, Tan YZ, Eng E, Lee Y, Kloss B, Liu Z, Hendrickson WA, Potter CS, Carragher B, Graziano J, Conigrave AD, Frank J, Clarke OB, & Fan QR (2021). Symmetric activation and modulation of the human calcium-sensing receptor. Proc Natl Acad Sci U S A 118 51:e2115849118. PubMed Id: 34916296. doi:10.1073/pnas.2115849118.
*Orphan GPR158 receptor: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.52 Å** cryo-EM structure in complex with RGS7-Gβ5 in a 2:1:1 ratio, 4.30 Å 7EWP in complex with RGS7-Gβ5 in a 2:2:2 ratio, 6.30 Å 7EWR	7EWL	Data File Jmol Viewer 7EWL 7EWR 7EWP	Jeong et al. (2021). Jeong E, Kim Y, Jeong J, & Cho Y (2021). Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. Nat Commun 12 1:6805. PubMed Id: 34815401. doi:10.1038/s41467-021-27147-1.
*Orphan GPR158 receptor: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure GPR158 coupled to the RGS7-Gβ5 complex, 3.40 Å	7SHE	Data File Jmol Viewer 7SHE	Patil et al. (2022). Patil DN, Singh S, Laboute T, Strutzenberg TS, Qiu X, Wu D, Novick SJ, Robinson CV, Griffin PR, Hunt JF, Izard T, Singh AK, & Martemyanov KA (2022). Cryo-EM structure of human GPR158 receptor coupled to the RGS7-Gβ5 signaling complex. Science 375 6576:86-91. PubMed Id: 34793198. doi:10.1126/science.abl4732.
G Protein-Coupled Receptors: Class D These are found exclusively in fungi
*Ste2 pheromone receptor, active state: Saccharomyces cerevisiae* E Eukaryota (expressed in Trichoplusia ni), 3.50 Å** cryo-EM structure	7AD3	Data File Jmol Viewer 7AD3	Velazhahan et al. (2021). Velazhahan V, Ma N, Pándy-Szekeres G, Kooistra AJ, Lee Y, Gloriam DE, Vaidehi N, & Tate CG (2021). Structure of the class D GPCR Ste2 dimer coupled to two G proteins. Nature 589 7840:148-153. PubMed Id: 33268889. doi:10.1038/s41586-020-2994-1.
*Ste2 pheromone receptor, ligand-free state: Saccharomyces cerevisiae* E Eukaryota (expressed in Trichoplusia ni), 3.10 Å** cryo-EM structure inactive state with bound antagonist, 2.70 Å 7QA8 inactive-like state with bound agonist, 3.53 Å 7QBC active-like state with bound agonist, 3.46 Å 7QBI	7QB9	Data File Jmol Viewer 7QB9 7QA8 7QBC 7QBI	Velazhahan et al. (2022). Velazhahan V, Ma N, Vaidehi N, & Tate CG (2022). Activation mechanism of the class D fungal GPCR dimer Ste2. Nature 603 7902:743-748. PubMed Id: 35296853. doi:10.1038/s41586-022-04498-3.
G Protein-Coupled Receptors: Class F
*Smoothened (SMO) receptor with bound antagonist, LY2940680: Homo sapiens* E Eukaryota, 2.45 Å** Engineered Protein: apocytochrome b562 RIL (BRIL) fused to truncated N-terminus at S190. C-terminus truncated at Q555.	4JKV	Data File Jmol Viewer 4JKV	Wang et al. (2013). Wang C, Wu H, Katritch V, Han GW, Huang XP, Liu W, Siu FY, Roth BL, Cherezov V, & Stevens RC (2013). Structure of the human smoothened receptor bound to an antitumour agent. Nature 497 :338-343. PubMed Id: 23636324. doi:10.1038/nature12167.
*Smoothened (SMO) receptor in complex with SANT-1,: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.80 Å** in complex with SAG1.5, 2.60 Å: 4QIN in complex with ANTA XV, 2.61 Å: 4QIM	4N4W	Data File Jmol Viewer 4N4W 4QIN 4QIM	Wang et al. (2014). Wang C, Wu H, Evron T, Vardy E, Han GW, Huang XP, Hufeisen SJ, Mangano TJ, Urban DJ, Katritch V, Cherezov V, Caron MG, Roth BL, & Stevens RC (2014). Structural basis for Smoothened receptor modulation and chemoresistance to anticancer drugs. Nat Commun 5 . PubMed Id: 25008467. doi:10.1038/ncomms5355.
*Smoothened (SMO) receptor in complex with cyclopamine: Homo Sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** XFEL structure	4O9R	Data File Jmol Viewer 4O9R	Weierstall et al. (2014). Weierstall U, James D, Wang C, White TA, Wang D, Liu W, Spence JC, Bruce Doak R, Nelson G, Fromme P, Fromme R, Grotjohann I, Kupitz C, Zatsepin NA, Liu H, Basu S, Wacker D, Han GW, Katritch V, Boutet S, Messerschmidt M, Williams GJ, Koglin JE, Marvin Seibert M, Klinker M, Gati C, Shoeman RL, Barty A, Chapman HN, Kirian RA, Beyerlein KR, Stevens RC, Li D, Shah ST, Howe N, Caffrey M, & Cherezov V (2014). Lipidic cubic phase injector facilitates membrane protein serial femtosecond crystallography. Nat Commun 5 :3309. PubMed Id: 24525480. doi:10.1038/ncomms4309.
*Smoothened (SMO) receptor in complex with cholesterol (apo-SMOΔC): Homo sapiens* E Eukaryota (expressed in HEK-293S-GnTI^-), 3.2 Å** Engineered protein: N- and C-termini truncated; apocytochrome b₅₆₂ RIL (BRIL) replaces intracellular loop 3. with bound vismodegib (vismo-SMOΔC), 3.3 Å: 5L7I	5L7D	Data File Jmol Viewer 5L7D 5L7I	Byrne et al. (2016). Byrne EF, Sircar R, Miller PS, Hedger G, Luchetti G, Nachtergaele S, Tully MD, Mydock-McGrane L, Covey DF, Rambo RP, Sansom MS, Newstead S, Rohatgi R, & Siebold,C. (2016). Structural basis of Smoothened regulation by its extracellular domains. Nature 535 :517-522. PubMed Id: 27437577.
*Smoothened (SMO) receptor (multi-domain) in complex with TC114: Homo sapiens* E Eukaryota (expressed in sf9 cells), 3.00 Å** engineered protein: Flavodoxin fused to ICL3 XFEL structure E194M, 2.90 Å: 5V56	5V57	Data File Jmol Viewer 5V57 5V56	Zhang et al. (2017). Zhang X, Zhao F, Wu Y, Yang J, Han GW, Zhao S, Ishchenko A, Ye L, Lin X, Ding K, Dharmarajan V, Griffin PR, Gati C, Nelson G, Hunter MS, Hanson MA, Cherezov V, Stevens RC, Tan W, Tao H, & Xu F (2017). Crystal structure of a multi-domain human smoothened receptor in complex with a super stabilizing ligand. Nat Commun 8 :15383. PubMed Id: 28513578. doi:10.1038/ncomms15383.
*Smoothened (SMO) receptor with bound oxysterol coupled to a heterotrimeric G_i: Homo sapiens* E Eukaryota (expressed in HEK293s cells), 3.84 Å** cryo-EM structure	6OT0	Data File Jmol Viewer 6OT0	Qi et al. (2019). Qi X, Liu H, Thompson B, McDonald J, Zhang C, & Li X (2019). Cryo-EM structure of oxysterol-bound human Smoothened coupled to a heterotrimeric G_i. Nature 571 7764:279-283. PubMed Id: 31168089. doi:10.1038/s41586-019-1286-0.
*Smoothened (SMO) receptor+G_i in complex with SAG: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.96 Å** cryo-EM structure in complex with 24(S),25-EC, 3.14 Å: 6XBM D384R mutant, 3.88 Å: 6XBJ G111C/I496C mutant, 3.24 Å: 6XBK	6XBL	Data File Jmol Viewer 6XBL 6XBK 6XBJ 6XBM	Qi et al. (2020). Qi X, Friedberg L, De Bose-Boyd R, Long T, & Li X (2020). Sterols in an intramolecular channel of Smoothened mediate Hedgehog signaling. Nat Chem Biol 16 12:1368-1375. PubMed Id: 32929279. doi:10.1038/s41589-020-0646-2.
*Smoothened (SMO) receptor bound to SAG21k, cholesterol, and NbSmo8: Mus musculus* E Eukaryota, 2.8 Å**	6O3C	Data File Jmol Viewer 6O3C	Deshpande et al. (2019). Deshpande I, Liang J, Hedeen D, Roberts KJ, Zhang Y, Ha B, Latorraca NR, Faust B, Dror RO, Beachy PA, Myers BR, & Manglik A (2019). Smoothened stimulation by membrane sterols drives Hedgehog pathway activity. Nature 571 7764:284-288. PubMed Id: 31263273. doi:10.1038/s41586-019-1355-4.
*Smoothened (SMO) receptor-PGS2 in a lipidic environment, unliganded: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.70 Å** cryo-EM structure	8CXO	Data File Jmol Viewer 8CXO	Zhang et al. (2022). Zhang K, Wu H, Hoppe N, Manglik A, & Cheng Y (2022). Fusion protein strategies for cryo-EM study of G protein-coupled receptors. Nat Commun 13 1:4366. PubMed Id: 35902590. doi:10.1038/s41467-022-32125-2.
*Frizzled 1 (FZD1) receptor - G_q complex, apo state: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.50 Å** cryo-EM structure FZD1-Fab-VHH complex, inactive state, 3.40 Å: 8J9O	8J9N	Data File Jmol Viewer 8J9N 8J9O	Zhang et al. (2024). Zhang Z, Lin X, Wei L, Wu Y, Xu L, Wu L, Wei X, Zhao S, Zhu X, & Xu F (2024). A framework for Frizzled-G protein coupling and implications to the PCP signaling pathways. Cell Discov 10 1:3. PubMed Id: 38182578. doi:10.1038/s41421-023-00627-y.
*Frizzled 3 (FZD3) receptor - G_s complex, apo state: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.20 Å** cryo-EM structure FZD3-Fab-VHH complex, inactive state, 3.30 Å: 8JHC	8JHI	Data File Jmol Viewer 8JHI 8JHC	Zhang et al. (2024). Zhang Z, Lin X, Wei L, Wu Y, Xu L, Wu L, Wei X, Zhao S, Zhu X, & Xu F (2024). A framework for Frizzled-G protein coupling and implications to the PCP signaling pathways. Cell Discov 10 1:3. PubMed Id: 38182578. doi:10.1038/s41421-023-00627-y.
*Frizzled 4 (FZD4) receptor in the ligand-free state: Homo sapiens* E Eukaryota, 2.4 Å** Engineered protein: ΔCRD contains residues 178-517. Residues of third intracellular loop (ICL3) replaced by rubredoxin. Member of class F receptor.	6BD4	Data File Jmol Viewer 6BD4	Yang et al. (2018). Yang S, Wu Y, Xu TH, de Waal PW, He Y, Pu M, Chen Y, DeBruine ZJ, Zhang B, Zaidi SA, Popov P, Guo Y, Han GW, Lu Y, Suino-Powell K, Dong S, Harikumar KG, Miller LJ, Katritch V, Xu HE, Shui W, Stevens RC, Melcher K, Zhao S, & Xu F (2018). Crystal structure of the Frizzled 4 receptor in a ligand-free state. Nature 560 7720:666-670. PubMed Id: 30135577. doi:10.1038/s41586-018-0447-x.
*Frizzled 5 (FZD5) receptor in the ligand-free state: Homo sapiens* E Eukaryota, 3.70 Å** cryo-EM structure Engineered protein: cytochrome b₅₆₂ inserted into intracellular loop 3. Structure includes anti-BRIL Fab and anti-Fab nanobody.	6WW2	Data File Jmol Viewer 6WW2	Tsutsumi et al. (2020). Tsutsumi N, Mukherjee S, Waghray D, Janda CY, Jude KM, Miao Y, Burg JS, Aduri NG, Kossiakoff AA, Gati C, & Garcia KC (2020). Structure of human Frizzled5 by fiducial-assisted cryo-EM supports a heterodimeric mechanism of canonical Wnt signaling. Elife 9 :e58464. PubMed Id: 32762848. doi:10.7554/eLife.58464.
*Frizzled 6 (FZD6) receptor - G_s complex, apo state: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.30 Å** cryo-EM structure FZD6-Fab-VHH complex, inactive state, 3.20 Å: 8JH7	8JHB	Data File Jmol Viewer 8JHB 8JH7	Zhang et al. (2024). Zhang Z, Lin X, Wei L, Wu Y, Xu L, Wu L, Wei X, Zhao S, Zhu X, & Xu F (2024). A framework for Frizzled-G protein coupling and implications to the PCP signaling pathways. Cell Discov 10 1:3. PubMed Id: 38182578. doi:10.1038/s41421-023-00627-y.
*Frizzled 7 (FZD7) receptor in complex with heterotrimeric G_s: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.22 Å** cryo-EM structure	7EVW	Data File Jmol Viewer 7EVW	Xu et al. (2021). Xu L, Chen B, Schihada H, Wright SC, Turku A, Wu Y, Han GW, Kowalski-Jahn M, Kozielewicz P, Bowin CF, Zhang X, Li C, Bouvier M, Schulte G, & Xu F (2021). Cryo-EM structure of constitutively active human Frizzled 7 in complex with heterotrimeric G_s. Cell Res . PubMed Id: 34239071. doi:10.1038/s41422-021-00525-6.
G Protein-Coupled Receptors: Class T
*Bitter taste receptor TAS2R46, apo state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.01 Å** cryo-EM structure in ligand-free state, 3.08 Å: 7XP5 in active state, 3.01 Å: 7XP6	7XP4	Data File Jmol Viewer 7XP4 7XP5 7XP6	Xu et al. (2022). Xu W, Wu L, Liu S, Liu X, Cao X, Zhou C, Zhang J, Fu Y, Guo Y, Wu Y, Tan Q, Wang L, Liu J, Jiang L, Fan Z, Pei Y, Yu J, Cheng J, Zhao S, Hao X, Liu ZJ, & Hua T (2022). Structural basis for strychnine activation of human bitter taste receptor TAS2R46. Science 377 6612:1298-1304. PubMed Id: 36108005. doi:10.1126/science.abo1633.
*Bitter taste receptor TAS2R14 - G_i complex with bound cholesterol and intracellular tastant cmpd28.1: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.68 Å** cryo-EM structure TAS2R14-G_gust complex, 2.88 Å: 8VY9	8VY7	Data File Jmol Viewer 8VY7 8VY9	Kim et al. (2024). Kim Y, Gumpper RH, Liu Y, Kocak DD, Xiong Y, Cao C, Deng Z, Krumm BE, Jain MK, Zhang S, Jin J, & Roth BL (2024). Bitter taste receptor activation by cholesterol and an intracellular tastant. Nature 628 8008:664-671. PubMed Id: 38600377. doi:10.1038/s41586-024-07253-y.
Wntless (WLS) Transporters Also called Evi and GPR177 transporters.
*Wntless (WLS) transporter in complex with WNT8A: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.19 Å** cryo-EM structure	7KC4	Data File Jmol Viewer 7KC4	Nygaard et al. (2021). Nygaard R, Yu J, Kim J, Ross DR, Parisi G, Clarke OB, Virshup DM, & Mancia F (2021). Structural Basis of WLS/Evi-Mediated Wnt Transport and Secretion. Cell 184 1:194-206.e14. PubMed Id: 33357447. doi:10.1016/j.cell.2020.11.038.
*Wntless (WLS) transporter in complex with Wnt3A: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.20 Å** cryo-EM structure	7DRT	Data File Jmol Viewer 7DRT	Zhong et al. (2021). Zhong Q, Zhao Y, Ye F, Xiao Z, Huang G, Xu M, Zhang Y, Zhan X, Sun K, Wang Z, Cheng S, Feng S, Zhao X, Zhang J, Lu P, Xu W, Zhou Q, & Ma D (2021). Cryo-EM structure of human Wntless in complex with Wnt3a. Nat Commun 12 1:4541. PubMed Id: 34315898. doi:10.1038/s41467-021-24731-3.
Host-Defense Proteins
*STING (aka TMEM173, MITA, ERIS, or MPHYS), full-length apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.1 Å** cryo-EM structure	6NT5	Data File Jmol Viewer 6NT5	Shang et al. (2019). Shang G, Zhang C, Chen ZJ, Bai XC, & Zhang X (2019). Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP. Nature 567 7748:389-393. PubMed Id: 30842659. doi:10.1038/s41586-019-0998-5.
*STING (aka TMEM173, MITA, ERIS, or MPHYS) bound to both cGAMP and Compound 53: homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.45 Å** cryo-EM structure	7SII	Data File Jmol Viewer 7SII	Lu et al. (2022). Lu D, Shang G, Li J, Lu Y, Bai XC, & Zhang X (2022). Activation of STING by targeting a pocket in the transmembrane domain. Nature 604 7906:557-562. PubMed Id: 35388221. doi:10.1038/s41586-022-04559-7.
*STING (aka TMEM173, MITA, ERIS, or MPHYS) bound to HB3089: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.47 Å** cryo-EM structure V147L mutant, 3.65 Å: 8GSZ	8GT6	Data File Jmol Viewer 8GT6 8GSZ	Xie et al. (2022). Xie Z, Wang Z, Fan F, Zhou J, Hu Z, Wang Q, Wang X, Zeng Q, Zhang Y, Qiu J, Zhou X, Xu H, Bai H, Zhan Z, Ding J, Zhang H, Duan W, Yu X, & Geng M (2022). Structural insights into a shared mechanism of human STING activation by a potent agonist and an autoimmune disease-associated mutation. Cell Discov 8 1:133. PubMed Id: 36513640. doi:10.1038/s41421-022-00481-4.
*adapter protein AP-1 in complex with STING (phosphorylated): Homo sapiens* E Eukaryota (expressed in E. coli), 2.34 Å** cryo-EM structure	7R4H	Data File Jmol Viewer 7R4H	Liu et al. (2022). Liu Y, Xu P, Rivara S, Liu C, Ricci J, Ren X, Hurley JH, & Ablasser A (2022). Clathrin-associated AP-1 controls termination of STING signalling. Nature 610 7933:761-767. PubMed Id: 36261523. doi:10.1038/s41586-022-05354-0.
*STING (aka TMEM173, MITA, ERIS, or MPHYS) apo state: Gallus gallus* E Eukaryota (expressed in HEK293 cells), 4 Å** cryo-EM structure in the cGAMP-bound dimeric state, 4 Å: 6NT7 in the cGAMP-bound tetrameric state, 6.5 Å: 6NT8	6NT6	Data File Jmol Viewer 6NT6 6NT8 6NT7	Shang et al. (2019). Shang G, Zhang C, Chen ZJ, Bai XC, & Zhang X (2019). Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP. Nature 567 7748:389-393. PubMed Id: 30842659. doi:10.1038/s41586-019-0998-5.
*chicken STING in complex with human TBK1: Gallus gallus & Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.3 Å** cryo-EM structure	6NT9	Data File Jmol Viewer 6NT9	Zhang et al. (2019). Zhang C, Shang G, Gui X, Zhang X, Bai XC, & Chen ZJ (2019). Structural basis of STING binding with and phosphorylation by TBK1. Nature 567 7748:394-398. PubMed Id: 30842653. doi:10.1038/s41586-019-1000-2.
H⁺/Cl^- or F^- Exchange Transporters
*H⁺/Cl^- Exchange Transporter: Salmonella typhimurium* B Bacteria (expressed in E. coli), 3.0 Å** Formerly ClC Chloride Channel. Escherichia coli protein, 3.5 Å: 1KPK	1KPL	Data File Jmol Viewer 1KPL 1KPK ClC chloride channel ClC chloride channel	Dutzler et al. (2002). Dutzler R, Campbell EB, Cadene M, Chait BT, & MacKinnon R (2002). X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature 415 :287-294. PubMed Id: 11796999.
*H⁺/Cl^- Exchange Transporter: Escherichia coli* B Bacteria, 2.51 Å** Formerly ClC Chloride Channel. Structure reveals gating by a glutamate residue E148A mutant, 3.00 Å: 1OTT. E148Q mutant, 3.30 Å: 1OTU.	1OTS	Data File Jmol Viewer 1OTS 1OTT 1OTU ClC chloride channel	Dutzler et al. (2003). Dutzler R, Campbell EB, & MacKinnon R (2003). Gating the selectivity filter in ClC chloride channels. Science 300 :108-112. PubMed Id: 12649487.
*H⁺/Cl^- Exchange Transporter without bound ions: Escherichia coli* B Bacteria, 3.20 Å** E148Q mutant without bound ions, 3.1 Å: 2EXY. S107A/E148Q/Y445A mutant with bound Br^-, 3.54 Å: 2EZ0.	2EXW	Data File Jmol Viewer 2EXW 2EZ0 2EXY	Lobet & Dutzler (2006). Lobet S & Dutzler R (2006). Ion-binding properties of the ClC chloride selectivity filter. EMBO J 25 :24-33. PubMed Id: 16341087.
*H⁺/Cl^- Exchange Transporter (truncated): Escherichia coli* B Bacteria, 2.50 Å** Truncation: Residues 2-16 at N-terminal and 461-464 at C-terminal. E202Y mutant, 3.20 Å: 4FTP	4ENE	Data File Jmol Viewer 4ENE 4FTP	Lim et al. (2012). Lim HH, Shane T, & Miller C (2012). Intracellular proton access in a Cl^-/H⁺ antiporter. PLoS Biol 10 :e1001441. PubMed Id: 23239938. doi:10.1371/journal.pbio.1001441.
*Monomeric H⁺/Cl^- Exchange Transporter (CLC-ec1): Escherichia coli* B Bacteria, 3.10 Å** ClC transporter was engineered to place tryptophan residues (I201W; I422W) at the momomer-monomer interface to prevent dimerization.	3NMO	Data File Jmol Viewer 3NMO	Robertson et al. (2010). Robertson JL, Kolmakova-Partensky L, & Miller C (2010). Design, function and structure of a monomeric ClC transporter. Nature 468 :844-847. PubMed Id: 21048711.
*H⁺/Cl^- Exchange Transporter CLC-ec1 in Glutamate: Escherichia coli* B Bacteria, 3.02 Å** E148A mutant	4FG6	Data File Jmol Viewer 4FG6	Feng et al. (2012). Feng L, Campbell EB, & Mackinnon R (2012). Molecular mechanism of proton transport in CLC Cl^-/H⁺ exchange transporters. Proc Natl Acad Sci USA 109 :11699-11704. PubMed Id: 22753511. doi:10.1073/pnas.1205764109.
*H⁺/Cl^- Exchange Transporter CLC-ec1, Cysless A399C-A432C mutant: Escherichia coli* B Bacteria, 3.52 Å** Fab complex.	4MQX	Data File Jmol Viewer 4MQX	Basilio et al. (2014). Basilio D, Noack K, Picollo A, & Accardi A (2014). Conformational changes required for H⁺/Cl^- exchange mediated by a CLC transporter. Nat Struct Mol Biol 21 :456-463. PubMed Id: 24747941. doi:10.1038/nsmb.2814.
*H⁺/Cl^- Exchange Transporter CLC-ec1, E148D mutant in 20 mM bromide: Escherichia coli* B Bacteria, 2.95 Å** E148D mutant in 50 mM bromide, 3.3 Å: 6AD8 E148D mutant in 200 mM bromide, 3.15 Å: 6ADA E148N mutant in 20 mM bromide, 2.69 Å: 6ADB E148N mutant in 200 mM bromide, 3.20 Å: 6K5D ΔNC construct in presence of 200 mM bromide, 3.20 Å: 6K5F E148D/R147A/F317A mutant in presence of 20 mM bromide, 3.02 Å: 6K5I E148D/R147A/F317A mutant in presence 200 mM bromide, 3.16 Å: 6K5A E148A mutant in presence of 50 mM bromoacetate, 3.06 Å: 6ADC	6AD7	Data File Jmol Viewer 6AD7 6K5I 6K5A 6AD8 6ADA 6K5F 6ADC 6K5D 6ADB	Park et al. (2019). Park K, Lee BC, & Lim HH (2019). Mutation of external glutamate residue reveals a new intermediate transport state and anion binding site in a CLC Cl^-/H⁺ antiporter. Proc Natl Acad Sci USA 116 35:17345-17354. PubMed Id: 31409705. doi:10.1073/pnas.1901822116.
*H⁺/Cl^- Exchange Transporter CLC-ec1, "QQQ" mutant (E148Q/E203Q/E113Q): Escherichia coli* B Bacteria, 2.62 Å**	6V2J	Data File Jmol Viewer 6V2J	Chavan et al. (2020). Chavan TS, Cheng RC, Jiang T, Mathews II, Stein RA, Koehl A, Mchaourab HS, Tajkhorshid E, & Maduke M (2020). A CLC-ec1 mutant reveals global conformational change and suggests a unifying mechanism for the CLC Cl^-/H⁺ transport cycle. Elife 9 :e53479. PubMed Id: 32310757. doi:10.7554/eLife.53479.
*H⁺/Cl^- Eukaryotic Exchange Transporter: Cyanidioschyzon merolae* E Eukaryota (expressed in Trichoplusia ni), 3.50 Å**	3ORG	Data File Jmol Viewer 3ORG	Feng et al. (2010). Feng L, Campbell EB, Hsiung Y, & MacKinnon R (2010). Structure of a eukaryotic CLC transporter defines an intermediate state in the transport cycle. Science 330 :635-641. PubMed Id: 20929736.
*H⁺/Cl^- Eukaryotic Exchange Transporter: Synechocystis sp. pcc 6803* B Bacteria (expressed in E. coli), 3.20 Å** In the presence of Br^-, 3.60 Å: 3Q17	3ND0	Data File Jmol Viewer 3ND0 3Q17	Jayaram et al. (2011). Jayaram H, Robertson JL, Wu F, Williams C, & Miller C (2011). Structure of a Slow CLC Cl^?/H⁺Antiporter from a Cyanobacterium. Biochemistry 50 :788-794. PubMed Id: 21174448.
*CLC-type F^-/H⁺ antiporter: Enterococcus casseliflavus* B Bacteria (expressed in E. coli), 3.00 Å** E118Q mutant, 3.35 Å: 6D0K V319G mutant, 3.12 Å: 6D0N	6D0J	Data File Jmol Viewer 6D0J 6D0N 6D0K	Last et al. (2018). Last NB, Stockbridge RB, Wilson AE, Shane T, Kolmakova-Partensky L, Koide A, Koide S, & Miller C (2018). A CLC-type F^-/H⁺ antiporter in ion-swapped conformations. Nat Struct Mol Biol 25 7:601-606. PubMed Id: 29941917. doi:10.1038/s41594-018-0082-0.
*CLC-7 Cl^-/H⁺ exchanger: Gallus gallus* E Eukaryota (expressed in HEK293 cells), 2.92 Å** cryo-EM structure	7JM6	Data File Jmol Viewer 7JM6	Schrecker et al. (2020). Schrecker M, Korobenko J, & Hite RK (2020). Cryo-EM structure of the lysosomal chloride-proton exchanger CLC-7 in complex with OSTM1. Elife 9 . PubMed Id: 32749217. doi:10.7554/eLife.59555.
*CLC-7 Cl^-/H⁺ exchanger in complex with OSTM1: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.82 Å** cryo-EM structure	7JM7	Data File Jmol Viewer 7JM7	Schrecker et al. (2020). Schrecker M, Korobenko J, & Hite RK (2020). Cryo-EM structure of the lysosomal chloride-proton exchanger CLC-7 in complex with OSTM1. Elife 9 . PubMed Id: 32749217. doi:10.7554/eLife.59555.
*CLC-7 Cl^-/H⁺ exchanger in complex with OSTM1: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.70 Å** cryo-EM structure	7BXU	Data File Jmol Viewer 7BXU	Zhang et al. (2020). Zhang S, Liu Y, Zhang B, Zhou J, Li T, Liu Z, Li Y, & Yang M (2020). Molecular insights into the human CLC-7/Ostm1 transporter. Sci Adv 6 33. PubMed Id: 32851177. doi:10.1126/sciadv.abb4747.
*CLCa-type 2NO₃⁻/1H⁺ antiporter: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 2.84 Å** cryo-EM structure	7XA9	Data File Jmol Viewer 7XA9	He et al. (2023). He J, Wang M, Li S, Chen L, Zhang K, & She J (2023). Cryo-EM structure of the plant nitrate transporter AtCLCa reveals characteristics of the anion-binding site and the ATP-binding pocket. J Biol Chem 299 2:102833. PubMed Id: 36581207. doi:10.1016/j.jbc.2022.102833.
*CLCa-type 2NO₃⁻/1H⁺ antiporter, with bound Cl^-, ATP, and PIP₂: Arabidopsis thaliana* E Eukaryota (expressed in Komagataella pastoris), 2.96 Å** cryo-EM structure with bound nitrate, ATP, and PIP₂, 3.16 Å: 8IAD	8IAB	Data File Jmol Viewer 8IAB 8IAD	Yang et al. (2023). Yang Z, Zhang X, Ye S, Zheng J, Huang X, Yu F, Chen Z, Cai S, & Zhang P (2023). Molecular mechanism underlying regulation of Arabidopsis CLCa transporter by nucleotides and phospholipids. Nat Commun 14 1:4879. PubMed Id: 37573431. doi:10.1038/s41467-023-40624-z.
AAA-ATPAse Membrane Translocators AAA: ATPases associated with various cellular activities
*heptameric Bcs1 AAA-ATPase that facilitates translocation of Rieske protein Rip1: Saccharomyces cerevisiae* E Eukaryota, 3.40 Å** cryo-EM structure Apo1 state, 4.40 Å: 6SH4 Apo2 state, 4.60 Å: 6SH5	6SH3	Data File Jmol Viewer 6SH3 6SH5 6SH4	Kater et al. (2020). Kater L, Wagener N, Berninghausen O, Becker T, Neupert W, & Beckmann R (2020). Structure of the Bcs1 AAA-ATPase suggests an airlock-like translocation mechanism for folded proteins. Nat Struct Mol Biol 27 2:142-149. PubMed Id: 31988523. doi:10.1038/s41594-019-0364-1.
*heptameric Bcs1 AAA-ATPase that facilitates translocation of the Rieske iron-sulfur protein (ISP), full-length: Mus musculus* E Eukaryota (expressed in Komagataella pastoris), 4.40 Å** cryo-EM structure bcs1 AAA domain by x-ray diffraction, 2.17 Å: 6U1Y Apo Bcs1, 3.81 Å: 6UKP ATPgammaS bound Bcs1, 3.20 Å: 6UKS	6UKO	Data File Jmol Viewer 6UKO 6UKP 6U1Y 6UKS	Tang et al. (2020). Tang WK, Borgnia MJ, Hsu AL, Esser L, Fox T, de Val N, & Xia D (2020). Structures of AAA protein translocase Bcs1 suggest translocation mechanism of a folded protein. Nat Struct Mol Biol 27 2:202-209. PubMed Id: 32042153. doi:10.1038/s41594-020-0373-0.
*hexameric AAA protein Msp1 mislocalized protein extractor (E214Q)-substrate complex: Chaetomium thermophilum* E Eukaryota (expressed in E. coli), 3.50 Å** cryo-EM structure. Not a transmembrane protein. Each subunit is anchored to the membrane by a single TM helix (not seen in structure) Msp1-substrate complex in closed conformation, 3.10 Å: 6PDW Msp1-substrate complex in open conformation, 3.70 Å: 6PDY	6PE0	Data File Jmol Viewer 6PE0 6PDW 6PDY	Wang et al. (2020). Wang L, Myasnikov A, Pan X, & Walter P (2020). Structure of the AAA protein Msp1 reveals mechanism of mislocalized membrane protein extraction. Elife 9 . PubMed Id: 31999255. doi:10.7554/eLife.54031.
*AAA protein ATAD1 (with a catalytic dead mutation) in complex with a peptide substrate, closed conformation: Homo sapiens* E Eukaryota (expressed in E. coli), 3.20 Å** cryo-EM structure open conformation, 3.50 Å: 7UPT	7UPR	Data File Jmol Viewer 7UPR 7UPT	Wang et al. (2022). Wang L, Toutkoushian H, Belyy V, Kokontis CY, & Walter P (2022). Conserved structural elements specialize ATAD1 as a membrane protein extraction machine. Elife 11 :e73941. PubMed Id: 35550246. doi:10.7554/eLife.73941.
Stomatin, Prohibitin, Flotillin, and HflK/C (SPFH) Family Proteins These proteins seem to play a scaffolding role microdomain formation.
*Supramolecular complex comprised of HflK, HflC, & FtsH: Escherichia coli* B Bacteria, 3.27 Å** cryo-EM structure Map of one quarter of the complex for symmetry expansion, 3.27 Å 7VHQ	7VHP	Data File Jmol Viewer 7VHP 7VHQ	Ma et al. (2022). Ma C, Wang C, Luo D, Yan L, Yang W, Li N, & Gao N (2022). Structural insights into the membrane microdomain organization by SPFH family proteins. Cell Res 32 2:176-189. PubMed Id: 34975153. doi:10.1038/s41422-021-00598-3.
*FtsH-HflkC AAA protease complex: Escherichia coli* B Bacteria, 4.00 Å** cryo-EM structure FtsH protease cytosolic domains, 3.40 Å: 7W14	7WI3	Data File Jmol Viewer 7WI3 7W14	Qiao et al. (2022). Qiao Z, Yokoyama T, Yan XF, Beh IT, Shi J, Basak S, Akiyama Y, & Gao YG (2022). Cryo-EM structure of the entire FtsH-HflKC AAA protease complex. Cell Rep 39 9:110890. PubMed Id: 35649372. doi:10.1016/j.celrep.2022.110890.
Celluose Synthases Membrane Imbedded Glycosyltransferases These use UDP-activated glucose to elongate nascent polysaccharides processively across membranes.
*BcsA-BcsB cellulose synthase/cellulose translocation intermediate.: Rhodobacter sphaeroides* B Bacteria (expressed in E. coli), 3.25 Å** Shows a translocating glucan	4HG6	Data File Jmol Viewer 4HG6	Morgan et al. (2013). Morgan JL, Strumillo J, & Zimmer J (2013). Crystallographic snapshot of cellulose synthesis and membrane translocation. Nature 493 :181-186. PubMed Id: 23222542. doi:10.1038/nature11744.
*BcsB cellulose synthase hexamer: Escherichia coli* B Bacteria, 3.40 Å** cryo-EM structure BcsB with polyalanine BcsA model, 4.20 Å: 7LBY	7L2Z	Data File Jmol Viewer 7L2Z 7LBY	Acheson et al. (2021). Acheson JF, Ho R, Goularte NF, Cegelski L, & Zimmer J (2021). Molecular organization of the E. coli cellulose synthase macrocomplex. Nat Struct Mol Biol 28 3:310-318. PubMed Id: 33712813. doi:10.1038/s41594-021-00569-7.
*CesA homotrimer involved in cellulose microfibril formation: Populus tremula* E Eukaryota (expressed in Spodoptera frugiperda), 3.50 Å** cryo-EM structure	6WLB	Data File Jmol Viewer 6WLB	Purushotham et al. (2020). Purushotham P, Ho R, & Zimmer J (2020). Architecture of a catalytically active homotrimeric plant cellulose synthase complex. Science 369 6507:1089-1094. PubMed Id: 32646917. doi:10.1126/science.abb2978.
*CesA7 cotton cellulose synthase isoform 7: Gossypium hirsutum* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure	7D5K	Data File Jmol Viewer 7D5K	Zhang et al. (2021). Zhang X, Xue Y, Guan Z, Zhou C, Nie Y, Men S, Wang Q, Shen C, Zhang D, Jin S, Tu L, Yin P, & Zhang X (2021). Structural insights into homotrimeric assembly of cellulose synthase CesA7 from Gossypium hirsutum. Plant Biotechnol J 19 8:1579-1587. PubMed Id: 33638282. doi:10.1111/pbi.13571.
*hyaluronan synthase: Chlorella virus CZ-2* V Viruses (expressed in E. coli), 3.10 Å** cryo-EM structure inhibited by UDP, 3.10 Å 7SP7 bound to UDP-GlcNAc, 2.70 Å 7SP8 in the GlcNAc-primed channel-closed state, 2.90 Å 7SP9 GlcNAc-primed, channel-open state, 2.80 Å 7SPA	7SP6	Data File Jmol Viewer 7SP6 7SPA 7SP8 7SP7 7SP9	Maloney et al. (2022). Maloney FP, Kuklewicz J, Corey RA, Bi Y, Ho R, Mateusiak L, Pardon E, Steyaert J, Stansfeld PJ, & Zimmer J (2022). Structure, substrate recognition and initiation of hyaluronan synthase. Nature 604 7904:195-201. PubMed Id: 35355017. doi:10.1038/s41586-022-04534-2.
PNPT Superfamily PNPT: polyprenylphosphate N-acetyl hexosamine 1-phosphate transferase Proteins in this superfamily are responsible for the synthesis of cell envelope polymers
*MraY phospho-MurNAc-pentapeptide translocase: Aquifex aeolicus* B Bacteria (expressed in E. coli), 3.30 Å**	4J72	Data File Jmol Viewer 4J72	Chung et al. (2013). Chung BC, Zhao J, Gillespie RA, Kwon DY, Guan Z, Hong J, Zhou P, & Lee SY (2013). Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis. Science 341 :1012-1016. PubMed Id: 23990562. doi:10.1126/science.1236501.
*MraY translocase in complex with Muraymycin D2: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.95 Å**	5CKR	Data File Jmol Viewer 5CKR	Chung et al. (2016). Chung BC, Mashalidis EH, Tanino T, Kim M, Matsuda A, Hong J, Ichikawa S, & Lee SY (2016). Structural insights into inhibition of lipid I production in bacterial cell wall synthesis. Nature 533 :557-560. PubMed Id: 27088606. doi:10.1038/nature17636.
*MraY translocase in complex with carbacaprazamycin: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.95 Å** in complex with capuramycin, 3.62 Å: 6OYZ in complex with 3'-hydroxymureidomycin A, 3.7 Å: 6OZ6	6OYH	Data File Jmol Viewer 6OYH 6OZ6 6OYZ	Mashalidis et al. (2019). Mashalidis EH, Kaeser B, Terasawa Y, Katsuyama A, Kwon DY, Lee K, Hong J, Ichikawa S, & Lee SY (2019). Chemical logic of MraY inhibition by antibacterial nucleoside natural products. Nat Commun 10 1. PubMed Id: 31266949. doi:10.1038/s41467-019-10957-9.
*MraY phospho-MurNAc-pentapeptide translocase in complex with tunicamycin: Clostridium bolteae* B Bacteria (expressed in E. coli), 2.60 Å**	5JNQ	Data File Jmol Viewer 5JNQ	Hakulinen et al. (2017). Hakulinen JK, Hering J, Brändén G, Chen H, Snijder A, Ek M, & Johansson P (2017). MraY-antibiotic complex reveals details of tunicamycin mode of action. Nat Chem Biol 13 3:265-267. PubMed Id: 28068312. doi:10.1038/nchembio.2270.
*MraY-Protein E_ID21-SlyD "YES_ID21" complex: E. coli* B Bacteria, 3.40 Å** cryo-EM structure MraY-Protein E_ΦX174-SlyD "YES_ΦX174" complex, 3.50 Å: 8G02	8G01	Data File Jmol Viewer 8G01 8G02	Orta et al. (2023). Orta AK, Riera N, Li YE, Tanaka S, Yun HG, Klaic L, & Clemons WM Jr (2023). The mechanism of the phage-encoded protein antibiotic from ΦX174. Science 381 6654:eadg9091. PubMed Id: 37440661. doi:10.1126/science.adg9091.
Shape, Elongation, Division, and Sporulation (SEDS) Proteins
*RodA peptidoglycan polymerase: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.91 Å** D255A mutant, 3.19 Å: 6BAS	6BAR	Data File Jmol Viewer 6BAR 6BAS	Sjodt et al. (2018). Sjodt M, Brock K, Dobihal G, Rohs PDA, Green AG, Hopf TA, Meeske AJ, Srisuknimit V, Kahne D, Walker S, Marks DS, Bernhardt TG, Rudner DZ, & Kruse AC (2018). Structure of the peptidoglycan polymerase RodA resolved by evolutionary coupling analysis. Nature 556 7699:118-121. PubMed Id: 29590088. doi:10.1038/nature25985.
Oligosaccharyltransferases (OST) Catalyses Asparagine-linked (N-linked) Glycosylation
*PglB OST in complex with acceptor peptide: Campylobacter lari* B Bacteria (expressed in E. coli), 3.40 Å**	3RCE	Data File Jmol Viewer 3RCE	Lizak et al. (2011). Lizak C, Gerber S, Numao S, Aebi M, & Locher KP (2011). X-ray structure of a bacterial oligosaccharyltransferase. Nature 474 :350-355. PubMed Id: 21677752. doi:10.1038/nature10151.
*PglB OST in complex trapped in an intermediate state: Campylobacter lari* B Bacteria (expressed in E. coli), 2.7 Å** bound to acceptor peptide and a synthetic lipid-linked oligosaccharide (LLO)	5OGL	Data File Jmol Viewer 5OGL	Napiórkowska et al. (2017). Napiórkowska M, Boilevin J, Sovdat T, Darbre T, Reymond JL, Aebi M, & Locher KP (2017). Molecular basis of lipid-linked oligosaccharide recognition and processing by bacterial oligosaccharyltransferase. Nat Struct Mol Biol 24 12:1100-1106. PubMed Id: 29058712. doi:10.1038/nsmb.3491.
*PglB OST in complex with an inhibitory peptide and a reactive lipid-linked oligosaccharide analog: Campylobacter lari* B Bacteria (expressed in E. coli), 3.40 Å**	6GXC	Data File Jmol Viewer 6GXC	Napiórkowska et al. (2018). Napiórkowska M, Boilevin J, Darbre T, Reymond JL, & Locher KP (2018). Structure of bacterial oligosaccharyltransferase PglB bound to a reactive LLO and an inhibitory peptide. Sci Rep 8 1:16297. PubMed Id: 30389987. doi:10.1038/s41598-018-34534-0.
*AglB OST with bound zinc & sulfate (C2 space group): Archaeoglobus fulgidus* A Archaea (expressed in E. coli), 2.50 Å** P4₃2₁2 space group, 3.41 Å: 3WAK	3WAJ	Data File Jmol Viewer 3WAJ 3WAK	Matsumoto et al. (2013). Matsumoto S, Shimada A, Nyirenda J, Igura M, Kawano Y, & Kohda D (2013). Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation. Proc Natl Acad Sci USA 110 :17868-17873. PubMed Id: 24127570. doi:10.1073/pnas.1309777110 .
*AglB OST with bound acceptor peptide: Archaeoglobus fulgidus* A Archaea (expressed in E. coli), 3.50 Å**	5GMY	Data File Jmol Viewer 5GMY	Matsumoto et al. (2017). Matsumoto S, Taguchi Y, Shimada A, Igura M, & Kohda D (2017). Tethering an N-Glycosylation Sequon-Containing Peptide Creates a Catalytically Competent Oligosaccharyltransferase Complex. Biochemistry 56 4:602-611. PubMed Id: 27997792. doi:10.1021/acs.biochem.6b01089.
*AglB OST with bound acceptor peptide and a dolichol-phosphate: Archaeoglobus fulgidus* A Archaea (expressed in E. coli), 2.70 Å**	7E9S	Data File Jmol Viewer 7E9S	Taguchi et al. (2021). Taguchi Y, Yamasaki T, Ishikawa M, Kawasaki Y, Yukimura R, Mitani M, Hirata K, & Kohda D (2021). The structure of an archaeal oligosaccharyltransferase provides insight into the strict exclusion of proline from the N-glycosylation sequon. Commun Biol 4 1:941. PubMed Id: 34354228. doi:10.1038/s42003-021-02473-8.
*Eukaryotic oligosaccharyltransferase Complex: Saccharomyces cerevisiae* E Eukaryota, 3.3 Å** cryo-EM structure This is the first eukaryotic OST complex structure.	6EZN	Data File Jmol Viewer 6EZN	Wild et al. (2018). Wild R, Kowal J, Eyring J, Ngwa EM, Aebi M, & Locher KP (2018). Structure of the yeast oligosaccharyltransferase complex gives insight into eukaryotic N-glycosylation. Science 359 6375:545-550. PubMed Id: 29301962. doi:10.1126/science.aar5140.
*Eukaryotic oligosaccharyltransferase Complex: Saccharomyces cerevisiae* E Eukaryota, 3.5 Å** cryo-EM structure	6C26	Data File Jmol Viewer 6C26	Bai et al. (2018). Bai L, Wang T, Zhao G, Kovach A, & Li H (2018). The atomic structure of a eukaryotic oligosaccharyltransferase complex. Nature 555 7696:328-333. PubMed Id: 29466327. doi:10.1038/nature25755.
*Oligosaccharyltransferase Complex containing Ost6p: Saccharomyces cerevisiae* E Eukaryota, 3.46 Å** cryo-EM structure	7OCI	Data File Jmol Viewer 7OCI	Neuhaus et al. (2021). Neuhaus JD, Wild R, Eyring J, Irobalieva RN, Kowal J, Lin CW, Locher KP, & Aebi M (2021). Functional analysis of Ost3p and Ost6p containing yeast oligosaccharyltransferases. Glycobiology 31 12:1604-1615. PubMed Id: 34974622. doi:10.1093/glycob/cwab084.
*Oligosaccharyltransferase A (OST-A): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.5 Å** cryo-EM structure Oligosaccharyltransferase B (OST-B), 3.5 Å: 6S7T	6S7O	Data File Jmol Viewer 6S7O 6S7T	Ramírez et al. (2019). Ramírez AS, Kowal J, & Locher KP (2019). Cryo-electron microscopy structures of human oligosaccharyltransferase complexes OST-A and OST-B. Science 366 6471:1372-1375. PubMed Id: 31831667. doi:10.1126/science.aaz3505.
Protein O-mannosyltransferases (POMT/PMT) POMT in mammals or PMT in yeast
*protein O-mannosyltransferase Pmt1-Pmt2 complex, bound to sugar donor: Saccharomyces cerevisiae* E Eukaryota, 3.2 Å** cryo-EM structure bound to the sugar donor and a peptide acceptor, 3.2 Å: 6P25 structure of the MIR domain (aa 337-532) by x-ray diffraction, 1.35 Å: 6P28	6P2R	Data File Jmol Viewer 6P2R 6P25 6P28	Bai et al. (2019). Bai L, Kovach A, You Q, Kenny A, & Li H (2019). Structure of the eukaryotic protein O-mannosyltransferase Pmt1-Pmt2 complex. Nat Struct Mol Biol 26 8:704-711. PubMed Id: 31285605. doi:10.1038/s41594-019-0262-6.
*O-mannosyltransferase Pmt2 MIR domain with bound ligands: Saccharomyces cerevisiae* E Eukaryota (expressed in E. coli), 1.60 Å** Pmt3 MIR domain with bound ligands, 1.90 Å: 6ZQQ	6ZQP	Data File Jmol Viewer 6ZQP 6ZQQ	Chiapparino et al. (2020). Chiapparino A, Grbavac A, Jonker HR, Hackmann Y, Mortensen S, Zatorska E, Schott A, Stier G, Saxena K, Wild K, Schwalbe H, Strahl S, & Sinning I (2020). Functional implications of MIR domains in protein O-mannosylation. Elife 9 :e61189. PubMed Id: 33357379. doi:10.7554/eLife.61189.
Glycosyltransfereases
*GtrB polyisoprenyl-glycosyltransferase (PI-GT): Synechocystis sp. PCC6803* B Bacteria (expressed in E. coli), 3.19 Å** F215A mutant, 3.0 Å: 5EKE	5EKP	Data File Jmol Viewer 5EKP 5EKE	Ardiccioni et al. (2016). Ardiccioni C, Clarke OB, Tomasek D, Issa HA, von Alpen DC, Pond HL, Banerjee S, Rajashankar KR, Liu Q, Guan Z, Li C, Kloss B, Bruni R, Kloppmann E, Rost B, Manzini MC, Shapiro L, & Mancia F (2016). Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun 7 :10175. PubMed Id: 26729507. doi:10.1038/ncomms10175.
*ArnT glycosyltransferase, apo form: Cupriavidus metallidurans* B Bacteria (expressed in E. coli), 2.7 Å** This is a lipid-to-lipid glycosyltransferase. with bound lipid carrier undecaprenyl phosphate, 3.2 Å: 5F15	5EZM	Data File Jmol Viewer 5EZM 5F15	Petrou et al. (2016). Petrou VI, Herrera CM, Schultz KM, Clarke OB, Vendome J, Tomasek D, Banerjee S, Rajashankar KR, Belcher Dufrisne M, Kloss B, Kloppmann E, Rost B, Klug CS, Trent MS, Shapiro L, & Mancia F (2016). Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation. Science 351 :608-612. PubMed Id: 26912703. doi:10.1126/science.aad1172.
*RodA-PBP2 peptidoglycan synthase complex: Thermus thermophilus* B Bacteria, 3.50 Å** RodA (D255A)-PBP2 variant complex, 3.30 Å: 6PL6	6PL5	Data File Jmol Viewer 6PL5 6PL6	Sjodt et al. (2020). Sjodt M, Rohs PDA, Gilman MSA, Erlandson SC, Zheng S, Green AG, Brock KP, Taguchi A, Kahne D, Walker S, Marks DS, Rudner DZ, Bernhardt TG, & Kruse AC (2020). Structural coordination of polymerization and crosslinking by a SEDS-bPBP peptidoglycan synthase complex. Nat Microbiol 5 6:813-820. PubMed Id: 32152588. doi:10.1038/s41564-020-0687-z.
*RodA-PBP2 peptidoglycan synthase complex: Escherichia coli* B Bacteria (expressed in E. coli), 3.20 Å** cryo-EM structure	8TJ3	Data File Jmol Viewer 8TJ3	Nygaard et al. (2023). Nygaard R, Graham CLB, Belcher Dufrisne M, Colburn JD, Pepe J, Hydorn MA, Corradi S, Brown CM, Ashraf KU, Vickery ON, Briggs NS, Deering JJ, Kloss B, Botta B, Clarke OB, Columbus L, Dworkin J, Stansfeld PJ, Roper DI, & Mancia F (2023). Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2 complex. Nat Commun 14 1:5151. PubMed Id: 37620344. doi:10.1038/s41467-023-40483-8.
*Arabinosyltransferase EmbA-EmbB-AcpM2 in complex with ethambutol: Mycolicibacterium smegmatis* B Bacteria, 2.90 Å** cryo-EM structure in complex with di-arabinose, 3.10 Å: 7BVG EmbC2-AcpM2 in complex with ethambutol, 2.81 Å: 7BVE EmbC2-AcpM2 complexed with di-arabinose, 3.30 Å: 7BVH	7BVC	Data File Jmol Viewer 7BVC 7BVH 7BVE 7BVG	Zhang et al. (2020). Zhang L, Zhao Y, Gao Y, Wu L, Gao R, Zhang Q, Wang Y, Wu C, Wu F, Gurcha SS, Veerapen N, Batt SM, Zhao W, Qin L, Yang X, Wang M, Zhu Y, Zhang B, Bi L, Zhang X, Yang H, Guddat LW, Xu W, Wang Q, Li J, Besra GS, & Rao Z (2020). Structures of cell wall arabinosyltransferases with the anti-tuberculosis drug ethambutol. Science 368 6496:1211-1219. PubMed Id: 32327601. doi:10.1126/science.aba9102.
*EmbB Arabinosyltransferase: Mycobacterium smegmatis* B Bacteria (expressed in E. coli), 3.30 Å** cryo-EM structure	6X0O	Data File Jmol Viewer 6X0O	Tan et al. (2020). Tan YZ, Rodrigues J, Keener JE, Zheng RB, Brunton R, Kloss B, Giacometti SI, Rosário AL, Zhang L, Niederweis M, Clarke OB, Lowary TL, Marty MT, Archer M, Potter CS, Carragher B, & Mancia F (2020). Cryo-EM structure of arabinosyltransferase EmbB from Mycobacterium smegmatis. Nat Commun 11 1:3396. PubMed Id: 32636380. doi:10.1038/s41467-020-17202-8.
*Arabinosyltransferase EmbA-EmbB-AcpM2 in complex with ethambutol: Mycobacterium tuberculosis* B Bacteria (expressed in Mycolicibacterium smegmatis), 2.97 Å** cryo-EM structure	7BVF	Data File Jmol Viewer 7BVF	Zhang et al. (2020). Zhang L, Zhao Y, Gao Y, Wu L, Gao R, Zhang Q, Wang Y, Wu C, Wu F, Gurcha SS, Veerapen N, Batt SM, Zhao W, Qin L, Yang X, Wang M, Zhu Y, Zhang B, Bi L, Zhang X, Yang H, Guddat LW, Xu W, Wang Q, Li J, Besra GS, & Rao Z (2020). Structures of cell wall arabinosyltransferases with the anti-tuberculosis drug ethambutol. Science 368 6496:1211-1219. PubMed Id: 32327601. doi:10.1126/science.aba9102.
*ManGT Mannosyltransferase: Pyrobaculum calidifontis* A Archaea (expressed in E. coli), 2.70 Å** in complex with GDP and Mn²⁺, 2.60 Å: 6YV8 in complex with GDP-Man and Mn²⁺, 2.70 Å: 6YV9	6YV7	Data File Jmol Viewer 6YV7 6YV8 6YV9	Gandini et al. (2020). Gandini R, Reichenbach T, Spadiut O, Tan TC, Kalyani DC, & Divne C (2020). A Transmembrane Crenarchaeal Mannosyltransferase Is Involved in N-Glycan Biosynthesis and Displays an Unexpected Minimal Cellulose-Synthase-like Fold. J Mol Biol 432 :4658-4672. PubMed Id: 32569746. doi:10.1016/j.jmb.2020.06.016.
*WaaL O-antigen ligase, ligand-bound state: Cupriavidus metallidurans* B Bacteria (expressed in E. coli), 3.23 Å** cryo-EM structure apo state, 3.46 Å 7TPJ	7TPG	Data File Jmol Viewer 7TPG 7TPJ	Ashraf et al. (2022). Ashraf KU, Nygaard R, Vickery ON, Erramilli SK, Herrera CM, McConville TH, Petrou VI, Giacometti SI, Dufrisne MB, Nosol K, Zinkle AP, Graham CLB, Loukeris M, Kloss B, Skorupinska-Tudek K, Swiezewska E, Roper DI, Clarke OB, Uhlemann AC, Kossiakoff AA, Trent MS, Stansfeld PJ, & Mancia F (2022). Structural basis of lipopolysaccharide maturation by the O-antigen ligase. Nature 604 7905:371-376. PubMed Id: 35388216. doi:10.1038/s41586-022-04555-x.
*Chitin synthase (CHS) 1: Phytophthora sojae* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure E495A mutant complexed with UDP-GlcNAc, 3.30 Å: 7WJN complexed with the nascent chitooligosaccharide, 3.90 Å: 7X05 complexed with UDP, 3.10 Å: 7X06 complexed with nikkomycin Z, 3.20 Å: 7WJO	7WJM	Data File Jmol Viewer 7WJM 7WJO 7X06 7WJN 7X05	Chen et al. (2022). Chen W, Cao P, Liu Y, Yu A, Wang D, Chen L, Sundarraj R, Yuchi Z, Gong Y, Merzendorfer H, & Yang Q (2022). Structural basis for directional chitin biosynthesis. Nature 610 7931:402-408. PubMed Id: 36131020. doi:10.1038/s41586-022-05244-5.
Glucosyltransferases
*ALG6 glucosyltransferase in nanodiscs: Saccharomyces cerevisiae* E Eukaryota (expressed in S. frugiperda), 3 Å** cryo-EM structure in complex with Dol25-P-Glc, 3.9 Å: 6SNH	6SNI	Data File Jmol Viewer 6SNI 6SNH	Bloch et al. (2020). Bloch JS, Pesciullesi G, Boilevin J, Nosol K, Irobalieva RN, Darbre T, Aebi M, Kossiakoff AA, Reymond JL, & Locher KP (2020). Structure and mechanism of the ER-based glucosyltransferase ALG6. Nature 579 7799:443-447. PubMed Id: 32103179. doi:10.1038/s41586-020-2044-z.
Chain Length Determinant and Associated Proteins Chain-length determinant protein involved in lipopolysaccharide synthesis
*Oligomeric Wzz protein: Escherichia coli* B Bacteria, 9 Å** cryo-EM structure	5NBZ	Data File Jmol Viewer 5NBZ	Collins et al. (2017). Collins RF, Kargas V, Clarke BR, Siebert CA, Clare DK, Bond PJ, Whitfield C, & Ford RC (2017). Full-length, Oligomeric Structure of Wzz Determined by Cryoelectron Microscopy Reveals Insights into Membrane-Bound States. Structure 25 5:806-815.e3. PubMed Id: 28434914. doi:10.1016/j.str.2017.03.017.
*WzzB co-polymerase component of the Wzy-dependent pathway: Escherichia coli* B Bacteria, 3.00 Å** cryo-EM structure	6RBG	Data File Jmol Viewer 6RBG	Wiseman et al. (2021). Wiseman B, Nitharwal RG, Widmalm G, & Högbom M (2021). Structure of a full-length bacterial polysaccharide co-polymerase. Nat Commun 12 1:369. PubMed Id: 33446644. doi:10.1038/s41467-020-20579-1.
*Wzc capsule assembly protein, K540M C1: Escherichia coli* B Bacteria, 2.85 Å** cryo-EM structure Wzc K540M C8, 2.30 Å 7NHS Wzc-K540M MgADP C1, 2.88 Å 7NII Wzc-K540M MgADP C8, 2.60 Å 7NIH Wzc-K540M-4YE C1, 3.51 Å 7NIB Wzc-K540M-4YE C8, 2.89 Å 7NI2	7NHR	Data File Jmol Viewer 7NHR 7NII 7NI2 7NIH 7NHS 7NIB	Yang et al. (2021). Yang Y, Liu J, Clarke BR, Seidel L, Bolla JR, Ward PN, Zhang P, Robinson CV, Whitfield C, & Naismith JH (2021). The molecular basis of regulation of bacterial capsule assembly by Wzc. Nat Commun 12 1:4349. PubMed Id: 34272394. doi:10.1038/s41467-021-24652-1.
Phospholipid Synthases
*PgsA1 phosphatidylinositol phosphate synthase, apo form: Mycobacterium tuberculosis* B Bacteria (expressed in E. coli), 2.9 Å** with bound CDP-DAG, 1.8 Å: 6H59 in complex with manganese and citrate, 1.88 Å: 6H5A	6H53	Data File Jmol Viewer 6H53 6H59 6H5A	Grãve et al. (2019). Grãve K, Bennett MD, & Högbom M (2019). Structure of Mycobacterium tuberculosis phosphatidylinositol phosphate synthase reveals mechanism of substrate binding and metal catalysis. Commun Biol 2 :175. PubMed Id: 31098408. doi:10.1038/s42003-019-0427-1.
*PgsA phosphatidylinositol phosphate synthase in complex with phosphatidylglycerol phosphate: Staphylococcus aureus* B Bacteria (expressed in E. coli), 2.50 Å** in complex with cytidine diphosphate-diacylglycerol, 3.00 Å 7DRK	7DRJ	Data File Jmol Viewer 7DRJ 7DRK	Yang et al. (2021). Yang B, Yao H, Li D, & Liu Z (2021). The phosphatidylglycerol phosphate synthase PgsA utilizes a trifurcated amphipathic cavity for catalysis at the membrane-cytosol interface. Curr Res Struct Biol 3 :312-323. PubMed Id: 34901881. doi:10.1016/j.crstbi.2021.11.005.
Diacylglyceryl Transferases
*Phosphatidylglycerol:prolipoprotein diacylglyceryl transferase (Lgt) in complex with phosphatidylglycerol: Escherichia coli* B Bacteria, 1.9 Å** in complex with palmitic acid inhibitor, 1.6 Å: 5AZB	5AZC	Data File Jmol Viewer 5AZC 5AZB	Mao et al. (2016). Mao G, Zhao Y, Kang X, Li Z, Zhang Y, Wang X, Sun F, Sankaran K, & Zhang XC (2016). Crystal structure of E. coli lipoprotein diacylglyceryl transferase. Nat Commun 7 . PubMed Id: 26729647. doi:10.1038/ncomms10198.
Liponucleotide Synthetases Cytidine-Diphosphate Diacylglycerol Synthetase is the prominent member of the family
*CDP-DAG synthetase, S200C/S258C active mutant: Thermotoga maritima* B Bacteria (expressed in E. coli), 3.4 Å** S200C/S223C inactive mutant, 3.4 Å:	4Q2E	Data File Jmol Viewer 4Q2E	Liu et al. (2014). Liu X, Yin Y, Wu J, & Liu Z (2014). Structure and mechanism of an intramembrane liponucleotide synthetase central for phospholipid biosynthesis. Nat Commun 5 :4244. PubMed Id: 24968740. doi:10.1038/ncomms5244.
N-acyltransferases
*Lnt apoplipoprotein N-acyltransferase: Escherichia coli* B Bacteria, 2.90 Å** C387A mutant, 2.90 Å: 5N6L	5N6H	Data File Jmol Viewer 5N6H 5N6L	Wiktor et al. (2017). Wiktor M, Weichert D, Howe N, Huang CY, Olieric V, Boland C, Bailey J, Vogeley L, Stansfeld PJ, Buddelmeijer N, Wang M, & Caffrey M (2017). Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis. Nat Commun 8 :15952. PubMed Id: 28675161. doi:10.1038/ncomms15952.
*Lnt apoplipoprotein N-acyltransferase: Escherichia coli* B Bacteria, 2.59 Å**	5XHQ	Data File Jmol Viewer 5XHQ	Lu et al. (2017). Lu G, Xu Y, Zhang K, Xiong Y, Li H, Cui L Wang X, Lou J, Zhai Y Sun F, & Zhang XC (2017). Crystal structure of E. coli apolipoprotein N-acyl transferase Nature Comms 18 :15948. PubMed Id: 28885614. doi:10.1038/ncomms15948.
*Lnt apoplipoprotein N-acyltransferase, Thioester acyl-intermediate: Escherichia coli* B Bacteria, 3.5 Å** Apo form, 3.1 Å: 6Q3A	6NWR	Data File Jmol Viewer 6NWR 6Q3A	Wiseman & Högbom (2020). Wiseman B, & Högbom M (2020). Conformational changes in Apolipoprotein N-acyltransferase (Lnt). Sci Rep 10 1. PubMed Id: 31959792. doi:10.1038/s41598-020-57419-7.
*Lnt apolipoprotein N-acyltransferase, apo: Escherichia coli* B Bacteria, 3.00 Å** cryo-EM structure in complex with PE, 3.13 Å: 8B0L in complex with PE-C387S, 3.01 Å: 8B0M in complex with lyso-PE, 2.67 Å: 8B0N in complex with FP3, 3.02 Å: 8B0O in complex with Pam3, 2.86 Å: 8B0P X-ray Structures: in complex with TITC and lyso-PE, in surfo (vapor diffusion) crystallization, 2.62 Å: 8AQ4 in complex with PE, in surfo crystallization, 2.40 Å: 8AQ3	8B0K	Data File Jmol Viewer 8B0K 8B0M 8B0N 8B0P 8AQ4 8B0L 8B0O 8AQ3	Smithers et al. (2023). Smithers L, Degtjarik O, Weichert D, Huang CY, Boland C, Bowen K, Oluwole A, Lutomski C, Robinson CV, Scanlan EM, Wang M, Olieric V, Shalev-Benami M, & Caffrey M (2023). Structure snapshots reveal the mechanism of a bacterial membrane lipoprotein N-acyltransferase. Sci Adv 9 26:eadf5799. PubMed Id: 37390210. doi:10.1126/sciadv.adf5799.
*Lnt apoplipoprotein N-acyltransferase in 7.10 monoacylglycerol (MAG): Escherichia coli* E Eukaryota, 2.19 Å** X-ray structure	8RQR	Data File Jmol Viewer 8RQR	Krawinski et al. (2024). Krawinski P, Smithers L, van Dalsen L, Boland C, Ostrovitsa N, Pérez J, & Caffrey M (2024). 7.10 MAG. A Novel Host Monoacylglyceride for In Meso (Lipid Cubic Phase) Crystallization of Membrane Proteins. Cryst Growth Des 24 7:2985-3001. PubMed Id: 38585376. doi:10.1021/acs.cgd.4c00087.
*Lnt apoplipoprotein N-acyltransferase: Pseudomonas aeruginosa* B Bacteria, 3.10 Å**	5N6M	Data File Jmol Viewer 5N6M	Wiktor et al. (2017). Wiktor M, Weichert D, Howe N, Huang CY, Olieric V, Boland C, Bailey J, Vogeley L, Stansfeld PJ, Buddelmeijer N, Wang M, & Caffrey M (2017). Structural insights into the mechanism of the membrane integral N-acyltransferase step in bacterial lipoprotein synthesis. Nat Commun 8 :15952. PubMed Id: 28675161. doi:10.1038/ncomms15952.
*Lnt apolipoprotein N-acyltransferase, covalently linked with TITC, in meso (LCP) crystallization: P. aeruginosa* B Bacteria, 2.60 Å**	8AQ2	Data File Jmol Viewer 8AQ2	Smithers et al. (2023). Smithers L, Degtjarik O, Weichert D, Huang CY, Boland C, Bowen K, Oluwole A, Lutomski C, Robinson CV, Scanlan EM, Wang M, Olieric V, Shalev-Benami M, & Caffrey M (2023). Structure snapshots reveal the mechanism of a bacterial membrane lipoprotein N-acyltransferase. Sci Adv 9 26:eadf5799. PubMed Id: 37390210. doi:10.1126/sciadv.adf5799.
O-acyltransferases Membrane-bound O-acyltransferases (MBOATS)
*DltB O-acyltransferase, crystal form I: Streptococcus thermophilus* B Bacteria (expressed in E. coli), 3.27 Å** crystal form II, 3.15 Å: 6BUH crystal form III, 3.27 Å: 6BUI	6BUG	Data File Jmol Viewer 6BUG 6BUI 6BUH	Ma et al. (2018). Ma D, Wang Z, Merrikh CN, Lang KS, Lu P, Li X, Merrikh H, Rao Z, & Xu W (2018). Crystal structure of a membrane-bound O-acyltransferase. Nature 562 7726:286-290. PubMed Id: 30283133. doi:10.1038/s41586-018-0568-2.
*diacylglycerol O-acyltransferase 1 (DGAT1), oleoyl-CoA free: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.00 Å** Cryo-EM structure complexed with acyl-CoA, 3.20 Å: 6VZ1	6VYI	Data File Jmol Viewer 6VYI 6VZ1	Sui et al. (2020). Sui X, Wang K, Gluchowski NL, Elliott SD, Liao M, Walther TC, & Farese RV Jr (2020). Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme. Nature 581 7808:323-328. PubMed Id: 32433611. doi:10.1038/s41586-020-2289-6.
*diacylglycerol O-acyltransferase 1 (DGAT1) in complex with oleoyl-CoA: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.10 Å** cryo-EM structure	6VP0	Data File Jmol Viewer 6VP0	Wang et al. (2020). Wang L, Qian H, Nian Y, Han Y, Ren Z, Zhang H, Hu L, Prasad BVV, Laganowsky A, Yan N, & Zhou M (2020). Structure and mechanism of human diacylglycerol O-acyltransferase 1. Nature 581 7808:329-332. PubMed Id: 32433610. doi:10.1038/s41586-020-2280-2.
*diacylglycerol O-acyltransferase 1 (DGAT1) with bound T863 inhibitor: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure with bound DGAT1IN1 inhibitor, 3.20 Å: 8ETM	8ESM	Data File Jmol Viewer 8ESM 8ETM	Sui et al. (2023). Sui X, Wang K, Song K, Xu C, Song J, Lee CW, Liao M, Farese RV Jr, & Walther TC (2023). Mechanism of action for small-molecule inhibitors of triacylglycerol synthesis. Nat Commun 14 1:3100. PubMed Id: 37248213. doi:10.1038/s41467-023-38934-3.
*sterol O-acyltransferase (ACAT1), nevanimibe-bound: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.67 Å** cryo-EM structure	6VUM	Data File Jmol Viewer 6VUM	Long et al. (2020). Long T, Sun Y, Hassan A, Qi X, & Li X (2020). Structure of nevanimibe-bound tetrameric human ACAT1. Nature 581 7808:339-343. PubMed Id: 32433613. doi:10.1038/s41586-020-2295-8.
*sterol O-acyltransferase (ACAT1), dimer: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure tetramer, 3.10 Å: 6P2P	6P2J	Data File Jmol Viewer 6P2J 6P2P	Qian et al. (2020). Qian H, Zhao X, Yan R, Yao X, Gao S, Sun X, Du X, Yang H, Wong CCL, & Yan N (2020). Structural basis for catalysis and substrate specificity of human ACAT1. Nature 581 7808:333-338. PubMed Id: 32433614. doi:10.1038/s41586-020-2290-0.
*sterol O-acyltransferase (ACAT1, SOAT1) in complex with CI-976: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure in resting state, 3.50 Å: 6L48	6L47	Data File Jmol Viewer 6L47 6L48	Guan et al. (2020). Guan C, Niu Y, Chen SC, Kang Y, Wu JX, Nishi K, Chang CCY, Chang TY, Luo T, & Chen L (2020). Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor. Nat Commun 11 1:2478. PubMed Id: 32424158. doi:10.1038/s41467-020-16288-4.
*sterol O-acyltransferase (ACAT2) with bound PPPA: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.87 Å** cryo-EM structure nevanimibe bound, 3.93 Å 7N6R	7N6Q	Data File Jmol Viewer 7N6Q 7N6R	Long et al. (2021). Long T, Liu Y, & Li X (2021). Molecular structures of human ACAT2 disclose mechanism for selective inhibition. Structure 29 12:1410-1418.e4. PubMed Id: 34520735. doi:10.1016/j.str.2021.07.009.
*Hedgehog acyltransferase (HHAT) in complex with palmitoyl-CoA: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.70 Å** cryo-EM structure in complex with a palmitoylated Hedgehog peptide, 3.20 Å: 7MHZ	7MHY	Data File Jmol Viewer 7MHY 7MHZ	Jiang et al. (2021). Jiang Y, Benz TL, & Long SB (2021). Substrate and product complexes reveal mechanisms of Hedgehog acylation by HHAT. Science 372 6547:1215-1219. PubMed Id: 34112694. doi:10.1126/science.abg4998.
*Hedgehog acyltransferase (HHAT) in complex with megabody 177 bound to non-hydrolysable palmitoyl-CoA (Composite Map): Homo sapiens* E Eukaryota (expressed in Homo sapiens), 2.70 Å** cryo-EM structure in complex with megabody 177 bound to IMP-1575, 3.59 Å: 7Q6Z	7Q1U	Data File Jmol Viewer 7Q1U 7Q6Z	Coupland et al. (2021). Coupland CE, Andrei SA, Ansell TB, Carrique L, Kumar P, Sefer L, Schwab RA, Byrne EFX, Pardon E, Steyaert J, Magee AI, Lanyon-Hogg T, Sansom MSP, Tate EW, & Siebold C (2021). Structure, mechanism, and inhibition of Hedgehog acyltransferase. Mol Cell 81 24:5025-5038.e10. PubMed Id: 34890564. doi:10.1016/j.molcel.2021.11.018.
*PORCN (Porcupine) in complex with Palmitoleoyl-CoA: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.11 Å** cryo-EM structure in complex with LGK974, 3.14 Å: 7URC in complex with LGK974 and WNT3A peptide, 2.92 Å: 7URD in complex with palmitoleoylated WNT3A peptide, 3.19 Å: 7URE HHAT H379C in complex with SHH N-terminal peptide, 2.80 Å: 7URF	7URA	Data File Jmol Viewer 7URA 7URD 7URE 7URC 7URF	Liu et al. (2022). Liu Y, Qi X, Donnelly L, Elghobashi-Meinhardt N, Long T, Zhou RW, Sun Y, Wang B, & Li X (2022). Mechanisms and inhibition of Porcupine-mediated Wnt acylation. Nature 607 7920:816-822. PubMed Id: 35831507. doi:10.1038/s41586-022-04952-2.
*Membrane-bound O-acyltransferase 7 (MBOAT7): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.70 Å** cryo-EM structure	8ERC	Data File Jmol Viewer 8ERC	Wang et al. (2023). Wang K, Lee CW, Sui X, Kim S, Wang S, Higgs AB, Baublis AJ, Voth GA, Liao M, Walther TC, & Farese RV Jr (2023). The structure of phosphatidylinositol remodeling MBOAT7 reveals its catalytic mechanism and enables inhibitor identification. Nat Commun 14 1:3533. PubMed Id: 37316513. doi:10.1038/s41467-023-38932-5.
O-Phosphatidyl Transferases
*phosphatidyl serine synthase (PSS); closed conformation with bound citrate: Methanocaldococcus jannaschii* B Bacteria (expressed in E. coli), 2.20 Å** in closed conformation with bound citrate, 1.85 Å 7B1L in transition state, 2.51 Å 7POW closed conformation with bound citrate, 2.80 Å 7B1N	7B1K	Data File Jmol Viewer 7B1K 7B1N 7B1L 7POW	Centola et al. (2021). Centola M, van Pee K, Betz H, & Yildiz Ö (2021). Crystal structures of phosphatidyl serine synthase PSS reveal the catalytic mechanism of CDP-DAG alcohol O-phosphatidyl transferases. Nat Commun 12 1:6982. PubMed Id: 34848707. doi:10.1038/s41467-021-27281-w.
S-acyltransferases Eukaryotic proteins that catalyze protein palmitoylation
*DHHC palmitoyltransferase, P2₁ space group: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 2.95 Å** DHHC = Asp-His-His-Cys P6₃ space group, 2.25 Å: 6BMN irreversibly inhibited by 2-bromopalmitate, 2.95 Å: 6BML Palmitoyltransferase from Danio rerio, 2.44 Å: 6BMS	6BML	Data File Jmol Viewer 6BML 6BMS 6BMN 6BML	Rana et al. (2018). Rana MS, Kumar P, Lee CJ, Verardi R, Rajashankar KR, & Banerjee A (2018). Fatty acyl recognition and transfer by an integral membrane S-acyltransferase. Science 359 6372:eaao6326. PubMed Id: 29326245. doi:10.1126/science.aao6326.
*Serine palmitoyltransferase (SPT) in complex with ORMDL3, dimer: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.80 Å** cryo-EM structure monomeric SPT-ORMDL3 complex, 3.40 Å: 6M4O substrate-bound SPT-ORMDL3 complex; monomer class I, 3.20 Å: 7CQI substrate-bound SPT-ORMDL3 complex; monomer class II, 3.30 Å: 7CQK	6M4N	Data File Jmol Viewer 6M4N 7CQK 7CQI 6M4O	Li et al. (2021). Li S, Xie T, Liu P, Wang L, & Gong X (2021). Structural insights into the assembly and substrate selectivity of human SPT-ORMDL3 complex. Nat Struct Mol Biol 28 3:249-257. PubMed Id: 33558762. doi:10.1038/s41594-020-00553-7.
*serine palmitoyltransferase complex SPTLC1/SPLTC2/ssSPTa: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure SPTLC1/SPLTC2/ssSPTa protomer, 3.10 Å: 7K0J SPTLC1/SPLTC2/ssSPTa, 3KS-bound, 2.60 Å: 7K0K SPTLC1/SPLTC2/ssSPTa, myriocin-bound, 3.40 Å: 7K0L SPTLC1/SPLTC2/ssSPTa/ORMDL3, class 1, 2.90 Å: 7K0M SPTLC1/SPLTC2/ssSPTa/ORMDL3, class 2, 3.10 Å: 7K0N SPTLC1/SPLTC2/ssSPTa/ORMDL3, class 3, 3.10 Å: 7K0O SPTLC1/SPLTC2/ssSPTa/ORMDL3, class 4, 3.10 Å: 7K0P SPTLC1/SPLTC2/ssSPTa/ORMDL3, myriocin-bound, 3.30 Å: 7K0Q	7K0I	Data File Jmol Viewer 7K0I 7K0L 7K0Q 7K0M 7K0J 7K0O 7K0P 7K0K 7K0N	Wang et al. (2021). Wang Y, Niu Y, Zhang Z, Gable K, Gupta SD, Somashekarappa N, Han G, Zhao H, Myasnikov AG, Kalathur RC, Dunn TM, & Lee CH (2021). Structural insights into the regulation of human serine palmitoyltransferase complexes. Nat Struct Mol Biol 28 3:240-248. PubMed Id: 33558761. doi:10.1038/s41594-020-00551-9.
*Serine palmitoyltransferase (SPT) in complex with ORMDL3, with bound C6-ceramide: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure in complex with ORMDL3 (ΔN2 variant), apo, 3.10 Å: 7YJ1 in complex with ORMDL3 (N13A mutant), apo, 2.90 Å: 7YJ2	7YIU	Data File Jmol Viewer 7YIU 7YJ1 7YJ2	Xie et al. (2023). Xie T, Liu P, Wu X, Dong F, Zhang Z, Yue J, Mahawar U, Farooq F, Vohra H, Fang Q, Liu W, Wattenberg BW, & Gong X (2023). Ceramide sensing by human SPT-ORMDL complex for establishing sphingolipid homeostasis. Nat Commun 14 1:3475. PubMed Id: 37308477. doi:10.1038/s41467-023-39274-y.
*Serine palmitoyltransferase (SPT) in complex with ORM1, dimer: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure monomer, 3.20 Å: 7YJM in complex with ORM1 (N17A mutant), monomer, 3.40 Å: 7YJN in complex with LCB2a (ΔN5 variant), monomer, 2.80 Å: 7YJO	7YJK	Data File Jmol Viewer 7YJK 7YJO 7YJN 7YJM	Liu et al. (2023). Liu P, Xie T, Wu X, Han G, Gupta SD, Zhang Z, Yue J, Dong F, Gable K, Niranjanakumari S, Li W, Wang L, Liu W, Yao R, Cahoon EB, Dunn TM, & Gong X (2023). Mechanism of sphingolipid homeostasis revealed by structural analysis of Arabidopsis SPT-ORM1 complex. Sci Adv 9 13:eadg0728. PubMed Id: 36989369. doi:10.1126/sciadv.adg0728.
Phospholipid Transferases Includes phosphoethanolamine (PEA) transferases and cardiolipin transferases involved in the assembly of outer membranes
*Lipid A phosphoethanolamine transferase: Neisseria meningitidis* B Bacteria (expressed in E. coli), 2.75 Å**	5FGN	Data File Jmol Viewer 5FGN	Anandan et al. (2017). Anandan A, Evans GL, Condic-Jurkic K, O'Mara ML, John CM, Phillips NJ, Jarvis GA, Wills SS, Stubbs KA, Moraes I, Kahler CM, & Vrielink A (2017). Structure of a lipid A phosphoethanolamine transferase suggests how conformational changes govern substrate binding. Proc Natl Acad Sci USA 114 :2218-2223. PubMed Id: 28193899. doi:10.1073/pnas.1612927114.
*PdgA inner membrane protein involved outer membrane homeostasis: Salmonella enterica* B Bacteria, 2.70 Å**	6V8Q	Data File Jmol Viewer 6V8Q	Fan et al. (2020). Fan J, Petersen EM, Hinds TR, Zheng N, & Miller SI (2020). Structure of an Inner Membrane Protein Required for PhoPQ-Regulated Increases in Outer Membrane Cardiolipin. mBio 11 1. PubMed Id: 32047135. doi:10.1128/mBio.03277-19.
*PbgA cardiolipin transport agent in complex with lipopolysaccharide: Escherichia coli* B Bacteria, 2.00 Å**	6XLP	Data File Jmol Viewer 6XLP	Clairfeuille et al. (2020). Clairfeuille T, Buchholz KR, Li Q, Verschueren E, Liu P, Sangaraju D, Park S, Noland CL, Storek KM, Nickerson NN, Martin L, Dela Vega T, Miu A, Reeder J, Ruiz-Gonzalez M, Swem D, Han G, DePonte DP, Hunter MS, Gati C, Shahidi-Latham S, Xu M, Skelton N, Sellers BD, Skippington E, Sandoval W, Hanan EJ, Payandeh J, & Rutherford ST (2020). Structure of the essential inner membrane lipopolysaccharide-PbgA complex. Nature 584 7821:479-483. PubMed Id: 32788728. doi:10.1038/s41586-020-2597-x.
*PbgA cardiolipin transport agent, soluble domain: Escherichia coli* B Bacteria, 1.65 Å**	5I5H	Data File Jmol Viewer 5I5H	Dong et al. (2016). Dong H, Zhang Z, Tang X, Huang S, Li H, Peng B, & Dong C (2016). Structural insights into cardiolipin transfer from the Inner membrane to the outer membrane by PbgA in Gram-negative bacteria. Sci Rep 6 :30815. PubMed Id: 27487745. doi:10.1038/srep30815.
Very Long Chain Fatty Acid Elongases
*ELOVL fatty acid elongase 7 (ELOVL7): Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.05 Å**	6Y7F	Data File Jmol Viewer 6Y7F	Nie et al. (2021). Nie L, Pascoa TC, Pike ACW, Bushell SR, Quigley A, Ruda GF, Chu A, Cole V, Speedman D, Moreira T, Shrestha L, Mukhopadhyay SMM, Burgess-Brown NA, Love JD, Brennan PE, & Carpenter EP (2021). The structural basis of fatty acid elongation by the ELOVL elongases. Nat Struct Mol Biol 28 6:512-520. PubMed Id: 34117479. doi:10.1038/s41594-021-00605-6.
Methyltransferases
*Isoprenylcysteine carboxyl methyltransferase (ICMT): Methanosarcina acetivorans* A Archaea (expressed in E. coli), 3.40 Å** Catalyzes the final step of CAAX processing. The protein has 5 TM helices.	4A2N	Data File Jmol Viewer 4A2N	Yang et al. (2011). Yang J, Kulkarni K, Manolaridis I, Zhang Z, Dodd RB, Mas-Droux C, & Barford D (2011). Mechanism of Isoprenylcysteine Carboxyl Methylation from the Crystal Structure of the Integral Membrane Methyltransferase ICMT Mol Cell 44 :997-1004. PubMed Id: 22195972. doi:10.1016/j.molcel.2011.10.020.
*Isoprenylcysteine carboxyl methyltransferase (ICMT) with monobody inhibitor: Tribolium castaneum* E Eukaryota (expressed in Pichia pastoris), 2.3 Å** ICMT without nanobody, 4 Å: 5VG9	5V7P	Data File Jmol Viewer 5V7P 5VG9	Diver et al. (2018). Diver MM, Pedi L, Koide A, Koide S, & Long SB (2018). Atomic structure of the eukaryotic intramembrane RAS methyltransferase ICMT. Nature 553 :526-529. PubMed Id: 29342140. doi:10.1038/nature25439.
Phosphotransferases
*DgkA diacylglycerol kinase (DAGK): Escherichia coli* B Bacteria, NMR structure (DPC micelles)** Domain-swapped homotrimer	2KDC	Data File Jmol Viewer 2KDC	van Horn et al.. (2009). van Horn WD, Kim HJ, Ellis CD, Hadziselimovic A, Sulistijo ES, Karra MD, Tian C, Sönnichsen FD, & Sanders CR (2009). Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase. Science 324 :1726-1729. PubMed Id: 19556511.
*DgkA diacylglycerol kinase (DAGK) with bound monoacylglycerol (7.8 MAG): Escherichia coli* B Bacteria, 3.70 Å** This structure does not show domain-swapping. Δ4 mutant, 3.10 Å: 3ZE5 Δ7 mutant, 2.05 Å: 3ZE3 Δ4 mutant = I53C, I70L, M96L, V107D. Δ7 mutant = A41C, C46A, I53V, I70L, M96L, V107D, C113A.	3ZE4	Data File Jmol Viewer 3ZE4 3ZE5 3ZE3	Li et al. (2013). Li D, Lyons JA, Pye VE, Vogeley L, Aragão D, Kenyon CP, Shah ST, Doherty C, Aherne M, & Caffrey M (2013). Crystal structure of the integral membrane diacylglycerol kinase. Nature 497 :521-524. PubMed Id: 23676677.
*DgkA diacylglycerol kinase (DAGK) Δ4 mutant with bound monoacylglycerol (9.9 MAG) and ACP: Escherichia coli* B Bacteria, 2.70 Å** ACP = non-hydrolysable ATP analogue: adenylylmethylenediphosphonate Δ4 mutant with 9.9MAG, 3.15 Å: 4UXW Δ7 mutant with 7.9 MAG, 2.18 Å: 4UXZ Δ7 mutant with 7.9 MAG (by free-electron laser), 2.18 Å: 4UYO	4UXX	Data File Jmol Viewer 4UXX 4UYO 4UXZ 4UXW	Li et al. (2015). Li D, Stansfeld PJ, Sansom MS, Keogh A, Vogeley L, Howe N, Lyons JA, Aragao D, Fromme P, Fromme R, Basu S, Grotjohann I, Kupitz C, Rendek K, Weierstall U, Zatsepin NA, Cherezov V, Liu W, Bandaru S, English NJ, Gati C, Barty A, Yefanov O, Chapman HN, Diederichs K, Messerschmidt M, Boutet S, Williams GJ, Marvin Seibert M, & Caffrey M (2015). Ternary structure reveals mechanism of a membrane diacylglycerol kinase. Nat Commun 6 :10140. PubMed Id: 26673816. doi:10.1038/ncomms10140.
*Choline/ethanolamine phosphotransferase 1 (CEPT1): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.70 Å** cryo-EM structure complexed with CDP-choline, 3.90 Å: 8GYW	8GYX	Data File Jmol Viewer 8GYX 8GYW	Wang et al. (2023). Wang Z, Yang M, Yang Y, He Y, & Qian H (2023). Structural basis for catalysis of human choline/ethanolamine phosphotransferase 1. Nat Commun 14 1:2529. PubMed Id: 37137909. doi:10.1038/s41467-023-38290-2.
*Cholinephosphotransferase-1 (CEPT1) in complex with CDP-choline: Xenopus laevis* E Eukaryota (expressed in Spodoptera frugiperda), 3.70 Å** cryo-EM structure in complex with CDP, 3.20 Å: 8ERO	8ERP	Data File Jmol Viewer 8ERP 8ERO	Wang & Zhou (2023). Wang L, & Zhou M (2023). Structure of a eukaryotic cholinephosphotransferase-1 reveals mechanisms of substrate recognition and catalysis. Nat Commun 14 1:2753. PubMed Id: 37179328. doi:10.1038/s41467-023-38003-9.
Phosphatidic Acid Phosphatases Membrane-integrated type II phosphatidic acid phosphatases (PAP2)
*PgpB phosphatidylglycerophosphate phosphatase B: Escherichia coli* B Bacteria, 3.20 Å**	4PX7	Data File Jmol Viewer 4PX7	Fan et al. (2014). Fan J, Jiang D, Zhao Y, Liu J, & Zhang XC (2014). Crystal structure of lipid phosphatase Escherichia coli phosphatidylglycerophosphate phosphatase B. Proc Natl Acad Sci USA 111 :7636-7640. PubMed Id: 24821770.
*BacA (UppP) undecaprenyl-pyrophosphate phosphatase: Escherichia coli* B Bacteria, 2.6 Å**	5OON	Data File Jmol Viewer 5OON	El Ghachi et al. (2018). El Ghachi M, Howe N, Huang CY, Olieric V, Warshamanage R, Touzé T, Weichert D, Stansfeld PJ, Wang M, Kerff F, & Caffrey M (2018). Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis. Nat Commun 9 1. PubMed Id: 29540682. doi:10.1038/s41467-018-03477-5.
*BacA (UppP) undecaprenyl-pyrophosphate phosphatase: Escherichia coli* B Bacteria, 2.0 Å**	6CB2	Data File Jmol Viewer 6CB2	Workman et al. (2018). Workman SD, Worrall LJ, & Strynadka NCJ (2018). Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling. Nat Commun 9 1. PubMed Id: 29559664. doi:10.1038/s41467-018-03547-8.
UbiA Prenyltransferases These enzymes are involved in the biosynthesis of a wide range molecules, including respiratory lipoquinones and archael lipids
*UbiA prenyltransferase domain-containing 1 (UBIAD1) with bound GPP and Mg⁺²: Archaeoglobus fulgidus* A Archaea (expressed in E. coli), 2.41 Å** with bound DMAPP and Mg⁺², 2.50 Å: 4TQ4 SeMet structure, 3.20 Å: 4TQ5 with bound Cd⁺², 3.07 Å: 4TQ6	4TQ3	Data File Jmol Viewer 4TQ3 4TQ4 4TQ5 4TQ6	Huang et al. (2014). Huang H, Levin EJ, Liu S, Bai Y, Lockless SW, & Zhou M (2014). Structure of a Membrane-Embedded Prenyltransferase Homologous to UBIAD1. PLoS Biol 12 7:e1001911. PubMed Id: 25051182. doi:10.1371/journal.pbio.1001911.
*UbiA homolog with bound substrate: Aeropyrum pernix* A Archaea (expressed in E. coli), 3.56 Å** apo protein, 3.3 Å: 4OD4	4OD5	Data File Jmol Viewer 4OD5 4OD4	Cheng & Li (2014). Cheng W, & Li W (2014). Structural insights into ubiquinone biosynthesis in membranes. Science 343 6173:878-881. PubMed Id: 24558159. doi:10.1126/science.1246774.
*Digeranylgeranylglyceryl phosphate synthase (DGGGPase), with bound SeMet-DGGGP lipids: Methanocaldococcus jannaschii* B Bacteria (expressed in E. coli), 2.30 Å** apo structure, 3.32 Å: 7BPU	6M31	Data File Jmol Viewer 6M31 7BPU	Ren et al. (2020). Ren S, de Kok NAW, Gu Y, Yan W, Sun Q, Chen Y, He J, Tian L, Andringa RLH, Zhu X, Tang M, Qi S, Xu H, Ren H, Fu X, Minnaard AJ, Yang S, Zhang W, Li W, Wei Y, Driessen AJM, & Cheng W (2020). Structural and Functional Insights into an Archaeal Lipid Synthase. Cell Rep 33 3:108294. PubMed Id: 33086053. doi:10.1016/j.celrep.2020.108294.
Phosphoenolpyruvate-Dependent Phosphotransferases (PTSs)
*ChbC EIIC phosphorylation-coupled saccharide transporter: Bacillus cereus* B Bacteria (expressed in E. coli), 3.30 Å** The protein is a homodimer in an inward-facing occluded conformation. Each protomer contains a diacetylchitobiose.	3QNQ	Data File Jmol Viewer 3QNQ	Cao et al. (2011). Cao Y, Jin X, Levin EJ, Huang H, Zong Y, Quick M, Weng J, Pan Y, Love J, Punta M, Rost B, Hendrickson WA, Javitch JA, Rajashankar KR, & Zhou M (2011). Crystal structure of a phosphorylation-coupled saccharide transporter Nature 473 :50-54. PubMed Id: 21471968. doi:10.1038/nature09939.
*UlaA bacterial vitamin C transporter, C2 space group: Escherichia coli* B Bacteria, 1.65 Å** P2₁ form, 2.36 Å: 4RP8	4RP9	Data File Jmol Viewer 4RP9 4RP8	Luo et al. (2015). Luo P, Yu X, Wang W, Fan S, Li X, & Wang J (2015). Crystal structure of a phosphorylation-coupled vitamin C transporter. Nat Struct Mol Biol 22 3:238-241. PubMed Id: 25686089. doi:10.1038/nsmb.2975.
*UlaA bacterial vitamin C transporter, inward facing conformation: Pasteurella multocida* B Bacteria (expressed in Enterobacteria phage L1), 3.33 Å**	5ZOV	Data File Jmol Viewer 5ZOV	Luo et al. (2018). Luo P, Dai S, Zeng J, Duan J, Shi H, & Wang J (2018). Inward-facing conformation of l-ascorbate transporter suggests an elevator mechanism. Cell Discov 4 :35. PubMed Id: 30038796. doi:10.1038/s41421-018-0037-y.
*MalT EIIC phosphorylation-coupled maltose transporter: Bacillus cereus* B Bacteria (expressed in E. coli), 2.55 Å** The protein is in an outward-facing conformation	5IWS	Data File Jmol Viewer 5IWS	McCoy et al. (2016). McCoy JG, Ren Z, Stanevich V, Lee J, Mitra S, Levin EJ, Poget S, Quick M, Im W, & Zhou M (2016). The Structure of a Sugar Transporter of the Glucose EIIC Superfamily Provides Insight into the Elevator Mechanism of Membrane Transport. Structure 24 6:956-964. PubMed Id: 27161976. doi:10.1016/j.str.2016.04.003.
*MalT EIIC phosphorylation-coupled maltose transporter, trapped in inward-facing state: Bacillus cereus* B Bacteria (expressed in E. coli), 3.2 Å**	6BVG	Data File Jmol Viewer 6BVG	Ren et al. (2018). Ren Z, Lee J, Moosa MM, Nian Y, Hu L, Xu Z, McCoy JG, Ferreon ACM, Im W, & Zhou M (2018). Structure of an EIIC sugar transporter trapped in an inward-facing conformation. Proc Natl Acad Sci USA 115 23:5962-5967. PubMed Id: 29784777. doi:10.1073/pnas.1800647115.
*ManYZ mannose-phosphotransferease system (man-PTS): Escherichia coli* B Bacteria, 3.52 Å** cryo-EM structure	6K1H	Data File Jmol Viewer 6K1H	Liu et al. (2019). Liu X, Zeng J, Huang K, & Wang J (2019). Structure of the mannose transporter of the bacterial phosphotransferase system. Cell Res 29 8:680-682. PubMed Id: 31209249. doi:10.1038/s41422-019-0194-z.
*ManYZ mannose-phosphotransferease system (man-PTS) and Microcin E492 (MceA) complex: Escherichia coli* B Bacteria, 2.28 Å** cryo-EM structure	7DYR	Data File Jmol Viewer 7DYR	Huang et al. (2021). Huang K, Zeng J, Liu X, Jiang T, & Wang J (2021). Structure of the mannose phosphotransferase system (man-PTS) complexed with microcin E492, a pore-forming bacteriocin. Cell Discov 7 1:20. PubMed Id: 33820910. doi:10.1038/s41421-021-00253-6.
*Mannose-phosphotransferease system (man-PTS): Listeria monocytogenes* B Bacteria (expressed in E. coli), 3.12 Å** cryo-EM structure complexed with pediocin PA-1, 2.45 Å: 7VLY	7VLX	Data File Jmol Viewer 7VLX 7VLY	Zhu et al. (2022). Zhu L, Zeng J, Wang C, & Wang J (2022). Structural Basis of Pore Formation in the Mannose Phosphotransferase System by Pediocin PA-1. Appl Environ Microbiol 88 3:e01992-21. PubMed Id: 34851716. doi:10.1128/AEM.01992-21.
Intramembrane Proteases ( NSMB News & Views on three GlpG Structures)
*GlpG rhomboid-family intramembrane protease: Escherichia coli* B Bacteria, 2.1 Å** P3₂ space group. One molecule in asymmetric unit.	2IC8	Data File Jmol Viewer 2IC8 Rhomboid Protease GlpG	Wang et al. (2006). Wang Y, Zhang Y, & Ha Y (2006). Crystal structure of a rhomboid family intramembrane protease. Nature 444 :179-183. PubMed Id: 17051161.
*GlpG rhomboid-family intramembrane protease: Escherichia coli* B Bacteria, 1.90 Å** W136A mutant, 1.70 Å: 3B44	3B45	Data File Jmol Viewer 3B45 3B44	Wang et al. (2007). Wang Y, Maegawa S, Akiyama Y, & Ha Y (2007). The role of L1 loop in the mechanism of rhomboid intramembrane protease GlpG. J Mol Biol 374 :1104-1113. PubMed Id: 17976648.
*GlpG rhomboid-family intramembrane protease: Escherichia coli* B Bacteria, 2.5 Å** Shows GlpG in a more open conformation.	2O7L	Data File Jmol Viewer 2O7L	Wang & Ha (2007). Wang Y & Ha Y (2007). Open-cap conformation of intramembrane protease GlpG. Proc Natl Acad Sci USA 104 :2098-2102. PubMed Id: 17277078.
*GlpG rhomboid-family intramembrane protease: Escherichia coli* B Bacteria, 2.6 Å** P3₁ space group. Two anti-parallel molecules in asymmetric unit.	2NRF	Data File Jmol Viewer 2NRF	Wu et al. (2006). Wu Z, Yan N, Feng L, Oberstein A, Yan H, Baker RP, Gu L, Jeffrey PD, Urban S & Shi Y (2006). Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry. Nature Struc. Molec. Biol. 13 :1084-1091. PubMed Id: 17099694.
*GlpG rhomboid-family intramembrane protease: Escherichia coli* B Bacteria, 2.3 Å** P2₁ space group. Two anti-parallel molecules in asymmetric unit.	2IRV	Data File Jmol Viewer 2IRV	Ben-Shem et al. (2007). Ben-Shem A, Fass D, & Bibi E (2007). Structural basis for intramembrane proteolysis by rhomboid serine proteases. Proc Natl Acad Sci USA 104 :426-466. PubMed Id: 17190827.
*GlpG rhomboid-family intramembrane protease: Escherichia coli* B Bacteria, 1.65 Å** Acyl GlpG: GlpG with covalently bound isocoumarin inhibitor, 2.09 Å: 2XOW	2XOV	Data File Jmol Viewer 2XOV 2XOW	Vinothkumar et al. (2010). Vinothkumar KR, Strisovsky K, Andreeva A, Christova Y, Verhelst S, & Freeman M (2010). The structural basis for catalysis and substrate specificity of a rhomboid protease. EMBO J 29 :3797-3809. PubMed Id: 20890268.
*GlpG rhomboid-family intramembrane protease with lipids: Escherichia coli* B Bacteria, 1.70 Å** S201T active-site mutant in orthorhombic crystal form. S201T active-site mutant in trigonal crystal form, 1.85 Å: 2XTU	2XTV	Data File Jmol Viewer 2XTV 2XTU	Vinothkumar (2011). Vinothkumar KR (2011). Structure of Rhomboid Protease in a Lipid Environment. J Mol Biol 407 :232-247. PubMed Id: 21256137.
*GlpG rhomboid-family intramembrane protease with a mechanism-based inhibitor: Escherichia coli* B Bacteria, 2.30 Å** The inhibitor is diisopropyl fluorophosphonate, which mimics the oxyanion-containing tetrahedral intermediate of the hydrolytic reaction.	3TXT	Data File Jmol Viewer 3TXT	Xue & Ha (2012). Xue Y & Ha Y (2012). Catalytic Mechanism of Rhomboid Protease GlpG Probed by 3,4-Dichloroisocoumarin and Diisopropyl Fluorophosphonate. J Biol Chem 287 :3099-3107. PubMed Id: 22130671. doi:10.1074/jbc.M111.310482.
*GlpG rhomboid-family intramembrane protease in complex with phosphonofluoridate inhibitor: Escherichia coli* B Bacteria, 2.60 Å** The phosphonofluoridate inhibitor is covalently bound to the catalytic serine	3UBB	Data File Jmol Viewer 3UBB	Xue et al. (2012). Xue Y, Chowdhury S, Liu X, Akiyama Y, Ellman J, & Ha Y (2012). Conformational Change in Rhomboid Protease GlpG Induced by Inhibitor Binding to Its S' Subsites. Biochemistry 51 :3723-3731. PubMed Id: 22515733. doi:10.1021/bi300368b.
*GlpG N-terminal cytoplasmic domain: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), NMR Structure**	2GQC	Data File Jmol Viewer 2GQC	Del Rio et al. (2007). Del Rio A, Dutta K, Chavez J, Ubarretxena-Belandia I, & Ghose R (2007). Solution structure and dynamics of the N-terminal cytosolic domain of rhomboid intramembrane protease from Pseudomonas aeruginosa: insights into a functional role in intramembrane proteolysis. J Mol Biol 365 :109-122. PubMed Id: 17059825. doi:10.1016/j.jmb.2006.09.047.
*GlpG N-terminal cytoplasmic domain: Escherichia coli* B Bacteria, NMR Structure**	2LEP	Data File Jmol Viewer 2LEP	Sherratt et al. (2009). Sherratt AR, Braganza MV, Nguyen E, Ducat T, & Goto NK (2009). Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain. BBA Biomembranes 1788 :2444-2453. PubMed Id: 19761755. doi:10.1016/j.bbamem.2009.09.003.
*GlpG N-terminal cytoplasmic domain: Escherichia coli* B Bacteria, 1.35 Å** Domain-swapped dimer.	4HDD	Data File Jmol Viewer 4HDD	Lazareno-Saez et al. (2013). Lazareno-Saez C, Arutyunova E, Coquelle N, & Lemieux MJ (2013). Domain Swapping in the Cytoplasmic Domain of the Escherichia coli Rhomboid Protease. J Mol Biol 425 :1127-1142. PubMed Id: 23353827. doi:10.1016/j.jmb.2013.01.019.
*GlpG rhomboid-family intramembrane protease in complex with inhibitor Ac-IATA-cmk : Escherichia coli* B Bacteria, 2.10 Å** in complex with inhibitor Ac-FATA-cmk, 2.90 Å: 4QO0 F146I mutant in complex with Ac-FATA-cmk, 2.55 Å: 4QNZ	4QO2	Data File Jmol Viewer 4QO2 4QO0 4QNZ	Zoll et al. (2014). Zoll S, Stanchev S, Began J, Skerle J, Lepšík M, Peclinovská L, Majer P, & Strisovsky K (2014). Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate-peptide complex structures. EMBO J 33 :2408-2421. PubMed Id: 25216680. doi:10.15252/embj.201489367.
*GlpG rhomboid-family intramembrane protease in complex with Ac-VRMA-CHO: Escherichia coli* B Bacteria, 2.3 Å** Y205F mutant crystalized from bicelles, 2.5 Å: 5F5D Y205F mutant in complex with Ac-RMA-CHO (from bicelles), 2.3 Å: 5F5G Y205F mutant in complex with Ac-VRMA-CHO (from bicelles), 2.4 Å: 5F5J Y205F mutant in complex with Ac-RKVRMA-CHO (from bicelles), 2.4 Å:5F5K	5F5B	Data File Jmol Viewer 5F5B 5F5K 5F5J 5F5G 5F5D	Cho et al. (2016). Cho S, Dickey SW, & Urban S (2016). Crystal Structures and Inhibition Kinetics Reveal a Two-Stage Catalytic Mechanism with Drug Design Implications for Rhomboid Proteolysis. Mol Cell 61 3:329-340. PubMed Id: 26805573. doi:10.1016/j.molcel.2015.12.022.
*GlpG rhomboid intramembrane protease snapshots, I1: Escherichia coli* B Bacteria, 2.3 Å** snapshot I2, 2.4 Å: 6PJ5 snapshot I3, 2.3 Å: 6PJ7 snapshot I4, 2.4 Å: 6PJ8 snapshot S1, 2.5 Å: 6PJ9 snapshot S2, 2.6 Å: 6PJA snapshot S3, 2.45 Å: 6PJP snapshot S4, 2.50 Å: 6PJQ snapshot S5, 2.30 Å: 6PJR snapshot S6, 2.50 Å: 6PJU	6PJ4	Data File Jmol Viewer 6PJ4 6PJQ 6PJ8 6PJR 6PJ5 6PJ9 6PJ7 6PJA 6PJP 6PJU	Cho et al. (2019). Cho S, Baker RP, Ji M, & Urban S (2019). Ten catalytic snapshots of rhomboid intramembrane proteolysis from gate opening to peptide release. Nat Struct Mol Biol 26 :910-918. PubMed Id: 31570873. doi:10.1038/s41594-019-0296-9.
*GlpG rhomboid-family intramembrane protease: Haemophilus influenzae* B Bacteria (expressed in E. coli), 2.2 Å** Shows three bound lipid molecules. Monoclinic C2 space group.	2NR9	Data File Jmol Viewer 2NR9 Rhomboid peptidase	Lemieux et al. (2007). Lemieux MJ, Fischer SJ, Cherney MM, Bateman KS, & James MNG (2007). The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis. Proc Natl Acad Sci USA 104 :750-754. PubMed Id: 17210913.
*GlpG rhomboid-family intramembrane protease: Haemophilus influenzae* B Bacteria (expressed in E. coli), 2.84 Å** Reveals disorder in loops 4 and 5 and helix 5.	3ODJ	Data File Jmol Viewer 3ODJ	Brooks et al. (2011). Brooks CL, Lazareno-Saez C, Lamoureux JS, Mak MW, & Lemieux MJ (2011). Insights into Substrate Gating inH. influenzaeRhomboid. J Mol Biol 407 :687-697. PubMed Id: 21295583.
*Site-2 Protease (S2P). Intramembrane Metalloprotease: Methanocaldococcus jannaschii* A Archaea, 3.3 Å** Structure is of the transmembrane core only.	3B4R	Data File Jmol Viewer 3B4R	Feng et al. (2007). Feng L, Yan H, Wu Z, Yan N, Wang Z, Jeffrey PD, & Shi Y (2007). Structure of a site-2 protease family intramembrane metalloprotease. Science 318 :1608-1612. PubMed Id: 18063795.
*Signal Peptide Peptidase (SppA), native protein: Escherichia coli* B Bacteria, 2.55 Å** SeMet protein, 2.76 Å: 3BEZ. Long thought to be a transmembrane protein, the structure reveals a peripheral homotetramer that likely is buried in the membrane interface. Each monomer has a putative N-terminal transmembrane helix for anchoring to the membrane. This anchor was removed for crystallization. Listed under TRANSMEMBRANE PROTEINS: ALPHA-HELICAL : Intramembrane Proteases, MONOTOPIC MEMBRANE PROTEINS : Peptidases.	3BF0	Data File Jmol Viewer 3BF0 3BEZ	Kim et al. (2008). Kim AC, Oliver DC, & Paetzel M (2008). Crystal structure of a bacterial signal Peptide peptidase. J Mol Biol 376 :352-366. PubMed Id: 18164727.
*Signal Peptide Peptidase (SppA): Bacillus subtilis* B Bacteria (expressed in E. coli), 2.37 Å** Each monomer of the homooctamer has a putative N-terminal transmembrane helix for anchoring to the membrane. This anchor was removed for crystallization. Listed under TRANSMEMBRANE PROTEINS: ALPHA-HELICAL : Intramembrane Proteases, MONOTOPIC MEMBRANE PROTEINS : Peptidases.	3RST	Data File Jmol Viewer 3RST	Nam et al. (2012). Nam SE, Kim AC, & Paetzel M (2012). Crystal Structure of Bacillus subtilis Signal Peptide Peptidase A. J Mol Biol 419 :347-358. PubMed Id: 22472423. doi:10.1016/j.jmb.2012.03.020.
*Signal Peptide Peptidase (SppA) K199A mutant showing C-terminal peptide bound in eight active sites: Bacillus subtilis* B Bacteria (expressed in E. coli), 2.39 Å** Each monomer of the homooctamer has a putative N-terminal transmembrane helix for anchoring to the membrane. This anchor was removed for crystallization. Listed under TRANSMEMBRANE PROTEINS: ALPHA-HELICAL : Intramembrane Proteases, MONOTOPIC MEMBRANE PROTEINS : Peptidases.	4KWB	Data File Jmol Viewer 4KWB	Nam & Paetzel (2013). Nam SE, & Paetzel M (2013). Structure of Signal Peptide Peptidase A with C-Termini Bound in the Active Sites: Insights into Specificity, Self-Processing, and Regulation. Biochemistry 52 :8811-8822. PubMed Id: 24228759.
*Lipoprotein signal peptidase II: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.8 Å** See also related proteins: diacylglyceryl transferase (Lgt) 5AZC; signal peptidase I 1B12 and 4WVG	5DIR	Data File Jmol Viewer 5DIR	Vogeley et al. (2016). Vogeley L, El Arnaout T, Bailey J, Stansfeld PJ, Boland C, & Caffrey M (2016). Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin. Science 351 :876-880. PubMed Id: 26912896. doi:10.1126/science.aad3747.
*LspA lipoprotein signal peptide peptidase II in complex with globomycin: Staphylococcus aureus* B Bacteria (expressed in E. coli), 1.92 Å** in complex with myxovirescin, 2.3 Å: 6RYP	6RYO	Data File Jmol Viewer 6RYO 6RYP	Olatunji et al. (2020). Olatunji S, Yu X, Bailey J, Huang CY, Zapotoczna M, Bowen K, Remškar M, Müller R, Scanlan EM, Geoghegan JA, Olieric V, & Caffrey M (2020). Structures of lipoprotein signal peptidase II from Staphylococcus aureus complexed with antibiotics globomycin and myxovirescin. Nat Commun 11 1. PubMed Id: 31919415. doi:10.1038/s41467-019-13724-y.
*PSH presenilin/SPP homologue aspartate protease (C222 space group): Methanoculleus marisnigri* A Archaea (expressed in E. coli), 3.32 Å** P2 space group, 3.95 Å: 4HYC C222₁ space group, 3.80 Å: 4HYD	4HYG	Data File Jmol Viewer 4HYG 4HYC 4HYD	Li et al. (2013). Li X, Dang S, Yan C, Gong X, Wang J, & Shi Y (2013). Structure of a presenilin family intramembrane aspartate protease. Nature 493 :56-61. PubMed Id: 23254940. doi:10.1038/nature11801.
*FlaK preflagellin aspartyl protease: Methanococcus maripaludis* A Archaea (expressed in E. coli), 3.60 Å** This is a GXGD protease related to presenilln.	3S0X	Data File Jmol Viewer 3S0X	Hu et al. (2011). Hu J, Xue Y, Lee S, & Ha Y (2011). The crystal structure of GXGD membrane protease FlaK Nature 475 :528-531. PubMed Id: 21765428. doi:10.1038/nature10218.
*CAAX protease Ste24p: Saccharomyces mikatae* E Eukaryota (expressed in S. cerevisiae), 3.10 Å**	4IL3	Data File Jmol Viewer 4IL3	Pryor et al. (2013). Pryor EE Jr, Horanyi PS, Clark KM, Fedoriw N, Connelly SM, Koszelak-Rosenblum M, Zhu G, Malkowski MG, Wiener MC, & Dumont ME (2013). Structure of the integral membrane protein CAAX protease Ste24p. Science 339 :1600-1604. PubMed Id: 23539602. doi:10.1126/science.1232048.
*CAAX protease ZMPSTE24: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.40 Å** E336A mutant in complex with C-terminus tetrapeptide from prelamin A, 3.80 Å: 2YPT	4AW6	Data File Jmol Viewer 4AW6 2YPT	Quigley et al. (2013). Quigley A, Dong YY, Pike AC, Dong L, Shrestha L, Berridge G, Stansfeld PJ, Sansom MS, Edwards AM, Bountra C, von Delft F, Bullock AN, Burgess-Brown NA, & Carpenter EP (2013). The structural basis of ZMPSTE24-dependent laminopathies. Science 339 :1604-1607. PubMed Id: 23539603. doi:doi:10.1126/science.1231513.
*CAAX protease ZMPSTE24 with bound phosphoramidon: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.85 Å**	6BH8	Data File Jmol Viewer 6BH8	Goblirsch et al. (2018). Goblirsch BR, Arachea BT, Councell DJ, & Wiener MC (2018). Phosphoramidon inhibits the integral membrane protein zinc metalloprotease ZMPSTE24. Acta Crystallogr D Struct Biol 74 :739-747. PubMed Id: 30082509. doi:10.1107/S2059798318003431.
*CAAX protease Rce1: Methanococcus maripaludis* A Archaea (expressed in E. coli), 2.50 Å**	4CAD	Data File Jmol Viewer 4CAD	Manolaridis et al. (2013). Manolaridis I, Kulkarni K, Dodd RB, Ogasawara S, Zhang Z, Bineva G, O'Reilly N, Hanrahan SJ, Thompson AJ, Cronin N, Iwata S, & Barford D (2013). Mechanism of farnesylated CAAX protein processing by the intramembrane protease Rce1. Nature 504 :301-305. PubMed Id: 24291792. doi:10.1038/nature12754.
*γ-secretase: Homo sapiens* E Eukaryota (expressed in HEK-293S cells), 4.32 Å**	4UIS	Data File Jmol Viewer 4UIS	Sun et al. (2015). Sun L, Zhao L, Yang G, Yan C, Zhou R, Zhou X, Xie T, Zhao Y, Wu S, Li X, & Shi Y (2015). Structural basis of human γ-secretase assembly. Proc Natl Acad Sci USA 112 :6003-6008. PubMed Id: 25918421. doi:10.1073/pnas.1506242112.
*γ-secretase: Homo sapiens* E Eukaryota (expressed in HEK293F cells), 3.4 Å** single-particle Cryo-EM structure	5A63	Data File Jmol Viewer 5A63	Bai et al. (2015). Bai XC, Yan C, Yang G, Lu P, Ma D, Sun L, Zhou R, Scheres SH, & Shi Y (2015). An atomic structure of human γ-secretase. Nature 525 :212-217. PubMed Id: 26280335. doi:10.1038/nature14892.
*γ-secretase nicastrin extracellular domain: Homo sapiens* E Eukaryota (expressed in HEK293F cells), 5.4 Å** Single-particle cryo-EM structure. 4.5 Å and 5.4 Å EM maps of the full protein including TM domains are available in the EMDB with accession codes EMD-2677 and EMD-2678, respectively.	4UPC	Data File Jmol Viewer 4UPC	Lu et al. (2014). Lu P, Bai XC, Ma D, Xie T, Yan C, Sun L, Yang G, Zhao Y, Zhou R, Scheres SH, & Shi Y (2014). Three-dimensional structure of human γ-secretase. Nature 512 :166-170. PubMed Id: 25043039. doi:10.1038/nature13567.
*γ-secretase nicastrin-a transmembrane domain in SDS:: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure** in dodecylphosphocholine micelles, 2NR7	2N7Q	Data File Jmol Viewer 2N7Q 2NR7	Li et al. (2016). Li Y, Liew LS, Li Q, & Kang C (2016). Structure of the transmembrane domain of human nicastrin-a component of γ-secretase. Sci Rep 6 :19522. PubMed Id: 26776682. doi:10.1038/srep19522.
*γ-secretase in complex with Notch-100: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.7 Å** cryo-EM structure	6IDF	Data File Jmol Viewer 6IDF	Yang et al. (2019). Yang G, Zhou R, Zhou Q, Guo X, Yan C, Ke M, Lei J, & Shi Y (2019). Structural basis of Notch recognition by human γ-secretase. Nature 565 7738:192-197. PubMed Id: 30598546. doi:10.1038/s41586-018-0813-8.
*γ-secretase cross-linked complex with APP-C83: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.6 Å** cryo-EM structure	6IYC	Data File Jmol Viewer 6IYC	Zhou et al. (2019). Zhou R, Yang G, Guo X, Zhou Q, Lei J, & Shi Y (2019). Recognition of the amyloid precursor protein by human γ-secretase. Science 363 6428. PubMed Id: 30630874. doi:10.1126/science.aaw0930.
*γ-secretase substrate: TREM2 transmembrane helix in DPC micelles: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure** TREM2: triggering receptor expressed on myeloid cells 2 K186A variant in DPC micelles: 6Z0H in complex with DAP12 in DPC micelles: 6Z0I	6Z0G	Data File Jmol Viewer 6Z0G 6Z0I 6Z0H	Steiner et al. (2020). Steiner A, Schlepckow K, Brunner B, Steiner H, Haass C, & Hagn F (2020). γ-Secretase cleavage of the Alzheimer risk factor TREM2 is determined by its intrinsic structural dynamics. EMBO J 39 20. PubMed Id: 32830336. doi:10.15252/embj.2019104247.
*γ-secretase with bound Semagacestat: Homo sapiens* E Eukaryota (expressed in HEK-293S cells), 3.00 Å** cryo-EM structure with bound Avagacestat, 3.10 Å: 6LQG with bound L-685458, 3.10 Å: 7C9I with bound E2012 and L685458, 2.60 Å: 7D8X	6LR4	Data File Jmol Viewer 6LR4 6LQG 7D8X 7C9I	Yang et al. (2021). Yang G, Zhou R, Guo X, Yan C, Lei J, & Shi Y (2021). Structural basis of γ-secretase inhibition and modulation by small molecule drugs. Cell 184 2:521-533.e14. PubMed Id: 33373587. doi:10.1016/j.cell.2020.11.049.
*γ-secretase, in complex with presenilin 1 (PS1), with bound PS1-selective inhibitor MRK-56: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure in complex with presenilin 2 (PS2), 3.00 Å: 7Y5X in complex with presenilin 2 (PS2), apo, 3.40 Å: 7Y5Z	7Y5T	Data File Jmol Viewer 7Y5T 7Y5X 7Y5Z	Guo et al. (2022). Guo X, Wang Y, Zhou J, Jin C, Wang J, Jia B, Jing D, Yan C, Lei J, Zhou R, & Shi Y (2022). Molecular basis for isoform-selective inhibition of presenilin-1 by MRK-560. Nat Commun 13 1:6299. PubMed Id: 36272978. doi:10.1038/s41467-022-33817-5.
*γ-secretase with bound ganglioside GM1: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure	8IM7	Data File Jmol Viewer 8IM7	Wang et al. (2023). Wang X, Zhou R, Sun X, Li J, Wang J, Yue W, Wang L, Liu H, Shi Y, & Zhang D (2023). Preferential Regulation of Γ-Secretase-Mediated Cleavage of APP by Ganglioside GM1 Reveals a Potential Therapeutic Target for Alzheimer's Disease. Adv Sci (Weinh) 10 32:e2303411. PubMed Id: 37759382. doi:10.1002/advs.202303411.
*γ-secretase with bound substrate mimetic: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.60 Å** cryo-EM structure	8K8E	Data File Jmol Viewer 8K8E	Devkota et al. (2024). Devkota S, Zhou R, Nagarajan V, Maesako M, Do H, Noorani A, Overmeyer C, Bhattarai S, Douglas JT, Saraf A, Miao Y, Ackley BD, Shi Y, & Wolfe MS (2024). Familial Alzheimer mutations stabilize synaptotoxic γ-secretase-substrate complexes. Cell Rep 43 2:113761. PubMed Id: 38349793. doi:10.1016/j.celrep.2024.113761.
*γ-secretase nicastrin extracellular domain: Dictyostelium purpureum* E Eukaryota (expressed in S. frugiperda), 1.95 Å**	4R12	Data File Jmol Viewer 4R12	Xie et al. (2014). Xie T, Yan C, Zhou R, Zhao Y, Sun L, Yang G, Lu P, Ma D, & Shi Y (2014). Crystal structure of the γ-secretase component nicastrin. Proc Natl Acad Sci USA 111 37:13349-13354. PubMed Id: 25197054. doi:10.1073/pnas.1414837111.
*Signal Peptidase Complex Paralog A (SPC-A): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.90 Å** cryo-EM structure Signal Peptidase Complex Paralog C (SPC-C), 4.90 Å: 7P2Q	7P2P	Data File Jmol Viewer 7P2P 7P2Q	Liaci et al. (2021). Liaci AM, Steigenberger B, Telles de Souza PC, Tamara S, Gröllers-Mulderij M, Ogrissek P, Marrink SJ, Scheltema RA, & Förster F (2021). Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage. Mol Cell 81 19:3934-3948.e11. PubMed Id: 34388369. doi:10.1016/j.molcel.2021.07.031.
*Signal peptidase complex subunit 1: Gallus gallus* E Eukaryota (expressed in Komagataella pastoris), 2.43 Å** The protein was stabilized for crystallization using a split superfolder green fluorescent protein (from Aequorea victoria) attached to N- and C-termini of the protein.	6WVE	Data File Jmol Viewer 6WVE	Liu et al. (2020). Liu S, Li S, Yang Y, & Li W (2020). Termini restraining of small membrane proteins enables structure determination at near-atomic resolution. Sci Adv 6 51:eabe3717. PubMed Id: 33355146. doi:10.1126/sciadv.abe3717.
*PGAM5 WT transmembrane domain (TMD): Homo sapiens* E Eukaryota, NMR structure** C12L mutant, 7QAL C12S mutant, 7QAO G17L mutant, 7QAP	7QAM	Data File Jmol Viewer 7QAM 7QAL 7QAP 7QAO	Siebert et al. (2022). Siebert V, Silber M, Heuten E, Muhle-Goll C, & Lemberg MK (2022). Cleavage of mitochondrial homeostasis regulator PGAM5 by the intramembrane protease PARL is governed by transmembrane helix dynamics and oligomeric state. J Biol Chem 298 9:e102321. PubMed Id: 35921890. doi:10.1016/j.jbc.2022.102321.
Cysteine Proteases Also known as Thiol Proteases
*Glycosylphosphatidylinositol (GPI) transamidase: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure	7W72	Data File Jmol Viewer 7W72	Zhang et al. (2022). Zhang H, Su J, Li B, Gao Y, Liu M, He L, Xu H, Dong Y, Zhang XC, & Zhao Y (2022). Structure of human glycosylphosphatidylinositol transamidase. Nat Struct Mol Biol 29 3:203-209. PubMed Id: 35165458. doi:10.1038/s41594-022-00726-6.
*Glycosylphosphatidylinositol (GPI) transamidase complex: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.53 Å** cryo-EM structure	7WLD	Data File Jmol Viewer 7WLD	Xu et al. (2022). Xu Y, Jia G, Li T, Zhou Z, Luo Y, Chao Y, Bao J, Su Z, Qu Q, & Li D (2022). Molecular insights into biogenesis of glycosylphosphatidylinositol anchor proteins. Nat Commun 13 1:2617. PubMed Id: 35551457. doi:10.1038/s41467-022-30250-6.
Membrane-Bound Metalloproteases
apo-FtsH ATP-dependent metalloprotease: Thermotoga maritima B Bacteria (expressed in E. coli), 2.60 Å This is a homo-hexameric AAA+ protease. Each monomer is anchored to the cytoplasmic membrane by two transmembrane segments, which are missing in the structure. The protease can degrade both soluble and membrane proteins.	3KDS	Data File Jmol Viewer 3KDS	Bieniossek et al. (2009). Bieniossek C, Niederhauser B, & Baumann UM (2009). The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation. Proc Natl Acad Sci USA 106 :21579-21584. PubMed Id: 19955424.
*FtsH ATP-dependent metalloprotease, ADP-bound state: Thermotoga maritima* B Bacteria (expressed in E. coli), 3.15 Å** cryo-EM structure	7TDO	Data File Jmol Viewer 7TDO	Liu et al. (2022). Liu W, Schoonen M, Wang T, McSweeney S, & Liu Q (2022). Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state. Commun Biol 5 1:257. PubMed Id: 35322207. doi:10.1038/s42003-022-03213-2.
*apo-FtsH ATP-dependent metalloprotease: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.96 Å** truncated protein, 3.25 Å: 4Z8X This is a homo-hexameric AAA+ protease. Each monomer is anchored to the cytoplasmic membrane by two transmembrane segments, which are missing in the structure. The protease can degrade both soluble and membrane proteins.	4WW0	Data File Jmol Viewer 4WW0 4Z8X	Vostrukhina et al. (2015). Vostrukhina M, Popov A, Brunstein E, Lanz MA, Baumgartner R, Bieniossek C, Schacherl M, & Baumann U (2015). The structure of Aquifex aeolicus FtsH in the ADP-bound state reveals a C2-symmetric hexamer. Acta Crystallogr D Biol Crystallogr 71 :1307-1318. PubMed Id: 26057670. doi:10.1107/S1399004715005945.
CorA Superfamily Ion Transporters Channels and transporters for divalent cation homeostasis. These have a membrane domain in series with a cytoplasmic domain that together form a continuous channel.
*CorA Mg²⁺ Transporter: Thermotoga maritima* B Bacteria (expressed in E. coli), 3.9 Å** Cytoplasmic domain alone, 1.85 Å: 2BBH	2BBJ	Data File Jmol Viewer 2BBJ 2BBH CorA Mg2+ transporter	Lunin et al. (2006). Lunin VV, Dobrovetsky E, Khutoreskaya G, Zhang R, Joachimiak A, Doyle DA, Bochkarev A, Maguire ME, Edwards AM, & Koth CM (2006). Crystal structure of the CorA Mg²⁺transporter. Nature 440 :833-837. PubMed Id: 16598263.
*CorA Mg²⁺ Transporter: Thermotoga maritima* B Bacteria (expressed in E. coli), 2.9 Å**	2IUB	Data File Jmol Viewer 2IUB	Eshaghi et al. (2006). Eshaghi S, Niegowski D, Kohl A, Martinez Molina D, Lesley SA, & Nordlund P (2006). Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution. Science 313 :354-357. PubMed Id: 16857941.
*CorA Mg²⁺ Transporter: Thermotoga maritima* B Bacteria (expressed in E. coli), 3.7 Å**	2HN2	Data File Jmol Viewer 2HN2	Payandeh & Pai (2006). Payandeh J & Pai EF (2006). A structural basis for Mg²⁺ homeostasis and the CorA translocation cycle EMBO J 25 :3762-3773. PubMed Id: 16902408. doi:10.1038/sj.emboj.7601269.
*CorA Mg²⁺ Transporter, coiled-coil mutant in the absence of Mg²⁺: Thermotoga maritima* B Bacteria (expressed in E. coli), 3.80 Å** Coiled-coil mutant in the presence of Mg²⁺, 3.92 Å: 4EED	4EEB	Data File Jmol Viewer 4EEB 4EED	Pfoh et al. (2012). Pfoh R, Li A, Chakrabarti N, Payandeh J, Pomès R, & Pai EF (2012). Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation. Proc Natl Acad Sci USA 109 :18809-18814. PubMed Id: 23112165. doi:10.1073/pnas.1209018109.
*CorA Mg²⁺ Transporter, cryo-EM structure, closed state: Thermotoga maritima* B Bacteria (expressed in E. coli), 3.8 Å** Mg-free, asymmetric open state I, 7.06 Å: 3JCG Mg-free, asymmetric open state II, 7.06 Å: 3JCH	3JCF	Data File Jmol Viewer 3JCF 3JCG 3JCH	Matthies et al. (2016). Matthies D, Dalmas O, Borgnia MJ, Dominik PK, Merk A, Rao P, Reddy BG, Islam S, Bartesaghi A, Perozo E, & Subramaniam S (2016). Cryo-EM Structures of the Magnesium Channel CorA Reveal Symmetry Break upon Gating. Cell 164 :747-756. PubMed Id: 26871634. doi:10.1016/j.cell.2015.12.055.
*CorA Mg²⁺ Transporter: Methanocaldococcus jannaschii* A Archaea (expressed in E. coli), 3.20 Å** Soluble domain, 2.50 Å: 4EGW	4EV6	Data File Jmol Viewer 4EV6 4EGW	Guskov et al. (2012). Guskov A, Nordin N, Reynaud A, Engman H, Lundbäck AK, Jong AJ, Cornvik T, Phua T, & Eshaghi S (2012). Structural insights into the mechanisms of Mg²⁺ uptake, transport, and gating by CorA. Proc Natl Acad Sci USA 109 :18459-18464. PubMed Id: 23091000. doi:10.1073/pnas.1210076109 .
*CorA Mg²⁺ Transporter cytoplasmic domain with bound Mg²⁺: Escherichia coli* B Bacteria, 2.8 Å** in complex with Mg²⁺ & cobalt hexammine, 2.85 Å: 5N78	5N77	Data File Jmol Viewer 5N77 5N78	Lerche et al. (2017). Lerche M, Sandhu H, Flöckner L, Högbom M, & Rapp M (2017). Structure and Cooperativity of the Cytosolic Domain of the CorA Mg²⁺ Channel from Escherichia coli. Structure 25 :1175-1186.e4. PubMed Id: 28669631. doi:10.1016/j.str.2017.05.024.
*ZntB Zn⁺² transporter cytoplasmic domain: Vibrio parahaemolyticus* B Bacteria (expressed in E. coli), 1.90 Å**	3CK6	Data File Jmol Viewer 3CK6	Tan et al. (2009). Tan K, Sather A, Robertson JL, Moy S, Roux B, & Joachimiak A (2009). Structure and electrostatic property of cytoplasmic domain of ZntB transporter Protein Sci 18 :2043-2052. PubMed Id: 19653298. doi:10.1002/pro.215.
*ZntB Zn⁺² transporter cytoplasmic domain, P2₁ space group: Salmonella enterica* B Bacteria (expressed in E. coli), 2.30 Å** C2 space group, 3.13 Å: 3NWI	3NVO	Data File Jmol Viewer 3NVO 3NWI	Wan et al. (2011). Wan Q, Ahmad MF, Fairman J, Gorzelle B, de la Fuente M, Dealwis C, & Maguire ME (2011). X-Ray crystallography and isothermal titration calorimetry studies of the Salmonella zinc transporter ZntB Structure 19 :700-710. PubMed Id: 21565704. doi:10.1016/j.str.2011.02.011.
Cyclin M/CorC Family of Mg²⁺ Transporters Cyclin M is generally abbreviated CNNM. Reviewed by Funato & Miki (2019)
*CNNM/CorC family Mg²⁺ transporter transmembrane domain in complex with Mg²⁺: Thermus parvatiensis* B Bacteria (expressed in E. coli), 3.20 Å** in complex with Mg²⁺, 2.00 Å: 7CFF CBS domain, 2.00 Å: 7CFH CBS domain in complex with ATP, 2.45 Å: 7CFI	7CFG	Data File Jmol Viewer 7CFG 7CFI 7CFH 7CFF	Huang et al. (2021). Huang Y, Jin F, Funato Y, Xu Z, Zhu W, Wang J, Sun M, Zhao Y, Yu Y, Miki H, & Hattori M (2021). Structural basis for the Mg²⁺ recognition and regulation of the CorC Mg²⁺ transporter. Sci Adv 7 7:eabe6140. PubMed Id: 33568487. doi:10.1126/sciadv.abe6140.
*CNNM/CorC family Mg²⁺ transporter, C-terminal deletion in complex with Mg²⁺-ATP: Methanoculleus thermophilus* B Bacteria (expressed in E. coli), 3.26 Å** R235L mutant with C-terminal deletion, 3.80 Å: 7M1U CBS-pair domain in complex with Mg²⁺-ATP, 2.07 Å: 7MSU	7M1T	Data File Jmol Viewer 7M1T 7MSU 7M1U	Chen et al. (2021). Chen YS, Kozlov G, Moeller BE, Rohaim A, Fakih R, Roux B, Burke JE, & Gehring K (2021). Crystal structure of an archaeal CorB magnesium transporter. Nat Commun 12 1:4028. PubMed Id: 34188059. doi:10.1038/s41467-021-24282-7.
Bacterial Mercury Detoxification Proteins
*MerF Hg(II) transporter: Morganella morganii* B Bacteria (expressed in E. coli), NMR structure** Structure of truncated protein (AAs 13-72) determined in aligned bicelles.	2H3O	Data File Jmol Viewer 2H3O	De Angelis et al. (2006). De Angelis AA, Howell SC, Nevzorov AA, & Opella SJ (2006). Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy. J AM Chem Soc 128 :12256-12267. PubMed Id: 16967977.
*MerF Hg(II) transporter: Morganella morganii* B Bacteria (expressed in E. coli), NMR structure** Structure of truncated protein (AAs 13-72) determined in SDS micelles.	1WAZ	Data File Jmol Viewer 1WAZ	Howell et al. (2005). Howell SC, Mesleh MF, & Opella SJ (2005). NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system. Biochemistry 44 :5196-5206. PubMed Id: 15794657.
*MerF Hg(II) transporter: Morganella morganii* B Bacteria (expressed in E. coli), NMR Structure** Structure of truncated protein (AAs 13-70) determined in proteoliposomes.	2LJ2	Data File Jmol Viewer 2LJ2	Das et al. (2012). Das BB, Nothnagel HJ, Lu GJ, Son WS, Tian Y, Marassi FM, & Opella SJ (2012). Structure determination of a membrane protein in proteoliposomes. J Amer Chem Soc 134 :2047-2056. PubMed Id: 22217388. doi:10.1021/ja209464f.
Rhodaneses Thiosulfate-Cyanide sulfurtransfereases
*YgaP rhodanese homodimeric transmembrane domain: Escherichia coli* B Bacteria, NMR Structure** cytoplasmic rhodanese domain, NMR structure: 2MOI cytoplasmic rhodanese domain of the full-length inner membrane protein, NMR structure: 2MOL	2MPN	Data File Jmol Viewer 2MPN 2MOL 2MOI	Eichmann et al. (2014). Eichmann C, Tzitzilonis C, Bordignon E, Maslennikov I, Choe S, & Riek R (2014). Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from Escherichia coli. J Biol Chem 289 :23482-23503. PubMed Id: 24958726. doi:10.1074/jbc.M114.571935. See also: Ling et al. (2016). Ling S, Wang W, Yu L, Peng J, Cai X, Xiong Y, Hayati Z, Zhang L, Zhang Z, Song L, & Tian C (2016). Structure of an E. coli integral membrane sulfurtransferase and its structural transition upon SCN^- binding defined by EPR-based hybrid method. Sci Rep 6 . PubMed Id: 26817826. doi:10.1038/srep20025.
Drug/Metabolite Transporter (DMT) Superfamily
*YddG aromatic amino acid exporter: Starkeya novella* B Bacteria (expressed in E. coli), 2.4 Å**	5I20	Data File Jmol Viewer 5I20	Tsuchiya et al. (2016). Tsuchiya H, Doki S, Takemoto M, Ikuta T, Higuchi T, Fukui K, Usuda Y, Tabuchi E, Nagatoishi S, Tsumoto K, Nishizawa T, Ito K, Dohmae N, Ishitani R, & Nureki O (2016). Structural basis for amino acid export by DMT superfamily transporter YddG. Nature 534 :417-420. PubMed Id: 27281193. doi:10.1038/nature17991.
*Chloroquine Resistance Transporter 7G8 Isoform: Plasmodium falciparum* E Eukaryota (expressed in HEK293 cells), 3.3 Å** cryo-EM structure	6UKJ	Data File Jmol Viewer 6UKJ	Kim et al. (2019). Kim J, Tan YZ, Wicht KJ, Erramilli SK, Dhingra SK, Okombo J, Vendome J, Hagenah LM, Giacometti SI, Warren AL, Nosol K, Roepe PD, Potter CS, Carragher B, Kossiakoff AA, Quick M, Fidock DA, & Mancia F (2019). Structure and drug resistance of the Plasmodium falciparum transporter PfCRT. Nature 576 7786:315-320. PubMed Id: 31776516. doi:10.1038/s41586-019-1795-x.
Multiple Peptide Resistance Factors (MprFs) These proteins use two separate domains to synthesize and translocate aminoacyl phospholipids
*multiple peptide resistance factor protein (MprF) loaded with one lysyl-phosphatidylglycerol molecule: Rhizobium tropici* B Bacteria (expressed in E. coli), 3.70 Å** cryo-EM structure loaded with two lysyl-phosphatidylglycerol molecules, 2.96 Å: 7DUW	6LVF	Data File Jmol Viewer 6LVF 7DUW	Song et al. (2021). Song D, Jiao H, & Liu Z (2021). Phospholipid translocation captured in a bifunctional membrane protein MprF. Nat Commun 12 1:2927. PubMed Id: 34006869. doi:10.1038/s41467-021-23248-z.
Multi-Drug Efflux Transporters Members of the multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) transporter superfamily
*AcrB bacterial multi-drug efflux transporter: Escherichia coli* B Bacteria, 3.5 Å** AcrB is a member of the resistance nodulation and cell division (RND) superfamily, as is SecDF.	1IWG	Data File Jmol Viewer 1IWG AcrB multidrug transporter	Murakami et al. (2002). Murakami S, Nakashima R, Yamashita E, & Yamaguchi A (2002). Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419 :587-593. PubMed Id: 12374972.
*AcrA fusion protein: Escherichia coli* B Bacteria, 2.70 Å** This is a soluble periplasmic protein. It bridges the AcrB multi-drug efflux transporter to the TolC outer membrane protein 1EK9	2F1M	Data File Jmol Viewer 2F1M	Mikolosko et al. (2006). Mikolosko J, Bobyk K, Zgurskaya HI, & Ghosh P (2006). Conformational flexibility in the multidrug efflux system protein AcrA. Structure 14 :577-587. PubMed Id: 16531241.
*AcrB bacterial multi-drug efflux transporter: Escherichia coli* B Bacteria, 3.7 Å** With substrates: rhodamine 6G, 3.63 Å: 1OY8. ethidium, 3.80 Å: 1OY9. dequalinium, 3.80 Å: 1OYD. ciprofloxacin, 3.48 Å: 1OYE.	1OY6	Data File Jmol Viewer 1OY6 1OY8 1OYD 1OY9 1OYE	Yu et al. (2003). Yu EW, McDermott G, Zgurskaya HI, Nikaido H, & Koshland Jr, DE (2003). Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump. Science 300 :976-980. PubMed Id: 12738864.
*AcrB bacterial multi-drug efflux transporter, apo protein, N109A mutant: Escherichia coli* B Bacteria, 3.23 Å** With substrates: ciprofloxacin, 3.11 Å: 1T9U. rhodamine 6G, 3.80 Å: 1T9V. nafcillin, 3.23 Å: 1T9W. ethidium, 3.08 Å: 1T9X. Phe-Arg-β-naphthylamide, 3.64 Å: 1T9Y.	1T9T	Data File Jmol Viewer 1T9T 1T9V 1T9U 1T9Y 1T9X 1T9W	Yu et al. (2005). Yu EW, Aires JR, McDermott G, & Nikaido H (2005). A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study. J Bacteriol 187 :6804-6815. PubMed Id: 16166543.
*AcrB bacterial multi-drug efflux transporter, D407A mutant: Escherichia coli* B Bacteria, 3.56 Å** D408A, 3.65 Å: 2HQD. K940A, 3.38 Å: 2HQF. T978A, 3.38 Å: 2HQG.	2HQC	Data File Jmol Viewer 2HQC 2HQF 2HQD 2HQG	Su et al. (2006). Su CC, Li M, Gu R, Takatsuka Y, McDermott G, Nikaido H, & Yu EW (2006). Conformation of the AcrB multidrug efflux pump in mutants of the putative proton relay pathway. J Bacteriol 188 :7290-7296. PubMed Id: 17015668.
*AcrB bacterial multi-drug efflux transporter: Escherichia coli* B Bacteria, 2.9 Å** Two crystal forms. C2: 2GIF. P1: 2HRT, 3.0 Å. Together, the two forms suggest a pump mechanism.	2GIF	Data File Jmol Viewer 2GIF 2HRT	Seeger et al. (2006). Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, & Pos KM (2006). Structural asymmetry of ArcB trimer suggests a peristaltic pump mechanism. Science 313 :1295-1298. PubMed Id: 16946072.
*AcrB bacterial multi-drug efflux transporter without ligands: Escherichia coli* B Bacteria, 2.8 Å** With minocycline, 3.1 Å: 2DRD. With doxorubicin, 3.3 Å: 2DR6	2DHH	Data File Jmol Viewer 2DHH 2DR6 2DRD	Murakami et al. (2006). Murakami S, Nakashima R, Yamashita E, Matsumoto T, & Yamaguchi A (2006). Crystal structures of a bacterial multidrug transporter reveal a functionally rotating mechanism. Nature 443 :173-179. PubMed Id: 16915237.
*AcrB in complex with DARPin: Escherichia coli* B Bacteria, 2.54 Å**	2J8S	Data File Jmol Viewer 2J8S	Sennhauser et al. (2007). Sennhauser G, Amstutz P, Briand C, Storchenegger O, & Grütter MG (2007). Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors. PLoS Biol. 5 1. PubMed Id: 17194213. doi:10.1371/journal.pbio.0050007.
*AcrB bacterial multi-drug efflux transporter with YajC subunit: Escherichia coli* B Bacteria, 3.5 Å**	2RDD	Data File Jmol Viewer 2RDD	Törnroth-Horsefield et al. (2007). Törnroth-Horsefield S, Gourdon P, Horsefield R, Brive L, Yamamoto N, Mori H, Snijder A, & Neutze R (2007). Crystal Structure of AcrB in Complex with a Single Transmembrane Subunit Reveals Another Twist. Structure 15 :1663-1673. PubMed Id: 18073115.
*AcrB bacterial multi-drug efflux transporter in complex with bile acid: Escherichia coli* B Bacteria, 3.85 Å**	2W1B	Data File Jmol Viewer 2W1B	Drew et al. (2008). Drew D, Klepsch MM, Newstead S, Flaig R, De Gier JW, Iwata S, & Beis K (2008). The structure of the efflux pump AcrB in complex with bile acid. Mol Membr Biol 25 :677-682. PubMed Id: 19023693.
*AcrB bacterial multi-drug efflux transporter: Escherichia coli* B Bacteria, 3.42 Å**	3D9B	Data File Jmol Viewer 3D9B	Veesler et al. (2008). Veesler D, Blangy S, Cambillau C, & Sciara G (2008). There is a baby in the bath water: AcrB contamination is a major problem in membrane-protein crystallization. Acta Crystallogr Sect F Struct Biol Cryst Commun 64 :880-885. PubMed Id: 18931428. doi:10.1107/S1744309108028248.
*AcrB bacterial multi-drug efflux transporter with bound rifampicin: Escherichia coli* B Bacteria, 3.35 Å** This and the additional structures below reveal two discrete multisite binding pockets. Unliganded AcrB, 3.35 Å: 3AOA With bound erythromycin, 3.34 Aring;: 3AOC With bound rifampicin & minocyline, 3.30 Å: 3AOD	3AOB	Data File Jmol Viewer 3AOB 3AOC 3AOA 3AOD	Nakashima et al. (2011). Nakashima R, Sakurai K, Yamasaki S, Nishino K, & Yamaguchi A (2011). Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket. Nature 480 :565-569. PubMed Id: 22121023. doi:10.1038/nature10641.
*AcrB bacterial multi-drug efflux transporter with bound designed ankyrin repeat protein (DARPin): Escherichia coli* B Bacteria, 2.70 Å** 3.34 Å: 3NOG	3NOC	Data File Jmol Viewer 3NOC 3NOG	Monroe et al. (2011). Monroe N, Sennhauser G, Seeger MA, Briand C, & Grütter MG (2011). Designed ankyrin repeat protein binders for the crystallization of AcrB: plasticity of the dominant interface. J Struct Biol 174 2:269-281. PubMed Id: 21296164. doi:10.1016/j.jsb.2011.01.014.
*wt AcrB/DARPin in complex with minocycline: Escherichia coli* B Bacteria, 1.90 Å** G616N mutant, 2.90 Å: 4DX6 wt AcrB/DARPin in complex with doxorubicin, 2.25 Å: 4DX7	4DX5	Data File Jmol Viewer 4DX5 4DX6 4DX7	Eicher et al. (2012). Eicher T, Cha HJ, Seeger MA, Brandstätter L, El-Delik J, Bohnert JA, Kern WV, Verrey F, Grütter MG, Diederichs K, & Pos KM (2012). Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop. Proc Natl Acad Sci USA 109 :5687-5692. PubMed Id: 22451937. doi:10.1073/pnas.1114944109.
*AcrB bacterial multi-drug efflux transporter with bound ABI-PP inhibitor: Escherichia coli* B Bacteria, 3.05 Å**	3W9H	Data File Jmol Viewer 3W9H	Nakashima et al. (2013). Nakashima R, Sakurai K, Yamasaki S, Hayashi K, Nagata C, Hoshino K, Onodera Y, Nishino K, & Yamaguchi A (2013). Structural basis for the inhibition of bacterial multidrug exporters. Nature 500 :102-106. PubMed Id: 23812586. doi:10.1038/nature12300.
*AcrB bacterial multi-drug efflux transporter in complex with Linezolid: Escherichia coli* B Bacteria, 3.50 Å**	4K7Q	Data File Jmol Viewer 4K7Q	Hung et al. (2013). Hung LW, Kim HB, Murakami S, Gupta G, Kim CY, & Terwilliger TC (2013). Crystal structure of AcrB complexed with linezolid at 3.5 Å resolution. J Struct Funct Genomics 14 2:71-75. PubMed Id: 23673416. doi:10.1007/s10969-013-9154-x.
*AcrB-AcrZ bacterial multi-drug efflux transporter complex: Escherichia coli* B Bacteria, 3.30 Å** AcrB-AcrZ-DARPin complex, 3.70 Å: 4CDI	4C48	Data File Jmol Viewer 4C48 4CDI	Du et al. (2014). Du D, Wang Z, James NR, Voss JE, Klimont E, Ohene-Agyei T, Venter H, Chiu W, & Luisi BF (2014). Structure of the AcrAB-TolC multidrug efflux pump. Nature 509 :512-515. PubMed Id: 24747401. doi:10.1038/nature13205.
*AcrB D407N mutant: Escherichia coli* B Bacteria, 2.30 Å** D408N mutant, 2.10 Å: 4U8Y K940A mutant, 2.00 Å: 4U95 R971A mutant, 2.00 Å: 4U96	4U8V	Data File Jmol Viewer 4U8V 4U8Y 4U95 4U96	Eicher et al. (2014). Eicher T, Seeger MA, Anselmi C, Zhou W, Brandstätter L, Verrey F, Diederichs K, Faraldo-Gómez JD, & Pos KM (2014). Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrB. Elife 3 :e03145. PubMed Id: 25248080. doi:10.7554/eLife.03145.
*AcrB bacterial multi-drug efflux transporter in complex with fusidic acid: Escherichia coli* B Bacteria, 2.5 Å**	5JMN	Data File Jmol Viewer 5JMN	Oswald et al. (2016). Oswald C, Tam HK, & Pos KM (2016). Transport of lipophilic carboxylates is mediated by transmembrane helix 2 in multidrug transporter AcrB. Nat Commun 7 :13819. PubMed Id: 27982032. doi:10.1038/ncomms13819.
*AcrB bacterial multi-drug efflux transporter in P2₁ space group: Escherichia coli* B Bacteria, 3.30 Å** triple mutant, 3.16 Å: 4ZIV deletion mutant, 3.40 Å: 4ZIW in complex with antibiotic, 3.47 Å: 4ZJL triple mutant in complex with antibiotic, 3.60 Å: 4ZJO deletion mutant in complex with antibiotic, 3.59 Å: 4ZJQ	4ZIT	Data File Jmol Viewer 4ZIT 4ZIV 4ZJO 4ZIW 4ZJL 4ZJQ	Ababou & Koronakis (2016). Ababou A, & Koronakis V (2016). Structures of Gate Loop Variants of the AcrB Drug Efflux Pump Bound by Erythromycin Substrate. PLoS One 11 7:e0159154. PubMed Id: 27403665. doi:10.1371/journal.pone.0159154.
*AcrABZ-TolC tripartite multi drug efflux pump with bound puromycin (asymmetric structure): Escherichia coli* B Bacteria, 5.9 Å** Formerly PDB 5V78 cryo-EM structure with bound MBX3132, 6.5 Å: 5NG5 apo form, 6.5 Å: 5V5S AcrBZ crystal structure, 3.2 Å: 5NC5	5OO6	Data File Jmol Viewer 5OO6 5V5S 5NG5 5NC5	Wang et al. (2017). Wang Z, Fan G, Hryc CF, Blaza JN, Serysheva II, Schmid MF, Chiu W, Luisi BF, & Du D (2017). An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump. Elife 6 :e24905. PubMed Id: 28355133. doi:10.7554/eLife.24905.
*AcrB bacterial multi-drug efflux transporter showing hoisting-loop: Escherichia coli* B Bacteria, 3.00 Å**	5YIL	Data File Jmol Viewer 5YIL	Zwama et al. (2017). Zwama M, Hayashi K, Sakurai K, Nakashima R, Kitagawa K, Nishino K, & Yamaguchi A (2017). Hoisting-Loop in Bacterial Multidrug Exporter AcrB Is a Highly Flexible Hinge That Enables the Large Motion of the Subdomains. Front Microbiol 8 :2095. PubMed Id: 29118749. doi:10.3389/fmicb.2017.02095.
*AcrB in native lipid bilayer membrane nanoparticles: Escherichia coli* B Bacteria, 3.2 Å** cryo-EM structure. Protein and surrounding lipids extracted using SMA polymers. D407A mutant in lipid bilayer, 3.0 Å: 6CSX	6BAJ	Data File Jmol Viewer 6BAJ 6CSX	Qiu et al. (2018). Qiu W, Fu Z, Xu GG, Grassucci RA, Zhang Y, Frank J, Hendrickson WA, & Guo Y (2018). Structure and activity of lipid bilayer within a membrane-protein transporter. Proc Natl Acad Sci USA 115 51:12985-12990. PubMed Id: 30509977. doi:10.1073/pnas.1812526115.
*AcrB bacterial multi-drug efflux transporter with bound fusidic acid, V340A mutant: Escherichia coli* B Bacteria, 2.8 Å** fusidic acid bound AcrB, I27A mutant, 2.8 Å: 6Q4O fusidic acid bound AcrB, N298A mutant, 2.8 Å: 6Q4P	6Q4N	Data File Jmol Viewer 6Q4N 6Q4O 6Q4P	Tam et al. (2020). Tam HK, Malviya VN, Foong WE, Herrmann A, Malloci G, Ruggerone P, Vargiu AV, & Pos KM (2020). Binding and Transport of Carboxylated Drugs by the Multidrug Transporter AcrB. J Mol Biol 432 4:861-877. PubMed Id: 31881208. doi:10.1016/j.jmb.2019.12.025.
*AcrBZ bacterial multi-drug efflux transporter in Saposin A-nanodisc: Escherichia coli* B Bacteria, 3.20 Å** cryo-EM structure AcrB and DARPin in Saposin A-nanodisc, 3.27 Å: 6SGU AcrBZ and DARPin in Saposin A-nanodisc with cardiolipin, 3.17 Å: 6SGR AcrB and DARPin in Saposin A-nanodisc with cardiolipin, 3.46 Å: 6SGT	6SGS	Data File Jmol Viewer 6SGS 6SGU 6SGT 6SGR	Du et al. (2020). Du D, Neuberger A, Orr MW, Newman CE, Hsu PC, Samsudin F, Szewczak-Harris A, Ramos LM, Debela M, Khalid S, Storz G, & Luisi BF (2020). Interactions of a Bacterial RND Transporter with a Transmembrane Small Protein in a Lipid Environment. Structure 28 6:625-634.e6. PubMed Id: 32348749. doi:10.1016/j.str.2020.03.013.
*AcrB bacterial multi-drug efflux transporter, G619P G621P mutant, fusidic acid bound to the TM1/TM2 groove: Escherichia coli* B Bacteria, 2.50 Å** G619P mutant, with bound minocycline, 2.35 Å 6ZO6 3-Formylrifamycin SV bound to the access pocket of G619P mutant, 2.85 Å 6ZO7 AcrB-G621P mutant with minocycline bound to the deep binding pocket, 2.50 Å 6ZO8 two rifabutins bound to access pocket, 2.70 Å 6ZO9 Partially induced AcrB T protomer and DDM binding to the TM8/PC2 pathway, 3.05 Å 6ZOA 3-Formylrifamycin SV binding to the access pocket of AcrB L protomer, 2.80 Å 6ZOB Erythromycin bound to the access pocket of AcrB-G616P L protomer, etc., 2.89 Å 6ZOC Fusidic acid bound to the allosteric deep transmembrane domain binding pocket, etc., 2.85 Å 6ZOD	6ZO5	Data File Jmol Viewer 6ZO5 6ZO8 6ZO7 6ZOA 6ZOB 6ZOC 6ZOD 6ZO6 6ZO9	Tam et al. (2021). Tam HK, Foong WE, Oswald C, Herrmann A, Zeng H, & Pos KM (2021). Allosteric drug transport mechanism of multidrug transporter AcrB. Nat Commun 12 1. PubMed Id: 34188038. doi:10.1038/s41467-021-24151-3.
*AcrB bacterial multi-drug efflux transporter in cycloalkane amphipol: Escherichia coli* B Bacteria, 3.20 Å** cryo-EM structure	7B5P	Data File Jmol Viewer 7B5P	Higgins et al. (2021). Higgins AJ, Flynn AJ, Marconnet A, Musgrove LJ, Postis VLG, Lippiat JD, Chung CW, Ceska T, Zoonens M, Sobott F, & Muench SP (2021). Cycloalkane-modified amphiphilic polymers provide direct extraction of membrane proteins for CryoEM analysis. Commun Biol 4 1:1337. PubMed Id: 34824357. doi:10.1038/s42003-021-02834-3.
*AcrB bacterial multi-drug efflux transporter with bound doxycycline: Escherichia coli* B Bacteria, 2.10 Å** with bound fusidic acid, 2.30 Å 7B8S with bound levofloxacin, 2.70 Å 7B8T	7B8R	Data File Jmol Viewer 7B8R 7B8S 7B8T	Ornik-Cha et al. (2021). Ornik-Cha A, Wilhelm J, Kobylka J, Sjuts H, Vargiu AV, Malloci G, Reitz J, Seybert A, Frangakis AS, & Pos KM (2021). Structural and functional analysis of the promiscuous AcrB and AdeB efflux pumps suggests different drug binding mechanisms. Nat Commun 12 1:6919. PubMed Id: 34824229. doi:10.1038/s41467-021-27146-2.
*AcrB bacterial multi-drug efflux transporter with BDM88855 inhibitor bound to TM domain: Escherichia coli* B Bacteria, 2.60 Å** R971A mutant with BDM88832 inhibitor bound to the transmembrane domain, 2.80 Å 7OUL R971A mutant with BDM88855 inhibitor bound to the transmembrane domain, 2.45 Å 7OUM	7OUK	Data File Jmol Viewer 7OUK 7OUM 7OUL	Plé et al. (2022). Plé C, Tam HK, Vieira Da Cruz A, Compagne N, Jiménez-Castellanos JC, Müller RT, Pradel E, Foong WE, Malloci G, Ballée A, Kirchner MA, Moshfegh P, Herledan A, Herrmann A, Deprez B, Willand N, Vargiu AV, Pos KM, Flipo M, & Hartkoorn RC (2022). Pyridylpiperazine-based allosteric inhibitors of RND-type multidrug efflux pumps. Nat Commun 13 1:115. PubMed Id: 35013254. doi:10.1038/s41467-021-27726-2.
*AcrB bacterial multi-drug efflux transporter, native-SAD structure determined at wavelength 3.02 Å: Escherichia coli* B Bacteria, 3.40 Å** X-ray Structure	8PX7	Data File Jmol Viewer 8PX7	El Omari et al. (2023). El Omari K, Duman R, Mykhaylyk V, Orr CM, Latimer-Smith M, Winter G, Grama V, Qu F, Bountra K, Kwong HS, Romano M, Reis RI, Vogeley L, Vecchia L, Owen CD, Wittmann S, Renner M, Senda M, Matsugaki N, Kawano Y, Bowden TA, Moraes I, Grimes JM, Mancini EJ, Walsh MA, Guzzo CR, Owens RJ, Jones EY, Brown DG, Stuart DI, Beis K, & Wagner A (2023). Experimental phasing opportunities for macromolecular crystallography at very long wavelengths. Commun Chem 6 1:219. PubMed Id: 37828292. doi:10.1038/s42004-023-01014-0.
*AcrB bacterial multi-drug efflux transporter in complex with Linezolid: Salmonella enterica* B Bacteria (expressed in E. coli), 4.60 Å** cryo-EM structure	6Z12	Data File Jmol Viewer 6Z12	Johnson et al. (2020). Johnson RM, Fais C, Parmar M, Cheruvara H, Marshall RL, Hesketh SJ, Feasey MC, Ruggerone P, Vargiu AV, Postis VLG, Muench SP, & Bavro VN (2020). Cryo-EM Structure and Molecular Dynamics Analysis of the Fluoroquinolone Resistant Mutant of the AcrB Transporter from Salmonella. Microorganisms 8 6:943. PubMed Id: 32585951. doi:10.3390/microorganisms8060943.
*MexB bacterial multi-drug efflux transporter: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 3.0 Å**	2V50	Data File Jmol Viewer 2V50	Sennhauser et al. (2009). Sennhauser G, Bukowska MA, Briand C, Grütter MG (2009). Crystal Structure of the Multidrug Exporter MexB from Pseudomonas aeruginosa. J Mol Biol 389 :134-145. PubMed Id: 19361527.
*MexA membrane fusion protein: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 3.00 Å** MexA is a soluble periplasmic protein that bridges MexB to OprM (1WP1, 3D5K ) to form the tripartite efflux complex MexAB-OprM.	1T5E	Data File Jmol Viewer 1T5E	Higgins et al. (2004). Higgins MK, Bokma E, Koronakis E, Hughes C, & Koronakis V (2004). Structure of the periplasmic component of a bacterial drug efflux pump. Proc Natl Acad Sci USA 101 :9994-9999. PubMed Id: 15226509. doi:10.1073/pnas.0400375101.
*MexA membrane fusion protein: Pseudomonas aeruginosa* B Bacteria, 2.40 Å** MexA is a soluble periplasmic protein that bridges MexB to OprM (1WP1, 3D5K ) to form the tripartite efflux complex MexAB-OprM.	1VF7	Data File Jmol Viewer 1VF7	Akama et al. (2004). Akama H, Matsuura T, Kashiwagi S, Yoneyama H, Narita S, Tsukihara T, Nakagawa A, & Nakae T (2004). Crystal structure of the membrane fusion protein, MexA, of the multidrug transporter in Pseudomonas aeruginosa. J Biol Chem 279 :25939-25942. PubMed Id: 15117957. doi:10.1074/jbc.C400164200.
*MexB bacterial multi-drug efflux transporter with bound ABI-PP inhibitor: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 3.15 Å** Drug-free MexB, 2.71 Å: 3W9I	3W9J	Data File Jmol Viewer 3W9J 3W9I	Nakashima et al. (2013). Nakashima R, Sakurai K, Yamasaki S, Hayashi K, Nagata C, Hoshino K, Onodera Y, Nishino K, & Yamaguchi A (2013). Structural basis for the inhibition of bacterial multidrug exporters. Nature 500 :102-106. PubMed Id: 23812586. doi:10.1038/nature12300.
*MexB bacterial multi-drug efflux transporter in complex with LMNG: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 2.91 Å**	6IIA	Data File Jmol Viewer 6IIA	Sakurai et al. (2019). Sakurai K, Yamasaki S, Nakao K, Nishino K, Yamaguchi A, & Nakashima R (2019). Crystal structures of multidrug efflux pump MexB bound with high-molecular-mass compounds. Sci Rep 9 1:4359. PubMed Id: 30867446. doi:10.1038/s41598-019-40232-2.
*MexAB-OprM tripartite efflux pump, 0 degree state: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 3.64 Å** cryo-EM structure 60 degree state, 3.76 Å: 6IOL See also 1WP1 and 3D5K	6IOK	Data File Jmol Viewer 6IOK 6IOL	Tsutsumi et al. (2019). Tsutsumi K, Yonehara R, Ishizaka-Ikeda E, Miyazaki N, Maeda S, Iwasaki K, Nakagawa A, & Yamashita E (2019). Structures of the wild-type MexAB-OprM tripartite pump reveal its complex formation and drug efflux mechanism. Nat Commun 10 1. PubMed Id: 30944318. doi:10.1038/s41467-019-09463-9.
*MexAB bacterial multi-drug efflux transporter in nanodisc: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 3.20 Å** cryo-EM structure OprM-MexA complex, 3.20 Å: 6TA5 MexB in nanodisc in absence of its protein partners, 4.50 Å: 6T7S	6TA6	Data File Jmol Viewer 6TA6 6T7S 6TA5	Glavier et al. (2020). Glavier M, Puvanendran D, Salvador D, Decossas M, Phan G, Garnier C, Frezza E, Cece Q, Schoehn G, Picard M, Taveau JC, Daury L, Broutin I, & Lambert O (2020). Antibiotic export by MexB multidrug efflux transporter is allosterically controlled by a MexA-OprM chaperone-like complex. Nat Commun 11 1:4948. PubMed Id: 33009415. doi:10.1038/s41467-020-18770-5.
*ZneA Zn(II)/proton antiporter: Cupriavidus metallidurans* B Bacteria (expressed in E. coli), 3.00 Å** Crystal form I. ZneA is a member of the resistance nodulation and cell division (RND) superfamily. Crystal form II, 3.71 Å: 4K0E	4K0J	Data File Jmol Viewer 4K0J 4K0E	Pak et al. (2013). Pak JE, Ekendé EN, Kifle EG, O'Connell JD 3rd, De Angelis F, Tessema MB, Derfoufi KM, Robles-Colmenares Y, Robbins RA, Goormaghtigh E, Vandenbussche G, & Stroud RM (2013). Structures of intermediate transport states of ZneA, a Zn(II)/proton antiporter. Proc Natl Acad Sci USA 110 :18484-18489. PubMed Id: 24173033. doi:10.1073/pnas.1318705110.
*CusA metal-ion efflux pump: Escherichia coli* B Bacteria, 3.52 Å** Pumps out Ag⁺ and Cu⁺ ions.	3K07	Data File Jmol Viewer 3K07	Long et al. (2010). Long F, Su CC, Zimmermann MT, Boyken SE, Rajashankar KR, Jernigan RL, & Yu EW (2010). Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport. Nature 467 :484-488. PubMed Id: 20865003.
*CusBA heavy-metal efflux complex: Escherichia coli* B Bacteria, 2.90 Å** CusA is the efflux transporter located in the inner membrane. CusB, located in the periplasmic space, is a so-called membrane fusion protein that bridges CusA to CusC to form the tripartite efflux complex CusCBA.	3NE5	Data File Jmol Viewer 3NE5	Su et al. (2011). Su CC, Long F, Zimmermann MT, Rajashankar KR, Jernigan RL, & Yu EW (2011). Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli. Nature 470 :558-562. PubMed Id: 21350490. doi:10.1038/nature09743.
*CusB membrane fusion protein (apo protein): Escherichia coli* B Bacteria, 3.40 Å** Note: 3OOC supersedes 3H9I, 3OPO supersedes 3H94, and 3OW7 supersedes 3H9T With bound Ag(I), 3.85 Å: 3OPO With bound Cu(I), 3.78 Å: 3OW7	3OOC	Data File Jmol Viewer 3OOC 3OW7 3OPO	Su et al. (2009). Su CC, Yang F, Long F, Reyon D, Routh MD, Kuo DW, Mokhtari AK, Van Ornam JD, Rabe KL, Hoy JA, Lee YJ, Rajashankar KR, & Yu EW (2009). Crystal structure of the membrane fusion protein CusB from Escherichia coli. J Mol Biol 393 :342-355. PubMed Id: 19695261. doi:10.1016/j.jmb.2009.08.029.
*CusA metal-ion efflux pump, symmetric closed state: Escherichia coli* B Bacteria, 3.20 Å** cryo-EM structure homogeneous binding copper(1) state, 3.40 Å: 7KF6 heterogeneous 1 open and 2 closed protomer conformation, 2.80 Å: 7KF7 heterogeneous 2 open and 1 closed protomer conformation, 3.00 Å: 7KF8	7KF5	Data File Jmol Viewer 7KF5 7KF8 7KF6 7KF7	Moseng et al. (2021). Moseng MA, Lyu M, Pipatpolkai T, Glaza P, Emerson CC, Stewart PL, Stansfeld PJ, & Yu EW (2021). Cryo-EM Structures of CusA Reveal a Mechanism of Metal-Ion Export. mBio 12 2:e00452-21. PubMed Id: 33820823. doi:10.1128/mBio.00452-21.
*EmrE bacterial multi-drug efflux transporter with bound TPP substrate: Escherichia coli* B Bacteria, 3.8 Å** 3B5D is C2 crystal form. P2₁ form with TPP, 4.5 Å: 3B62 3B5D and 3B62 expressed in cell-free system. Ligand-free structure expressed in vivo, 4.5 Å: 3B61	3B5D	Data File Jmol Viewer 3B5D 3B62 3B61	Chen et al. (2007). Chen YJ, Pornillos O, Lieu S, Ma C, Chen AP, & Chang G (2007). X-ray structure of EmrE supports dual topology model. Proc Natl Acad Sci USA 104 :18999-19004. PubMed Id: 18024586.
*EmrE bacterial multi-drug efflux transporter, S64V mutant bound to tetra(4-fluorophenyl)phosphonium at pH 5.8: Escherichia coli* B Bacteria, NMR structure**	7JK8	Data File Jmol Viewer 7JK8	Shcherbakov et al. (2021). Shcherbakov AA, Hisao G, Mandala VS, Thomas NE, Soltani M, Salter EA, Davis JH Jr, Henzler-Wildman KA, & Hong M (2021). Structure and dynamics of the drug-bound bacterial transporter EmrE in lipid bilayers. Nat Commun 12 1:172. PubMed Id: 33420032. doi:10.1038/s41467-020-20468-7.
*EmrE bacterial multi-drug efflux transporter, S64V mutant Bound to tetra(4-fluorophenyl)phosphonium at pH 8.0: Escherichia coli* B Bacteria, NMR structure**	7SFQ	Data File Jmol Viewer 7SFQ	Shcherbakov et al. (2022). Shcherbakov AA, Spreacker PJ, Dregni AJ, Henzler-Wildman KA, & Hong M (2022). High-pH structure of EmrE reveals the mechanism of proton-coupled substrate transport. Nat Commun 13 1:991. PubMed Id: 35181664. doi:10.1038/s41467-022-28556-6.
*EmrE-D3 mutant bacterial multi-drug efflux transporter in complex with monobody L10 in low pH (protonated state): Escherichia coli* B Bacteria, 2.85 Å** in complex with methyl viologen, 3.13 Å 7MGX in complex with harmane, 3.90 Å 7SVX in complex with methyltriphenylphosphonium, 3.22 Å 7SSU in complex with TPP, 3.66 Å 7SV9 in complex with benzyltrimethylammonium, 3.91 Å 7T00 Gdx-Clo from Small Multidrug Resistance family of transporters in low pH (protonated state), 2.32 Å 7SZT	7MH6	Data File Jmol Viewer 7MH6 7SV9 7SSU 7MGX 7T00 7SZT 7SVX	Kermani et al. (2022). Kermani AA, Burata OE, Koff BB, Koide A, Koide S, & Stockbridge RB (2022). Crystal structures of bacterial small multidrug resistance transporter EmrE in complex with structurally diverse substrates. Elife 11 :e76766. PubMed Id: 35254261. doi:10.7554/eLife.76766.
*Gdx-Clo multi-drug efflux transporter: Clostridiales bacterium oral taxon 876* B Bacteria (expressed in E. coli), 3.50 Å** in complex with phenylguanidinium, 2.53 Å: 6WK8 in complex with octylguanidinium, 2.32 Å: 6WK9	6WK5	Data File Jmol Viewer 6WK5 6WK9 6WK8	Kermani et al. (2020). Kermani AA, Macdonald CB, Burata OE, Ben Koff B, Koide A, Denbaum E, Koide S, & Stockbridge RB (2020). The structural basis of promiscuity in small multidrug resistance transporters. Nat Commun 11 1:6064. PubMed Id: 33247110. doi:10.1038/s41467-020-19820-8.
*NorM Multidrug and Toxin Compound Extrusion (MATE) transporter (apo form): Vibrio cholerae* B Bacteria (expressed in E. coli), 3.65 Å** With bound Rb⁺, 4.20 Å: 3MKU	3MKT	Data File Jmol Viewer 3MKT 3MKU	He et al. (2010). He X, Szewczyk P, Karyakin A, Evin M, Hong WX, Zhang Q, & Chang G (2010). Structure of a cation-bound multidrug and toxic compound extrusion transporter. Nature 467 :991-994. PubMed Id: 20861838.
*NorM Multidrug and Toxin Compound Extrusion (MATE) transporter: Vibrio cholerae* B Bacteria (expressed in E. coli), 3.47 Å** cryo-EM structure structure determined by NabFab-fiducial assisted cryo-EM	7PHP	Data File Jmol Viewer 7PHP	Bloch et al. (2021). Bloch JS, Mukherjee S, Kowal J, Filippova EV, Niederer M, Pardon E, Steyaert J, Kossiakoff AA, & Locher KP (2021). Development of a universal nanobody-binding Fab module for fiducial-assisted cryo-EM studies of membrane proteins. Proc Natl Acad Sci U S A 118 47:e2115435118. PubMed Id: 34782475. doi:10.1073/pnas.2115435118.
*NorM Multidrug and Toxin Compound Extrusion (MATE) transporter in complex with tetraphenylphosphonium: Neisseria gonorrhoeae* B Bacteria (expressed in E. coli), 3.59 Å** Complex with Cs⁺, 3.81 Å: 4HUL Complex with ethidium, 3.49 Å: 4HUM Complex with rhodamine 6G, 3.59 Å: 4HUN	4HUK	Data File Jmol Viewer 4HUK 4HUM 4HUL 4HUN	Lu et al. (2013). Lu M, Symersky J, Radchenko M, Koide A, Guo Y, Nie R, & Koide S (2013). Structures of a Na⁺-coupled, substrate-bound MATE multidrug transporter. Proc Natl Acad Sci USA 110 :2099-2104. PubMed Id: 23341609. doi:10.1073/pnas.1219901110.
*NorM Multidrug and Toxin Compound Extrusion (MATE) transporter in complex with verapamil: Neisseria gonorrhoeae* B Bacteria (expressed in E. coli), 3.00 Å**	5C6P	Data File Jmol Viewer 5C6P	Radchenko et al. (2015). Radchenko M, Symersky J, Nie R, & Lu M (2015). Structural basis for the blockade of MATE multidrug efflux pumps. Nat Commun 6 :7995. PubMed Id: 26246409. doi:10.1038/ncomms8995.
*Multidrug and Toxin Compound Extrusion (MATE) transporter; outward-open apo form, straight conformation: Pyrococcus furiosus* A Archaea (expressed in E. coli), 2.40 Å** outward-open apo form, bent conformation, 2.50 Å: 3VVO in complex with Br-NRF, 2.91 Å: 3VVP in complex with MaL6, 2.40 Å: 3VVQ in complex with MaD5, 3.00 Å: 3VVR in complex with MaD3S, 2.60 Å: 3VVS P26A mutant, 2.10 Å: 3W4T	3VVN	Data File Jmol Viewer 3VVN 3VVQ 3VVR 3VVP 3W4T 3VVO 3VVS	Tanaka et al. (2013). Tanaka Y, Hipolito CJ, Maturana AD, Ito K, Kuroda T, Higuchi T, Katoh T, Kato HE, Hattori M, Kumazaki K, Tsukazaki T, Ishitani R, Suga H, & Nureki O (2013). Structural basis for the drug extrusion mechanism by a MATE multidrug transporter. Nature 496 :247-251. PubMed Id: 23535598. doi:10.1038/nature12014.
*Multidrug and Toxin Compound Extrusion (MATE) transporter, inward-facing conformation, lipidic cubic phase: Pyrococcus furiosus* B Bacteria (expressed in E. coli), 2.8 Å** outward-facing conformation, 2.8 Å: 6GWH outward-facing (vapor diffusion method), 3.50 Å: 6HFB outward-facing (vapor diffusion method), 2.35 Å: 4MLB	6FHZ	Data File Jmol Viewer 6FHZ 6GWH 4MLB 6HFB	Zakrzewska et al. (2019). Zakrzewska S, Mehdipour AR, Malviya VN, Nonaka T, Koepke J, Muenke C, Hausner W, Hummer G, Safarian S, & Michel H (2019). Inward-facing conformation of a multidrug resistance MATE family transporter. Proc Natl Acad Sci USA 116 25:12275-12284. PubMed Id: 31160466. doi:10.1073/pnas.1904210116.
*DinF-BH Multidrug and Toxin Compound Extrusion (MATE) transporter: Bacillus halodurans* B Bacteria (expressed in E. coli), 3.20 Å** In complex with R6G, 3.70 Å: 4LZ9	4LZ6	Data File Jmol Viewer 4LZ6 4LZ9	Lu et al. (2013). Lu M, Radchenko M, Symersky J, Nie R, & Guo Y (2013). Structural insights into H⁺-coupled multidrug extrusion by a MATE transporter. Nat. Struct. Mol. Biol. 20 :1310-1317. PubMed Id: 24141706. doi:10.1038/nsmb.2687.
*DinF-BH Multidrug and Toxin Compound Extrusion (MATE) transporter, D40N mutant: Bacillus halodurans* B Bacteria (expressed in E. coli), 3.00 Å** with bound verapmil, 3.00 Å: 5C6O	5C6N	Data File Jmol Viewer 5C6N 5C6O	Radchenko et al. (2015). Radchenko M, Symersky J, Nie R, & Lu M (2015). Structural basis for the blockade of MATE multidrug efflux pumps. Nat Commun 6 :7995. PubMed Id: 26246409. doi:10.1038/ncomms8995.
*ClbM Multidrug and Toxin Compound Extrusion (MATE) transporter: Escherichia coli* B Bacteria, 2.70 Å** in complex with Rb⁺, 3.30 Å: 4Z3P	4Z3N	Data File Jmol Viewer 4Z3N 4Z3P	Mousa et al. (2016). Mousa JJ, Yang Y, Tomkovich S, Shima A, Newsome RC, Tripathi P, Oswald E, Bruner SD, & Jobin C (2016). MATE transport of the E. coli-derived genotoxin colibactin. Nat Microbiol 1 :15009. PubMed Id: 27571755. doi:10.1038/nmicrobiol.2015.9.
*VcmN Multidrug and Toxin Compound Extrusion (MATE) transporter, straight form: Vibrio cholerae* B Bacteria (expressed in E. coli), 2.20 Å** bent form, 2.50 Å: 6IDR D35N mutant, 2.78 Å: 6IDS	6IDP	Data File Jmol Viewer 6IDP 6IDS 6IDR	Kusakizako et al. (2019). Kusakizako T, Claxton DP, Tanaka Y, Maturana AD, Kuroda T, Ishitani R, Mchaourab HS, & Nureki O (2019). Structural Basis of H⁺-Dependent Conformational Change in a Bacterial MATE Transporter. Structure 27 2:293-301.e3. PubMed Id: 30449688. doi:10.1016/j.str.2018.10.004.
*Aq_128 MATE family multidrug resistance transporter, outward-facing state: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.00 Å** in the outward-facing state, 3.00 Å 6FV8 Monomer, outward-facing state, 3.80 Å 6FV6	6Z70	Data File Jmol Viewer 6Z70 6FV8 6FV6	Zhao et al. (2021). Zhao J, Xie H, Mehdipour AR, Safarian S, Ermler U, Münke C, Thielmann Y, Hummer G, Ebersberger I, Wang J, & Michel H (2021). The structure of the Aquifex aeolicus MATE family multidrug resistance transporter and sequence comparisons suggest the existence of a new subfamily. Proc Natl Acad Sci U S A 118 46:e2107335118. PubMed Id: 34753818. doi:10.1073/pnas.2107335118.
*MurJ lipid II flippase: Thermosipho africanus* B Bacteria (expressed in E. coli), 2.0 Å** This protein flips the lipid-linked PG precursor lipid II across the cytoplasmic membrane. It is a member of the MATE transporter family	5T77	Data File Jmol Viewer 5T77	Kuk et al. (2017). Kuk AC, Mashalidis EH, & Lee SY (2017). Crystal structure of the MOP flippase MurJ in an inward-facing conformation. Nat. Struct. Mol. Biol. 24 :171-176. PubMed Id: 28024149. doi:10.1038/nsmb.3346.
*MurJ lipid II flippase, inward closed conformation: Thermosipho africanus* B Bacteria (expressed in E. coli), 3.2 Å** inward open conformation, 3 Å: 6NC7 inward occluded conformation, 2.60 Å: 6NC8 outward-facing conformation, 1.8 Å: 6NC9	6NC6	Data File Jmol Viewer 6NC6 6NC7 6NC8 6NC9	Kuk et al. (2019). Kuk ACY, Hao A, Guan Z, & Lee SY (2019). Visualizing conformation transitions of the Lipid II flippase MurJ. Nat Commun 10 1. PubMed Id: 30988294. doi:10.1038/s41467-019-09658-0.
*MurJ lipid II flippase: Escherichia coli* B Bacteria, 3.5 Å**	6CC4	Data File Jmol Viewer 6CC4	Zheng et al. (2018). Zheng S, Sham LT, Rubino FA, Brock KP, Robins WP, Mekalanos JJ, Marks DS, Bernhardt TG, & Kruse AC (2018). Structure and mutagenic analysis of the lipid II flippase MurJ from Escherichia coli. Proc Natl Acad Sci USA 115 26:6709-6714. PubMed Id: 29891673. doi:10.1073/pnas.1802192115.
*MurJ lipid II flippase, squeezed form: Escherichia coli* B Bacteria, 2.55 Å**	7WAG	Data File Jmol Viewer 7WAG	Kohga et al. (2022). Kohga H, Mori T, Tanaka Y, Yoshikaie K, Taniguchi K, Fujimoto K, Fritz L, Schneider T, & Tsukazaki T (2022). Crystal structure of the lipid flippase MurJ in a "squeezed" form distinct from its inward- and outward-facing forms. Structure 30 8:1088-1097.e3. PubMed Id: 35660157. doi:10.1016/j.str.2022.05.008.
*MurJ lipid II flippase, inward closed form: Arsenophonus endosymbiont* B Bacteria (expressed in E. coli), 2.80 Å** inward occluded form, 2.35 Å: 7WAX	7WAW	Data File Jmol Viewer 7WAW 7WAX	Kohga et al. (2022). Kohga H, Mori T, Tanaka Y, Yoshikaie K, Taniguchi K, Fujimoto K, Fritz L, Schneider T, & Tsukazaki T (2022). Crystal structure of the lipid flippase MurJ in a "squeezed" form distinct from its inward- and outward-facing forms. Structure 30 8:1088-1097.e3. PubMed Id: 35660157. doi:10.1016/j.str.2022.05.008.
*MtrD Inner Membrane Multidrug Efflux Pump: Neisseria gonorrhoeae* B Bacteria (expressed in E. coli), 3.54 Å** For outer membrane component, see 4MT0	4MT1	Data File Jmol Viewer 4MT1	Bolla et al. (2014). Bolla JR, Su CC, Do SV, Radhakrishnan A, Kumar N, Long F, Chou TH, Delmar JA, Lei HT, Rajashankar KR, Shafer WM, & Yu EW (2014). Crystal structure of the Neisseria gonorrhoeae MtrD inner membrane multidrug efflux pump. PLoS ONE 9 6:e97903. PubMed Id: 24901477. doi:10.1371/journal.pone.0097903.
*MtrD Inner Membrane Multidrug Efflux Pump with bound ampicillin: Neisseria gonorrhoeae* B Bacteria (expressed in E. coli), 3.02 Å** cryo-EM structure with bound erythromycin, 2.72 Å: 6VKT	6VKS	Data File Jmol Viewer 6VKS 6VKT	Lyu et al. (2020). Lyu M, Moseng MA, Reimche JL, Holley CL, Dhulipala V, Su CC, Shafer WM, & Yu EW (2020). Cryo-EM Structures of a Gonococcal Multidrug Efflux Pump Illuminate a Mechanism of Drug Recognition and Resistance. mBio 11 3. PubMed Id: 32457251. doi:10.1128/mBio.00996-20.
*HpnN hopanoid transporter (crystal form I): Burkholderia multivorans* B Bacteria (expressed in E. coli), 3.44 Å** crystal form II, 3.76 Å: 5KHS	5KHN	Data File Jmol Viewer 5KHN 5KHS	Kumar et al. (2017). Kumar N, Su CC, Chou TH, Radhakrishnan A, Delmar JA, Rajashankar KR, & Yu EW (2017). Crystal structures of the Burkholderia multivorans hopanoid transporter HpnN. Proc Natl Acad Sci USA 114 :6557-6562. PubMed Id: 28584102. doi:10.1073/pnas.1619660114.
*HpnN hopanoid transporter: Burkholderia pseudomallei* B Bacteria (expressed in E. coli), 3.59 Å** cryo-EM structure	6WU0	Data File Jmol Viewer 6WU0	Su et al. (2021). Su CC, Lyu M, Morgan CE, Bolla JR, Robinson CV, & Yu EW (2021). A 'Build and Retrieve' methodology to simultaneously solve cryo-EM structures of membrane proteins. Nat Methods 18 1:69-75. PubMed Id: 33408407. doi:10.1038/s41592-020-01021-2.
*CmeB multi-drug efflux transporter, C2 space group: Campylobacter jejuni* B Bacteria (expressed in E. coli), 3.15 Å** P1 space group, 3.55 Å: 5LQ3	5T0O	Data File Jmol Viewer 5T0O 5LQ3	Su et al. (2017). Su CC, Yin L, Kumar N, Dai L, Radhakrishnan A, Bolla JR, Lei HT, Chou TH, Delmar JA, Rajashankar KR, Zhang Q, Shin YK, & Yu EW (2017). Structures and transport dynamics of a Campylobacter jejuni multidrug efflux pump. Nat Commun 8 1:171. PubMed Id: 28761097. doi:10.1038/s41467-017-00217-z.
*Plant MATE protein: Camelina sativa* E Eukaryota (expressed in Pichia pastoris), 2.9 Å** The first plant MATE transporter	5XJJ	Data File Jmol Viewer 5XJJ	Tanaka et al. (2017). Tanaka Y, Iwaki S, & Tsukazaki T (2017). Crystal Structure of a Plant Multidrug and Toxic Compound Extrusion Family Protein. Structure 25 :1455-1460.e2. PubMed Id: 28877507. doi:10.1016/j.str.2017.07.009.
*MATE2 nicotine transporter: Nicotiana tabacum* E Eukaryota (expressed in Komagataella pastoris), 3.50 Å**	7DQK	Data File Jmol Viewer 7DQK	Tanaka et al. (2021). Tanaka Y, Iwaki S, Sasaki A, & Tsukazaki T (2021). Crystal structures of a nicotine MATE transporter provide insight into its mechanism of substrate transport. FEBS Lett 595 14:1902-1913. PubMed Id: 34050946. doi:10.1002/1873-3468.14136.
*Patched1 (Ptch1) of the Hedgehog (Hh) signaling pathway, wild-type: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.9 Å** cryo-EM structure. While not a multi-drug transporter, it is structurally similar. L282Q/T500F/P504L mutant, 4.1 Å: 6DMO ShhN-bound form, 3.6 Å: 6DMY	6DMB	Data File Jmol Viewer 6DMB 6DMY 6DMO	Gong et al. (2018). Gong X, Qian H, Cao P, Zhao X, Zhou Q, Lei J, & Yan N (2018). Structural basis for the recognition of Sonic Hedgehog by human Patched1. Science 361 6402:568. PubMed Id: 29954986. doi:10.1126/science.aas8935.
*Patched1 (Ptch1) of the Hedgehog (Hh) signaling pathway: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure. Previous PDB codes: 6D4H & 6D4J in complex with native Sonic Hedgehog, 3.80 Å: 6OEV	6OEU	Data File Jmol Viewer 6OEU 6OEV	Qi et al. (2018). Qi X, Schmiege P, Coutavas E, Wang J, & Li X (2018). Structures of human Patched and its complex with native palmitoylated sonic hedgehog. Nature 560 7716:128-132. PubMed Id: 29995851. doi:10.1038/s41586-018-0308-7.
*2:1 human Ptch1-SHH-N complex: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.5 Å** cryo-EM structure	6E1H	Data File Jmol Viewer 6E1H	Qi et al. (2018). Qi X, Schmiege P, Coutavas E, & Li X (2018). Two Patched molecules engage distinct sites on Hedgehog yielding a signaling-competent complex. Science 362 6410:eaas8843. PubMed Id: 30139912. doi:10.1126/science.aas8843.
*2:1 human Ptch1-SHH-N complex (revised structure): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure x-ray: ectodomain complex with nanobody NB64, 2.10 Å: 6RTY x-ray: ectodomain in complex with nanobody NB64 & cholesterol-hemisuccinate, 1.90 Å: 6RTW x-ray: ectodomain 1, 1.95 Å: 6RTX x-ray: ectodomain 2 (PTCH1-ECD2) in complex with nanobody 75, 2.20 Å: 6RVC	6RVD	Data File Jmol Viewer 6RVD 6RTY 6RTW 6RVC 6RTX	Rudolf et al. (2019). Rudolf AF, Kinnebrew M, Kowatsch C, Ansell TB, El Omari K, Bishop B, Pardon E, Schwab RA, Malinauskas T, Qian M, Duman R, Covey DF, Steyaert J, Wagner A, Sansom MSP, Rohatgi R, & Siebold C (2019). The morphogen Sonic hedgehog inhibits its receptor Patched by a pincer grasp mechanism. Nat Chem Biol 15 10:975-982. PubMed Id: 31548691. doi:10.1038/s41589-019-0370-y.
*4:2 human Ptch1-SHH-N complex (form I): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 6.8 Å** cryo-EM structure in complex with SHHH-N (form II), 6.5 Å: 6N7K 2:1 Ptch1-Shhp complex, 3.6 Å: 6N7H	6N7G	Data File Jmol Viewer 6N7G 6N7K 6N7H	Qian et al. (2019). Qian H, Cao P, Hu M, Gao S, Yan N, & Gong X (2019). Inhibition of tetrameric Patched1 by Sonic Hedgehog through an asymmetric paradigm. Nat Commun 10 1. PubMed Id: 31127104. doi:10.1038/s41467-019-10234-9.
*Patched1 (Ptch1) of the Hedgehog (Hh) signaling pathway bound to ShhN_C24II: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure	6RMG	Data File Jmol Viewer 6RMG	Qi et al. (2019). Qi C, Di Minin G, Vercellino I, Wutz A, & Korkhov VM (2019). Structural basis of sterol recognition by human hedgehog receptor PTCH1. Sci Adv 5 9. PubMed Id: 31555730. doi:10.1126/sciadv.aaw6490.
*Patched1 (Ptch1) of the Hedgehog (Hh) signaling pathway: Mus musculus* E Eukaryota (expressed in Sf9 cells), 3.60 Å** Cryo-EM structure	6MG8	Data File Jmol Viewer 6MG8	Zhang et al. (2018). Zhang Y, Bulkley DP, Xin Y, Roberts KJ, Asarnow DE, Sharma A, Myers BR, Cho W, Cheng Y, & Beachy PA (2018). Structural Basis for Cholesterol Transport-like Activity of the Hedgehog Receptor Patched. Cell 175 5:1352-1364.e14. PubMed Id: 30415841. doi:10.1016/j.cell.2018.10.026.
*Patched1 (Ptch1) of the Hedgehog (Hh) signaling pathway in complex with conformation selective nanobody TI23: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure	7K65	Data File Jmol Viewer 7K65	Zhang et al. (2020). Zhang Y, Lu WJ, Bulkley DP, Liang J, Ralko A, Han S, Roberts KJ, Li A, Cho W, Cheng Y, Manglik A, & Beachy PA (2020). Hedgehog pathway activation through nanobody-mediated conformational blockade of the Patched sterol conduit. Proc Natl Acad Sci U S A 117 46:28838-28846. PubMed Id: 33139559. doi:10.1073/pnas.2011560117.
*Patched1 (Ptch1) of the Hedgehog (Hh) signaling pathway in nanodisc, wild-type: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.50 Å** formerly 7DZQ & 7DZR cryo-EM structure V1084A mutant, 3.64 Å 7V6Z	7V6Y	Data File Jmol Viewer 7V6Y 7V6Z	Luo et al. (2021). Luo Y, Wan G, Zhang X, Zhou X, Wang Q, Fan J, Cai H, Ma L, Wu H, Qu Q, Cong Y, Zhao Y, & Li D (2021). Cryo-EM study of patched in lipid nanodisc suggests a structural basis for its clustering in caveolae. Structure 29 . PubMed Id: 34174188. doi:10.1016/j.str.2021.06.004.
*Dispatched of the Hedgehog (Hh) signaling pathway: Drosophila melanogaster* E Eukaryota (expressed in HEK293 cells), 3.16 Å** cryo-EM structure bound to a modified Hedgehog ligand, HhN-C85II, 4.76 Å:	6TBU	Data File Jmol Viewer 6TBU	Cannac et al. (2020). Cannac F, Qi C, Falschlunger J, Hausmann G, Basler K, & Korkhov VM (2020). Cryo-EM structure of the Hedgehog release protein Dispatched. Sci Adv 6 16. PubMed Id: 32494603. doi:10.1126/sciadv.aay7928.
*Dispatched-1 (DISP1) of the Hedgehog (Hh) signaling pathway: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.53 Å** cryo-EM structure	6XE6	Data File Jmol Viewer 6XE6	Chen et al. (2020). Chen H, Liu Y, & Li X (2020). Structure of human Dispatched-1 provides insights into Hedgehog ligand biogenesis. Life Sci Alliance 3 8:e202000776. PubMed Id: 32646883. doi:10.26508/lsa.202000776.
*Dispatched-1 (DISP1) of the Hedgehog (Hh) signaling pathway, Disp1^NNN-3C: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.61 Å** cryo-EM structure Disp1^NNN-3C-Cleavage, 3.68 Å 7E2H Disp1^NNN-ShhN, 4.07 Å 7E2I	7E2G	Data File Jmol Viewer 7E2G 7E2I 7E2H	Li et al. (2021). Li W, Wang L, Wierbowski BM, Lu M, Dong F, Liu W, Li S, Wang P, Salic A, & Gong X (2021). Structural insights into proteolytic activation of the human Dispatched1 transporter for Hedgehog morphogen release. Nat Commun 12 1:6966. PubMed Id: 34845226. doi:10.1038/s41467-021-27257-w.
*Dispatched-1 (DISP1) homolog of the Hedgehog (Hh) signaling pathway, 'R' conformation: Mus musculus* E Eukaryota (expressed in HEK293 cells), 2.50 Å** cryo-EM structure 'T' conformation, 2.50 Å 7RPI NNN mutant, 3.20 Å 7RPj complex with Sonic hedgehog, 2.70 Å 7RPK	7RPH	Data File Jmol Viewer 7RPH 7RPj 7RPI 7RPK	Wang et al. (2021). Wang Q, Asarnow DE, Ding K, Mann RK, Hatakeyama J, Zhang Y, Ma Y, Cheng Y, & Beachy PA (2021). Dispatched uses Na⁺ flux to power release of lipid-modified Hedgehog. Nature 599 7884:320-324. PubMed Id: 34707294. doi:10.1038/s41586-021-03996-0.
*MmpL3 mycolic acid transporter: Mycobacterium smegmatis* B Bacteria, 2.70 Å** MmpL3 is an important drug target for anti-tuberculosis drugs. It is a member of the resistance and cell division (RND) superfamily. in complex with SQ109, 2.60 Å: 6AJG in complex with AU1235, 2.82 Å: 6AJH in complex with ICA38, 2.79 Å: 6AJJ in complex with Rimonabant, 2.9 Å: 6AJI	6AJF	Data File Jmol Viewer 6AJF 6AJJ 6AJI 6AJH 6AJG	Zhang et al. (2019). Zhang B, Li J, Yang X, Wu L, Zhang J, Yang Y, Zhao Y, Zhang L, Yang X, Yang X, Cheng X, Liu Z, Jiang B, Jiang H, Guddat LW, Yang H, & Rao Z (2019). Crystal Structures of Membrane Transporter MmpL3, an Anti-TB Drug Target. Cell 176 3:636-648.e13. PubMed Id: 30682372. doi:10.1016/j.cell.2019.01.003.
*MmpL3 mycolic acid transporter with bound phosphatidylethanolamine: Mycobacterium smegmatis* B Bacteria (expressed in E. coli), 2.59 Å** 6OR2 supersedes 6N3T. Truncated protein: residues 1-773 full-length protein, 3.31 Å: 6N40	6OR2	Data File Jmol Viewer 6OR2 6N40	Su et al. (2019). Su CC, Klenotic PA, Bolla JR, Purdy GE, Robinson CV, & Yu EW (2019). MmpL3 is a lipid transporter that binds trehalose monomycolate and phosphatidylethanolamine. Proc Natl Acad Sci USA 116 23:11241-11246. PubMed Id: 31113875. doi:10.1073/pnas.1901346116.
*MmpL3 mycolic acid transporter in complex with NITD-349: Mycolicibacterium smegmatis* B Bacteria, 3.10 Å** complexed with SPIRO, 2.82 Å: 7C2N	7C2M	Data File Jmol Viewer 7C2M 7C2N	Yang et al. (2020). Yang X, Hu T, Yang X, Xu W, Yang H, Guddat LW, Zhang B, & Rao Z (2020). Structural Basis for the Inhibition of Mycobacterial MmpL3 by NITD-349 and SPIRO. J Mol Biol 432 16:4426-4434. PubMed Id: 32512002. doi:10.1016/j.jmb.2020.05.019.
*MmpL3 mycolic acid transporter in lipid nanodiscs: Mycolicibacterium smegmatis* B Bacteria (expressed in E. coli), 3.65 Å** cryo-EM structure MmpL3-GDN, 2.94 Å 7K8B MmpL3-TMM, 4.27 Å 7K8C MmpL3-TMM (form II), 4.33 Å 7K8D in the TMM bound state, 2.66 Å 7N6B x-ray structure, 3.33 Å 7K7M	7K8A	Data File Jmol Viewer 7K8A 7K8D 7N6B 7K8C 7K7M 7K8B	Su et al. (2021). Su CC, Klenotic PA, Cui M, Lyu M, Morgan CE, & Yu EW (2021). Structures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport. PLoS Biol 19 8:3001370. PubMed Id: 34383749. doi:10.1371/journal.pbio.3001370.
*MmpL3 mycolic acid transporter: Mycobacterium tuberculosis* B Bacteria (expressed in E. coli), 3.00 Å** cryo-EM structure	7NVH	Data File Jmol Viewer 7NVH	Adams et al. (2021). Adams O, Deme JC, Parker JL, , Fowler PW, Lea SM, & Newstead S (2021). Cryo-EM structure and resistance landscape of M. tuberculosis MmpL3: An emergent therapeutic target. Structure 29 10:1182-1191.e4. PubMed Id: 34242558. doi:10.1016/j.str.2021.06.013.
*TriABC Triclosan Efflux Pump: Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 4.50 Å** cryo-EM structure	6VEJ	Data File Jmol Viewer 6VEJ	Fabre et al. (2021). Fabre L, Ntreh AT, Yazidi A, Leus IV, Weeks JW, Bhattacharyya S, Ruickoldt J, Rouiller I, Zgurskaya HI, & Sygusch J (2021). A "Drug Sweeping" State of the TriABC Triclosan Efflux Pump from Pseudomonas aeruginosa. Structure 29 3:261-274.e6. PubMed Id: 32966762. doi:10.1016/j.str.2020.09.001.
*OqxB bacterial multi-drug efflux transporter: Klebsiella pneumoniae* B Bacteria (expressed in E. coli), 1.85 Å** OqxB is a member of the resistance nodulation and cell division (RND) superfamily.	7CZ9	Data File Jmol Viewer 7CZ9	Bharatham et al. (2021). Bharatham N, Bhowmik P, Aoki M, Okada U, Sharma S, Yamashita E, Shanbhag AP, Rajagopal S, Thomas T, Sarma M, Narjari R, Nagaraj S, Ramachandran V, Katagihallimath N, Datta S, & Murakami S (2021). Structure and function relationship of OqxB efflux pump from Klebsiella pneumoniae. Nat Commun 12 1:5400. PubMed Id: 34518546. doi:10.1038/s41467-021-25679-0.
*AdeB multidrug transporter, OOO state: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 3.54 Å** cryo-EM structure L*OO state, 3.84 Å 7B8Q	7B8P	Data File Jmol Viewer 7B8P 7B8Q	Ornik-Cha et al. (2021). Ornik-Cha A, Wilhelm J, Kobylka J, Sjuts H, Vargiu AV, Malloci G, Reitz J, Seybert A, Frangakis AS, & Pos KM (2021). Structural and functional analysis of the promiscuous AcrB and AdeB efflux pumps suggests different drug binding mechanisms. Nat Commun 12 1:6919. PubMed Id: 34824229. doi:10.1038/s41467-021-27146-2.
*NorA efflux pump in complex with Fab25: Staphylococcus aureus* B Bacteria (expressed in E. coli), 3.74 Å** cryo-EM structure in complex with Fab36, 3.16 Å: 7LO8	7LO7	Data File Jmol Viewer 7LO7 7LO8	Brawley et al. (2022). Brawley DN, Sauer DB, Li J, Zheng X, Koide A, Jedhe GS, Suwatthee T, Song J, Liu Z, Arora PS, Koide S, Torres VJ, Wang DN, & Traaseth NJ (2022). Structural basis for inhibition of the drug efflux pump NorA from Staphylococcus aureus. Nat Chem Biol 18 7:706-712. PubMed Id: 35361990. doi:10.1038/s41589-022-00994-9.
*BpeB bacterial multi-drug efflux transporter: Burkholderia pseudomallei* B Bacteria (expressed in E. coli), 2.94 Å** X-ray structure	7WLS	Data File Jmol Viewer 7WLS	Kato et al. (2023). Kato T, Okada U, Hung LW, Yamashita E, Kim HB, Kim CY, Terwilliger TC, Schweizer HP, & Murakami S (2023). Crystal structures of multidrug efflux transporters from Burkholderia pseudomallei suggest details of transport mechanism. Proc Natl Acad Sci U S A 120 29:e2215072120. PubMed Id: 37428905. doi:10.1073/pnas.2215072120.
*BpeF bacterial multi-drug efflux transporter: Burkholderia pseudomallei* B Bacteria (expressed in E. coli), 3.00 Å** X-ray structure	7WLV	Data File Jmol Viewer 7WLV	Kato et al. (2023). Kato T, Okada U, Hung LW, Yamashita E, Kim HB, Kim CY, Terwilliger TC, Schweizer HP, & Murakami S (2023). Crystal structures of multidrug efflux transporters from Burkholderia pseudomallei suggest details of transport mechanism. Proc Natl Acad Sci U S A 120 29:e2215072120. PubMed Id: 37428905. doi:10.1073/pnas.2215072120.
AbgT Family of Transporters Involved in bacterial folate synthesis through catabolite transport Proteins in this family may also function as drug efflux pumps
*YdaH transporter: Alcanivorax borkumensis* B Bacteria (expressed in E. coli), 2.96 Å** The first structure determined for a member of the AbgT family.	4R0C	Data File Jmol Viewer 4R0C	Bolla et al. (2015). Bolla JR, Su CC, Delmar JA, Radhakrishnan A, Kumar N, Chou TH, Long F, Rajashankar KR, & Yu EW (2015). Crystal structure of the Alcanivorax borkumensis YdaH transporter reveals an unusual topology. Nat Commun 6 :6874. PubMed Id: 25892120. doi:10.1038/ncomms7874.
Sulfate-Uptake Transporters/Permeases
*CysZ sulfate permease: Idiomarina loihiensis* B Bacteria (expressed in E. coli), 2.3 Å** The subunits of this transporter, like EmrE, are organized with inverted transmembrane topology	3TX3	Data File Jmol Viewer 3TX3	Assur Sanghai et al. (2018). Assur Sanghai Z, Liu Q, Clarke OB, Belcher-Dufrisne M, Wiriyasermkul P, Giese MH, Leal-Pinto E, Kloss B, Tabuso S, Love J, Punta M, Banerjee S, Rajashankar KR, Rost B, Logothetis D, Quick M, Hendrickson WA, & Mancia F (2018). Structure-based analysis of CysZ-mediated cellular uptake of sulfate. Elife 7 :e27829. PubMed Id: 29792261. doi:10.7554/eLife.27829.
*CysZ sulfate permease: Pseudomonas fragi* B Bacteria (expressed in E. coli), 3.50 Å**	6D79	Data File Jmol Viewer 6D79	Assur Sanghai et al. (2018). Assur Sanghai Z, Liu Q, Clarke OB, Belcher-Dufrisne M, Wiriyasermkul P, Giese MH, Leal-Pinto E, Kloss B, Tabuso S, Love J, Punta M, Banerjee S, Rajashankar KR, Rost B, Logothetis D, Quick M, Hendrickson WA, & Mancia F (2018). Structure-based analysis of CysZ-mediated cellular uptake of sulfate. Elife 7 :e27829. PubMed Id: 29792261. doi:10.7554/eLife.27829.
*CysZ sulfate permease: Pseudomonas sp. ATCC 13867* B Bacteria (expressed in E. coli), 3.40 Å**	6D9Z	Data File Jmol Viewer 6D9Z	Assur Sanghai et al. (2018). Assur Sanghai Z, Liu Q, Clarke OB, Belcher-Dufrisne M, Wiriyasermkul P, Giese MH, Leal-Pinto E, Kloss B, Tabuso S, Love J, Punta M, Banerjee S, Rajashankar KR, Rost B, Logothetis D, Quick M, Hendrickson WA, & Mancia F (2018). Structure-based analysis of CysZ-mediated cellular uptake of sulfate. Elife 7 :e27829. PubMed Id: 29792261. doi:10.7554/eLife.27829.
Membrane-Associated Proteins in Eicosanoid and Glutathione Metabolism (MAPEG)
*Microsomal Glutathione Transferase 1 (MGST1): Rattus norvegicus* E Eukaryota, 3.2 Å** Electron Diffraction	2H8A	Data File Jmol Viewer 2H8A	Holm et al. (2006). Holm PJ, Bhakat P, Jegerschold C, Gyobu N, Mitsuoka K, Fujiyoshi Y, Morgenstern R, & Hebert H. (2006). Structural Basis for Detoxification and Oxidative Stress Protection in Membranes. J Mol Biol 360 :934-945. PubMed Id: 16806268.
*Microsomal Glutathione Transferase 2(MGST2): Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 2.50 Å** in complex with co-substrate Glutathione, 2.50 Å: 6SSU in complex with an Inhibitor Glutathione sulfonic acid, 3.00 Å: 6SSW neat structure at 3.80 Å: 6SSR	6SSS	Data File Jmol Viewer 6SSS 6SSW 6SSU 6SSR	Thulasingam et al. (2021). Thulasingam M, Orellana L, Nji E, Ahmad S, Rinaldo-Matthis A, & Haeggström JZ (2021). Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis. Nat Commun 12 1:1728. PubMed Id: 33741927. doi:10.1038/s41467-021-21924-8.
*Microsomal Prostaglandin E Synthase 1: Homo sapiens* E Eukaryota (expressed in E. coli), 3.5 Å** Electron Diffraction. In complex with glutathione.	3DWW	Data File Jmol Viewer 3DWW	Jegerschöld et al. (2008). Jegerschöld C, Pawelzik SC, Purhonen P, Bhakat P, Gheorghe KR, Gyobu N, Mitsuoka K, Morgenstern R, Jakobsson PJ, & Hebert H (2008). Structural basis for induced formation of the inflammatory mediator prostaglandin E2. Proc Natl Acad Sci USA 105 :11110-11115. PubMed Id: 18682561.
*Microsomal Prostaglandin E Synthase 1: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 1.16 Å** With GSH analog, 1.95 Å: 4AL1	4AL0	Data File Jmol Viewer 4AL0 4AL1	Sjögren et al. (2013). Sjögren T, Nord J, Ek M, Johansson P, Liu G, & Geschwindner S (2013). Crystal structure of microsomal prostaglandin E₂ synthase provides insight into diversity in the MAPEG superfamily. Proc Natl Acad Sci USA 110 :3806-3811. PubMed Id: 23431194. doi:10.1073/pnas.1218504110.
*Microsomal Prostaglandin E Synthase 1 with bound inhibitor DG-031: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 1.40 Å**	6VL4	Data File Jmol Viewer 6VL4	Ho et al. (2021). Ho JD, Lee MR, Rauch CT, Aznavour K, Park JS, Luz JG, Antonysamy S, Condon B, Maletic M, Zhang A, Hickey MJ, Hughes NE, Chandrasekhar S, Sloan AV, Gooding K, Harvey A, Yu XP, Kahl SD, & Norman BH (2021). Structure-based, multi-targeted drug discovery approach to eicosanoid inhibition: Dual inhibitors of mPGES-1 and 5-lipoxygenase activating protein (FLAP). Biochim Biophys Acta Gen Subj 1865 2:129800. PubMed Id: 33246032. doi:10.1016/j.bbagen.2020.129800.
*Microsomal Prostaglandin E Synthase 1 with bound compound 30: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 1.42 Å** with bound compound MF63, 1.52 Å: 4YL0 with bound compound 3, 1.41 Å: 4YL1 with bound compound 5, 1.41 Å: 4YL3	4YK5	Data File Jmol Viewer 4YK5 4YL1 4YL3 4YL0	Luz et al. (2015). Luz JG, Antonysamy S, Kuklish SL, Condon B, Lee MR, Allison D, Yu XP, Chandrasekhar S, Backer R, Zhang A, Russell M, Chang SS, Harvey A, Sloan AV, & Fisher MJ (2015). Crystal Structures of mPGES-1 Inhibitor Complexes Form a Basis for the Rational Design of Potent Analgesic and Anti-Inflammatory Therapeutics. J Med Chem 58 11:4727-4737. PubMed Id: 25961169. doi:10.1021/acs.jmedchem.5b00330.
*Microsomal Prostaglandin E Synthase 1 in complex with GSH analog, native-SAD structure determined at wavelength 2.755 Å: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 1.77 Å** X-Ray Structure	8PYV	Data File Jmol Viewer 8PYV	El Omari et al. (2023). El Omari K, Duman R, Mykhaylyk V, Orr CM, Latimer-Smith M, Winter G, Grama V, Qu F, Bountra K, Kwong HS, Romano M, Reis RI, Vogeley L, Vecchia L, Owen CD, Wittmann S, Renner M, Senda M, Matsugaki N, Kawano Y, Bowden TA, Moraes I, Grimes JM, Mancini EJ, Walsh MA, Guzzo CR, Owens RJ, Jones EY, Brown DG, Stuart DI, Beis K, & Wagner A (2023). Experimental phasing opportunities for macromolecular crystallography at very long wavelengths. Commun Chem 6 1:219. PubMed Id: 37828292. doi:10.1038/s42004-023-01014-0.
*5-Lipoxygenase-Activating Protein (FLAP) with Bound MK-591 Inhibitor: Homo sapiens* E Eukaryota (expressed in E. coli), 4.0 Å** FLAP with iodinated MK-591 analog: 2Q7R.	2Q7M	Data File Jmol Viewer 2Q7M 2Q7R	Ferguson et al. (2007). Ferguson AD, McKeever BM, Xu S, Wisniewski D, Miller DK, Yamin TT, Spencer RH, Chu L, Ujjainwalla F, Cunningham BR, Evans JF, & Becker JW (2007). Crystal structure of inhibitor-bound human 5-lipoxygenase-activating protein. Science 317 :510-512. PubMed Id: 17600184.
*5-Lipoxygenase-Activating Protein (FLAP) with bound DG-031: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.37 Å** with bound MK-866, 2.61 Å: 6VGI	6VGC	Data File Jmol Viewer 6VGC 6VGI	Ho et al. (2021). Ho JD, Lee MR, Rauch CT, Aznavour K, Park JS, Luz JG, Antonysamy S, Condon B, Maletic M, Zhang A, Hickey MJ, Hughes NE, Chandrasekhar S, Sloan AV, Gooding K, Harvey A, Yu XP, Kahl SD, & Norman BH (2021). Structure-based, multi-targeted drug discovery approach to eicosanoid inhibition: Dual inhibitors of mPGES-1 and 5-lipoxygenase activating protein (FLAP). Biochim Biophys Acta Gen Subj 1865 2:129800. PubMed Id: 33246032. doi:10.1016/j.bbagen.2020.129800.
*Leukotriene LTC₄ Synthase in complex with glutathione: Homo sapiens* E Eukaryota (expressed in Shizosaccharomyces pombe), 3.3 Å**	2PNO	Data File Jmol Viewer 2PNO	Ago et al. (2007). Ago H, Kanaoka Y, Irikura D, Lam BK, Shimamura T, Austen KF, & Miyano M (2007). Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis. Nature 448 :609-612. PubMed Id: 17632548.
*Leukotriene LTC₄ Synthase in complex with glutathione: Homo sapiens* E Eukaryota (expressed in Pichia pastoris), 2.15 Å** apo form: 2UUI, 2.00 Å.	2UUH	Data File Jmol Viewer 2UUH 2UUI	Molina et al. (2007). Molina DM, Wetterholm A, Kohl A, McCarthy AA, Niegowski D, Ohlson E, Hammarberg T, Eshaghi S, Haeggstrom JZ, & Nordlund P (2007). Structural basis for synthesis of inflammatory mediators by human leukotriene C₄synthase. Nature 448 :613-616. PubMed Id: 17632546.
*Leukotriene LTC₄ Synthase in complex with stable leukotriene analog I: Homo sapiens* E Eukaryota (expressed in Pichia pastoris), 2.75 Å** W116A mutant with analog I, 2.70 Å: 4JC7 W116F mutant with analog I, 2.40 Å: 4JRZ wild-type with analog II, 3.20 Å: 4J7T wild-type with analog III, 2.90 Å: 4J7Y	4JCZ	Data File Jmol Viewer 4JCZ 4J7T 4JC7 4JRZ 4J7Y	Niegowski et al. (2014). Niegowski D, Kleinschmidt T, Olsson U, Ahmad S, Rinaldo-Matthis A, & Haeggström JZ (2014). Crystal Structures of Leukotriene C4 Synthase in Complex with Product Analogs: IMPLICATIONS FOR THE ENZYME MECHANISM. J Biol Chem 289 :5199-5207. PubMed Id: 24366866. doi:10.1074/jbc.M113.534628.
SWEET and semiSWEET Transporters, and Their Relatives SWEETs are monsaccharide and disaccharide transporters. Bacterial homologues are semiSWEETS.
*semiSWEET transporter in occluded state: Leptospira biflexa* B Bacteria (expressed in E. coli), 2.39 Å**	4QNC	Data File Jmol Viewer 4QNC	Xu et al. (2014). Xu Y, Tao Y, Cheung LS, Fan C, Chen LQ, Xu S, Perry K, Frommer WB, & Feng L (2014). Structures of bacterial homologues of SWEET transporters in two distinct conformations. Nature 515 7527:448-452. PubMed Id: 25186729. doi:10.1038/nature13670.
*semiSWEET transporter in outward-open state: Leptospira biflexa* B Bacteria (expressed in E. coli), 2.8 Å**	5UHQ	Data File Jmol Viewer 5UHQ	Latorraca et al. (2017). Latorraca NR, Fastman NM, Venkatakrishnan AJ, Frommer WB, Dror RO, & Feng L (2017). Mechanism of Substrate Translocation in an Alternating Access Transporter. Cell 169 :96-107.e12. PubMed Id: 28340354. doi:10.1016/j.cell.2017.03.010.
*semiSWEET transporter in outward-open conformation: Vibrio sp. n418* B Bacteria (expressed in E. coli), 1.70 Å**	4QND	Data File Jmol Viewer 4QND	Xu et al. (2014). Xu Y, Tao Y, Cheung LS, Fan C, Chen LQ, Xu S, Perry K, Frommer WB, & Feng L (2014). Structures of bacterial homologues of SWEET transporters in two distinct conformations. Nature 515 7527:448-452. PubMed Id: 25186729. doi:10.1038/nature13670.
*semiSWEET transporter in occluded state: Thermodesulfovibrio yellowstonii* B Bacteria (expressed in E. coli), 2.40 Å**	4RNG	Data File Jmol Viewer 4RNG	Wang et al. (2014). Wang J, Yan C, Li Y, Hirata K, Yamamoto M, Yan N, & Hu Q (2014). Crystal structure of a bacterial homologue of SWEET transporters. Cell Res 24 12:1486-1489. PubMed Id: 25378180. doi:10.1038/cr.2014.144.
*semiSWEET transporter in inward-open conformation (crystal I): Escherichia coli* B Bacteria, 2.00 Å** outward-open state (crystal II), 3.00 Å: 4X5N (crystal I:P2₁2₁2₁. Crystal II: C2)	4X5M	Data File Jmol Viewer 4X5M 4X5N	Lee et al. (2015). Lee Y, Nishizawa T, Yamashita K, Ishitani R, & Nureki O (2015). Structural basis for the facilitative diffusion mechanism by SemiSWEET transporter. Nat Commun 6 :6112. PubMed Id: 25598322. doi:10.1038/ncomms7112.
*SWEET transporter in a homotrimeric complex: Oryza sativa* E Eukaryota (expressed in Komagataella pastoris), 3.10 Å** lower resolution structure, 3.7 Å: 5CTH	5CTG	Data File Jmol Viewer 5CTG 5CTH	Tao et al. (2015). Tao Y, Cheung LS, Li S, Eom JS, Chen LQ, Xu Y, Perry K, Frommer WB, & Feng L (2015). Structure of a eukaryotic SWEET transporter in a homotrimeric complex. Nature 527 :259-263. PubMed Id: 26479032. doi:10.1038/nature15391.
*PnuC vitamin B₃ transporter: Neisseria mucosa* B Bacteria (expressed in E. coli), 2.80 Å**	4QTN	Data File Jmol Viewer 4QTN	Jaehme et al. (2014). Jaehme M, Guskov A, & Slotboom DJ (2014). Crystal structure of the vitamin B3 transporter PnuC, a full-length SWEET homolog. Nat Struct Mol Biol 21 11:1013-1015. PubMed Id: 25291599. doi:10.1038/nsmb.2909.
*KDEL receptor with bound nanobody: Gallus gallus* E Eukaryota (expressed in S. cerevisiae), 2.23 Å** peptide-free state, 2.59 Å: 6I6B peptide-bound state, 2 Å: 6I6H	6IJ6	Data File Jmol Viewer 6IJ6 6I6B 6I6H	Bräuer et al. (2019). Bräuer P, Parker JL, Gerondopoulos A, Zimmermann I, Seeger MA, Barr FA, & Newstead S (2019). Structural basis for pH-dependent retrieval of ER proteins from the Golgi by the KDEL receptor. Science 363 6431:1103-1107. PubMed Id: 30846601. doi:10.1126/science.aaw2859.
*KDEL receptor bound to HDEL peptide at pH 6.0: Gallus gallus* E Eukaryota (expressed in S. cerevisiae), 2.24 Å** bound to RDEL peptide at pH 6.0, 2.31 Å: 6ZXR	6Y7V	Data File Jmol Viewer 6Y7V 6ZXR	Gerondopoulos et al. (2021). Gerondopoulos A, Bräuer P, Sobajima T, Wu Z, Parker JL, Biggin PC, Barr FA, & Newstead S (2021). A signal capture and proofreading mechanism for the KDEL-receptor explains selectivity and dynamic range in ER retrieval. eLife 10 :e68380. PubMed Id: 34137369. doi:10.7554/eLife.68380.
*KDEL receptor with bound nanobody-binding scaffold (Legobody): Gallus gallus* E Eukaryota (expressed in S. cerevisiae), 3.20 Å** cryo-EM structure	7RXC	Data File Jmol Viewer 7RXC	Wu & Rapoport (2021). Wu X, & Rapoport TA (2021). Cryo-EM structure determination of small proteins by nanobody-binding scaffolds (Legobodies). Proc Natl Acad Sci U S A 118 41:e2115001118. PubMed Id: 34620716. doi:10.1073/pnas.2115001118.
*Cystinosin cystine transporter bound to sybody and nanobody: Arabidopsis thaliana* E Eukaryota (expressed in Saccharomyces cerevisiae), 2.65 Å** Cystinosin is a member of the PQ-loop family of solute carrier (SLC) transporters. bound to two nanobodies, 2.33 Å: 7ZKZ in complex with Cystine and sybody, 3.37 Å: 7ZKW	7ZK1	Data File Jmol Viewer 7ZK1 7ZKW 7ZKZ	Löbel et al. (2022). Löbel M, Salphati SP, El Omari K, Wagner A, Tucker SJ, Parker JL, & Newstead S (2022). Structural basis for proton coupled cystine transport by cystinosin. Nat Commun 13 1:4845. PubMed Id: 35977944. doi:10.1038/s41467-022-32589-2.
*Cystinosin cystine transporter, lumen-open state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.32 Å** cryo-EM structure with bound cystine, 3.39 Å: 8DKM cytosol-open state, 3.18 Å: 8DKE N288K mutant, cytosol-open state, ph5.0, 3.09 Å: 8DKW N288K mutant, cytosol-open state, ph7.5, 3.00 Å: 8DKX x-ray structure, 3.40 Å: 8DYP	8DKI	Data File Jmol Viewer 8DKI 8DKX 8DKE 8DYP 8DKM 8DKW	Guo et al. (2022). Guo X, Schmiege P, Assafa TE, Wang R, Xu Y, Donnelly L, Fine M, Ni X, Jiang J, Millhauser G, Feng L, & Li X (2022). Structure and mechanism of human cystine exporter cystinosin. Cell 185 20:3739-3752.e18. PubMed Id: 36113465. doi:10.1016/j.cell.2022.08.020.
Aluminum-Activated Malate Transporter Family (ALMTs)
*Aluminum-Activated Malate Transporter 1 (ALMT1), apo state at pH 5.0: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure apo state at pH 7.5, 3.20 Å 7VQ4 malate-bound at pH 7.5, 3.10 Å 7VQ5 Al-bound at pH 5.0, 3.60 Å 7VQ7 M60A mutant, Al-bound, 3.00 Å 7VOJ	7VQ3	Data File Jmol Viewer 7VQ3 7VQ4 7VQ5 7VOJ 7VQ7	Wang et al. (2022). Wang J, Yu X, Ding ZJ, Zhang X, Luo Y, Xu X, Xie Y, Li X, Yuan T, Zheng SJ, Yang W, & Guo J (2022). Structural basis of ALMT1-mediated aluminum resistance in Arabidopsis. Cell Res 32 1:89-98. PubMed Id: 34799726. doi:10.1038/s41422-021-00587-6.
Neurotransmitter Sodium Symporter (NSS) Family NSS family catalyze uptake of a variety of neurotransmitters, amino acids, and osmolytes
*serotonin transporter in complex with paroxetine, ts2-inactive: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.30 Å** cryo-EM structure ts2-active with bound ibogaine, 4.10 Å 6DZY with bound ibogaine in occluded conformation, 4.20 Å 6DZV complex with ibogaine in the inward conformation, 3.60 Å 6DZZ	6DZW	Data File Jmol Viewer 6DZW 6DZY 6DZZ 6DZV	Coleman et al. (2019). Coleman JA, Yang D, Zhao Z, Wen PC, Yoshioka C, Tajkhorshid E, & Gouaux E (2019). Serotonin transporter-ibogaine complexes illuminate mechanisms of inhibition and transport. Nature 569 7754:141-145. PubMed Id: 31019304. doi:10.1038/s41586-019-1135-1.
*serotonin transporter in nanodisc, 5-HT bound NaCl occluded conformation: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure 5-HT bound in KCl, 3.90 Å 7LI9 apo form in presence of NaCl in occluded conformation, 4.10 Å 7LI7 apo form in presence of NaCl in inward open conformation, 3.90 Å 7LI8 apo form in KCl, 3.50 Å 7LI6	7MGW	Data File Jmol Viewer 7MGW 7LI8 7LI9 7LI6 7LI7	Yang & Gouaux (2021). Yang D, & Gouaux E (2021). Illumination of serotonin transporter mechanism and role of the allosteric site. Sci Adv 7 49:eabl3857. PubMed Id: 34851672. doi:10.1126/sciadv.abl3857.
*GABA transporter GAT1, inward-open state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.20 Å** cryo-EM structure with bound GABA in NaCl solution, inward-occluded state, 2.40 Å: 7Y7W with bound nipecotic acid in NaCl solution, inward-occluded state, 2.40 Å: 7Y7Y with bound tiagabine in NaCl solution, inward-open state, 3.20 Å: 7Y7Z	7Y7V	Data File Jmol Viewer 7Y7V 7Y7Y 7Y7Z 7Y7W	Zhu et al. (2023). Zhu A, Huang J, Kong F, Tan J, Lei J, Yuan Y, & Yan C (2023). Molecular basis for substrate recognition and transport of human GABA transporter GAT1. Nat Struct Mol Biol 30 7:1012-1022. PubMed Id: 37400655. doi:10.1038/s41594-023-00983-z.
*GABA transporter 1 (GAT1), cytosol-facing, substrate-bound: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure	8GNK	Data File Jmol Viewer 8GNK	Nayak et al. (2023). Nayak SR, Joseph D, Höfner G, Dakua A, Athreya A, Wanner KT, Kanner BI, & Penmatsa A (2023). Cryo-EM structure of GABA transporter 1 reveals substrate recognition and transport mechanism. Nat Struct Mol Biol 30 7:1023-1032. PubMed Id: 37400654. doi:10.1038/s41594-023-01011-w.
Amino Acid Secondary Transporters
*LeuT_Aa Leucine transporter: Aquifex aeolicus* B Bacteria (expressed in E. coli), 1.65 Å**	2A65	Data File Jmol Viewer 2A65	Yamashita et al. (2005). Yamashita A, Singh SK, Kawate T, Jin Y, & Gouaux E (2005). Crystal structure of a bacterial homologue of Na⁺/Cl^--dependent neurotransmitter transporters. Nature 437 :215-223. PubMed Id: 16041361.
*LeuT Leucine transporter with bound inhibitors: Aquifex aeolicus* B Bacteria (expressed in E. coli), 1.85 Å** Alanine-Sodium-Clomipramine Leucine-Sodium-Clomipramine, 2Q6H Leucine-Sodium-Imipramine, 2Q72 Leucine-Sodium-Desipramine, 2QB4	2QEI	Data File Jmol Viewer 2QEI 2Q6H 2QB4	Singh et al. (2007). Singh SK, Yamashita A, & Gouaux E (2007). Antidepressant binding site in a bacterial homologue of neurotransmitter transporters. Nature 448 :952-956. PubMed Id: 17687333.
*LeuT Leucine transporter with bound Na⁺ and tryptophan: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.00 Å** Shows the transporter in an open-to-out conformation. w. bound glycine, 2.15 Å: 3F4J w. bound alanine, 1.90 Å: 3F48 w. bound leucine (30mM), 1.80 Å: 3F3E w. bound methionine, 1.90 Å: 3F3D w. bound selenomethionine, 1.95 Å: 3F4I w. bound 4-fluorophenylalanine, 2.10 Å: 3F3C	3F3A	Data File Jmol Viewer 3F3A 3F48 3F4I 3F3E 3F3C 3F3D 3F4J	Singh et al. (2009). Singh SK, Piscitelli CL, Yamashita A, & Gouaux E (2009). A competitive inhibitor traps LeuT in an open-to-out conformation. Science 322 :1655-1661. PubMed Id: 19074341.
*LeuT Leucine Transporter with Bound Desipramine: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.9 Å**	2QJU	Data File Jmol Viewer 2QJU	Zhou et al. (2007). Zhou Z, Zhen J, Karpowich NK, Goetz RM, Law CJ, Reith ME, & Wang DN (2007). LeuT-desipramine structure reveals how antidepressants block neurotransmitter reuptake. Science 317 :1390-1393. PubMed Id: 17690258.
*Wild-type LeuT transporter with bound octylglucopyranoside (OG): Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.0 Å** E290S mutant with bound OG, 2.8 Å: 3GJC	3GJD	Data File Jmol Viewer 3GJD 3GJC	Quick et al. (2009). Quick M, Winther AM, Shi L, Nissen P, Weinstein H, & Javitch JA (2009). Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation. Proc. Natl. Acad. Sci. USA 106 :5563-5568. PubMed Id: 19307590.
*Mutant LeuT transporter with Nitroxide Spin Label (F177R1): Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.25 Å** I204R1 mutant, 2.25 Å: 3MPQ	3MPN	Data File Jmol Viewer 3MPN 3MPQ	Kroncke et al. (2010). Kroncke BM, Horanyi PS, Columbus L. (2010). Structural Origins of Nitroxide Side Chain Dynamics on Membrane Protein Î±-Helical Sites. Biochemistry 49 :10045-10060. PubMed Id: 20964375.
*LeuT engineered to transport tryptophan (F259V): Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.63 Å** All structures are with protein-bound Na⁺ & L-Trp I359Q mutant, 2.60 Å: 3QS5 F259V,I359Q mutant, 2.80 Å:3QS6	3QS4	Data File Jmol Viewer 3QS4 3QS5 3QS6	Piscitelli & Gouaux (2012). Piscitelli CL & Gouaux E (2012). Insights into transport mechanism from LeuT engineered to transport tryptophan. EMBO J 31 :228-235. PubMed Id: 21952050. doi:10.1038/emboj.2011.353.
*Crystal Structure of LeuT in the outward-open conformation in complex with Fab: Aquifex aeolicus* B Bacteria (expressed in E. coli), 3.10 Å** (LeuT^K(Y108F)-2B12 Complex) LeuT in the inward-open conformation in complex with Fab, 3.22 Å: 3TT3 (LeuT^K(TSY)-6A10 complex) LeuT mutant T355V, S354A, K288A in complex with alanine and sodium, 2.99 Å: 3TU0 (LeuT^K(TS) complex with Ala)	3TT1	Data File Jmol Viewer 3TT1 3TT3 3TU0	Krishnamurthy & Gouaux (2012). Krishnamurthy H & Gouaux E (2012). X-ray structures of LeuT in substrate-free outward-open and apo inward-open states. Nature 481 :469-474. PubMed Id: 22230955. doi:10.1038/nature10737.
*LeuT Leucine Transporter Crystallized from Bicelles: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.50 Å** 3USG is designated as LeuT-Leu (C2 bicelle) LeuT-Leu (P2 bicelle), 3.11 Å: 3USI LeuT-Leu (P21 form A bicelle), 3.50 Å: 3USJ LeuT-Leu (P21 form B bicelle), 4.50 Å: 3USK LeuT-SeMet (C2 bicelle), 2.71 Å: 3USL LeuT-SeMet (C2 bicelle, collected at 1.2 Å), 3.01 Å: 3USM LeuT-SeMet (P21212 bicelle), 4.50 Å: 3USO LeuT-β-SeHG (C2 β-SeHG), 2.10 Å: 3USP	3USG	Data File Jmol Viewer 3USG 3USM 3USO 3USI 3USJ 3USP 3USL 3USK	Wang et al. (2012). Wang H, Elferich J, & Gouaux E (2012). Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context. Nature Struc Mol Biol 19 :212-219. PubMed Id: 22245965. doi:10.1038/nsmb.2215.
*LeuT in outward-facing Na⁺-free state, pH 6.5: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.50 Å** in Na⁺-free return state, pH 5.0, 3.02 Å: 5JAF T354H mutant in the outward-oriented Na⁺-free return state, 2.58 Å: 5JAG	5JAE	Data File Jmol Viewer 5JAE 5JAG 5JAF	Malinauskaite et al. (2016). Malinauskaite L, Said S, Sahin C, Grouleff J, Shahsavar A, Bjerregaard H, Noer P, Severinsen K, Boesen T, Schiφtt B, Sinning S, & Nissen P (2016). A conserved leucine occupies the empty substrate site of LeuT in the Na⁺-free return state. Nat Commun 7 :11673. PubMed Id: 27221344. doi:10.1038/ncomms11673.
*LeuT Leucine Transporter, substrate bound in inward-facing occluded conformation: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.6 Å**	6XWM	Data File Jmol Viewer 6XWM	Gotfryd et al. (2020). Gotfryd K, Boesen T, Mortensen JS, Khelashvili G, Quick M, Terry DS, Missel JW, LeVine MV, Gourdon P, Blanchard SC, Javitch JA, Weinstein H, Loland CJ, Nissen P, & Gether U (2020). X-ray structure of LeuT in an inward-facing occluded conformation reveals mechanism of substrate release. Nat Commun 11 1. PubMed Id: 32081981. doi:10.1038/s41467-020-14735-w.
*LeuBAT Δ13 mutant with bound paroxetine: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.89 Å** LeuBAT is an engineered LeuT harboring the human biogenic amine transporter (BAT) binding motif. Δ13 mutant with bound sertraline, 3.20 Å: 4MM5 Δ13 mutant with bound duloxetine, 3.10 Å: 4MM6 Δ13 mutant with bound desvenlafaxine, 2.85 Å: 4MM7 Δ13 mutant with bound fluoxetine, 3.31 Å: 4MM8 Δ13 mutant with bound fluvoxamine, 2.90 Å: 4MM9 Δ13 mutant with bound clomipramine, 3.30 Å: 4MMA Δ6 mutant with bound sertraline, 2.25 Å: 4MMB Δ6 mutant with bound desvenlafaxine, 2.30 Å: 4MMC Δ6 mutant with bound duloxetine, 2.30 Å: 4MMD Δ6 mutant with bound mazindol, 2.50 Å: 4MME Δ5 mutant with bound mazindol, 2.70 Å: 4MMF	4MM4	Data File Jmol Viewer 4MM4 4MM5 4MMA 4MMD 4MM7 4MMF 4MM8 4MM9 4MMC 4MME 4MMB 4MM6	Wang et al. (2013). Wang H, Goehring A, Wang KH, Penmatsa A, Ressler R, & Gouaux E (2013). Structural basis for action by diverse antidepressants on biogenic amine transporters. Nature 503 :141-145. PubMed Id: 24121440. doi:10.1038/nature12648.
*Glutamate Transporter Homologue (Glt_Ph): Pyrococcus horikoshii* A Archaea (expressed in E. coli), 3.50 Å** Outward-facing state	1XFH	Data File Jmol Viewer 1XFH	Yernool et al. (2004). Yernool D, Boudker O, Jin Y, & Gouaux E (2004). Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431 :811-818. PubMed Id: 15483603.
*Glutamate Transporter Homologue (Glt_Ph): Pyrococcus horikoshii* A Archaea (expressed in E. coli), 3.51 Å** Inward-facing state	3KBC	Data File Jmol Viewer 3KBC	Reyes et al. (2009). Reyes N, Ginter C, & Boudker O (2009). Transport mechanism of a bacterial homologue of glutamate transporters. Nature 462 :880-885. PubMed Id: 19924125.
*Glutamate Transporter Homologue (Glt_Ph), cross-linked V216C-M385C mutant: Pyrococcus horikoshii* A Archaea (expressed in E. coli), 3.80 Å** Two protomers are inward facing and a third is outward facing. V198C, A380C mutant, 4.66 Å: 3V8G	3V8F	Data File Jmol Viewer 3V8F 3V8G	Verdon & Boudker (2012). Verdon G & Boudker O (2012). Crystal structure of an asymmetric trimer of a bacterial glutamate transporter homolog. Nature Struc Mol Biol 19 :355-357. PubMed Id: 22343718. doi:10.1038/nsmb.2233.
*Glutamate Transporter Homologue (Glt_Ph), inward-facing apo form: Pyrococcus horikoshii* A Archaea (expressed in E. coli), 3.25 Å** Tl⁺-bound, inward-facing apo conformation, 3.75 Å: 4P1A alkali-free, inward-facing, 3.50 Å: 4P3J Tl⁺-bound inward-facing, bound conformation, 4.08 Å: 4P6H R397A mutant, outward-facing, 4.00 Å: 4OYE R397A mutant, outward-facing, Na⁺-bound, 3.39 Å: 4OYF R397A mutant, outward-facing, Na⁺/Asp-bound, 3.50 Å: 4OYG	4P19	Data File Jmol Viewer 4P19 4OYE 4OYG 4P1A 4OYF 4P6H 4P3J	Verdon et al. (2014). Verdon G, Oh S, Serio RN, & Boudker O (2014). Coupled ion binding and structural transitions along the transport cycle of glutamate transporters. eLife 3 :e02283. PubMed Id: 24842876. doi:10.7554/eLife.02283.
*Glutamate Transporter Homologue (Glt_Ph), R276S/M395R mutant, inward facing: Pyrococcus horikoshii* A Archaea (expressed in E. coli), 4.21 Å**	4X2S	Data File Jmol Viewer 4X2S	Akyuz et al. (2015). Akyuz N, Georgieva ER, Zhou Z, Stolzenberg S, Cuendet MA, Khelashvili G, Altman RB, Terry DS, Freed JH, Weinstein H, Boudker O, & Blanchard SC (2015). Transport domain unlocking sets the uptake rate of an aspartate transporter. Nature 518 7537:68-73. PubMed Id: 25652997. doi:10.1038/nature14158.
*Glutamate Transporter Homologue (Glt_Ph), L66C-S300C mutant crosslinked with divalent mercury: Pyrococcus horikoshii* A Archaea (expressed in E. coli), 4.50 Å**	4IZM	Data File Jmol Viewer 4IZM	Reyes et al. (2013). Reyes N, Oh S, & Boudker O (2013). Binding thermodynamics of a glutamate transporter homolog. Nat Struct Mol Biol 20 5:634-640. PubMed Id: 23563139. doi:10.1038/nsmb.2548.
*Glutamate Transporter Homologue (GltPh), Outward-facing state, in complex with TBOA: Pyrococcus horikoshii* A Archaea (expressed in E. coli), 3.66 Å** cryo-EM structure Inward-facing state, in complex with L-aspartate and sodium ions, 3.05 Å: 6X15 Inward-facing state, in complex with TBOA, 3.39 Å: 6X16 Inward-facing state, in complex with TFB-TBOA, 3.71 Å: 6X14 Inward-facing sodium-bound state, 3.66 Å: 6X13 Inward-facing Apo-open state, 3.52 Å: 6X12	6X17	Data File Jmol Viewer 6X17 6X12 6X15 6X14 6X13 6X16	Wang & Boudker (2020). Wang X, & Boudker O (2020). Large domain movements through the lipid bilayer mediate substrate release and inhibition of glutamate transporters. Elife 9 . PubMed Id: 33155546. doi:10.7554/eLife.58417.
*Glutamate Transporter Homologue (Glt_Ph),outward-facing state of the substrate-free Na⁺-only state: Pyrococcus horikoshii* A Archaea (expressed in E. coli), 2.50 Å**	7AHK	Data File Jmol Viewer 7AHK	Alleva et al. (2020). Alleva C, Kovalev K, Astashkin R, Berndt MI, Baeken C, Balandin T, Gordeliy V, Fahlke C, & Machtens JP (2020). Na⁺-dependent gate dynamics and electrostatic attraction ensure substrate coupling in glutamate transporters. Sci Adv 6 47. PubMed Id: 33208356. doi:10.1126/sciadv.aba9854.
*Glutamate Transporter Homologue (Glt_Ph) with L-Asp & Na⁺, outward-facing state: Pyrococcus horikoshii* A Archaea (expressed in E. coli), 3.08 Å** cryo-EM structure in intermediate outward-facing state, 3.62 Å: 6UWL	6UWF	Data File Jmol Viewer 6UWF 6UWL	Huang et al. (2020). Huang Y, Wang X, Lv G, Razavi AM, Huysmans GHM, Weinstein H, Bracken C, Eliezer D, & Boudker O (2020). Use of paramagnetic ¹⁹F NMR to monitor domain movement in a glutamate transporter homolog. Nat Chem Biol 16 9:1006-1012. PubMed Id: 32514183. doi:10.1038/s41589-020-0561-6.
*Glutamate Transporter Homologue transition state (Y204L/A345V/V366A mutant): Pyrococcus horikoshii* A Archaea (expressed in E. coli), 3.38 Å**	6V8G	Data File Jmol Viewer 6V8G	Huysmans et al. (2021). Huysmans GHM, Ciftci D, Wang X, Blanchard SC, & Boudker O (2021). The high-energy transition state of the glutamate transporter homologue GltPh. EMBO J 40 1:e105415. PubMed Id: 33185289. doi:10.15252/embj.2020105415.
*Glutamate Transporter Homologue (Glt_Ph), V216C-A391C mutant cross-linked in outward-facing state: Pyrococcus horikoshii* A Archaea (expressed in E. coli), 3.65 Å** 6X01 is by x-ray crystallography. cryo-EM structures: V216C-G388C mutant cross-linked with divalent mercury, 3.45 Å: 6WZB L152C-G321C mutant in the intermediate state, 3.70 Å: 6WYJ L152C-G321C mutant in the intermediate chloride conducting state, 4.00 Å: 6WYK L152C-G351C mutant in the intermediate outward-facing state, 3.90 Å: 6WYL	6X01	Data File Jmol Viewer 6X01 6WYJ 6WYK 6WZB 6WYL	Chen et al. (2021). Chen I, Pant S, Wu Q, Cater RJ, Sobti M, Vandenberg RJ, Stewart AG, Tajkhorshid E, Font J, & Ryan RM (2021). Glutamate transporters have a chloride channel with two hydrophobic gates. Nature 591 7849:327-331. PubMed Id: 33597752. doi:10.1038/s41586-021-03240-9.
*Glutamate Transporter Homologue (Glt_Ph), S279E/D405N mutant, in complex with L-aspartate and sodium ions: Pyrococcus horikoshii* A Archaea (expressed in E. coli), 2.20 Å** cryo-EM structure	7RCP	Data File Jmol Viewer 7RCP	Reddy et al. (2022). Reddy KD, Ciftci D, Scopelliti AJ, & Boudker O (2022). The archaeal glutamate transporter homologue GltPh shows heterogeneous substrate binding. J Gen Physiol 154 5:e202213131. PubMed Id: 35452090. doi:10.1085/jgp.202213131.
*Glutamate Transporter Homologue (Glt_Tk) with bound D-aspartate: Thermococcus kodakarensis* A Archaea (expressed in E. coli), 2.8 Å** see also 5LLM and 6GCT	6R7R	Data File Jmol Viewer 6R7R	Arkhipova et al. (2019). Arkhipova V, Trinco G, Ettema TW, Jensen S, Slotboom DJ, & Guskov A (2019). Binding and transport of D-aspartate by the glutamate transporter homolog Glt_Tk. eLife 8 :e45286. PubMed Id: 30969168. doi:10.7554/eLife.45286.
*Glutamate Transporter Homologue Glt_Tk, Na⁺ only: Thermococcus kodakarensis* A Archaea (expressed in E. coli), 3.22 Å** cryo-EM structure in the unsaturated conditions - inward-inward-outward configuration, 3.39 Å: 6XWO unsaturated conditions - outward-outward-inward configuration, 3.38 Å: 6XWP in saturated conditions, 3.41 Å: 6XWQ in the presence of TBOA inhibitor, 3.47 Å: 6XWN	6XWR	Data File Jmol Viewer 6XWR 6XWQ 6XWP 6XWO 6XWN	Arkhipova et al. (2020). Arkhipova V, Guskov A, & Slotboom DJ (2020). Structural ensemble of a glutamate transporter homologue in lipid nanodisc environment. Nat Commun 11 1:998. PubMed Id: 32081874. doi:10.1038/s41467-020-14834-8.
*Glutamate Transporter Homologue (Glt_Tk) in complex with a photo switchable compound (trans): Thermococcus kodakarensis* A Archaea (expressed in E. coli), 2.80 Å** in complex with a photo switchable compound (cis), 3.00 Å: 6ZL4 in complex with a photo cage compound, 3.20 Å: 6ZGB	6ZLH	Data File Jmol Viewer 6ZLH 6ZL4 6ZGB	Arkhipova et al. (2021). Arkhipova V, Fu H, Hoorens MWH, Trinco G, Lameijer LN, Marin E, Feringa BL, Poelarends GJ, Szymanski W, Slotboom DJ, & Guskov A (2021). Structural Aspects of Photopharmacology: Insight into the Binding of Photoswitchable and Photocaged Inhibitors to the Glutamate Transporter Homologue. J Am Chem Soc 143 3:1513-1520. PubMed Id: 33449695. doi:10.1021/jacs.0c11336.
*Glutamate Transporter Homologue (Glt_Tk), P208R mutant, with bound L-aspartate: Thermococcus kodakarensis* A Archaea, 3.16 Å** cryo-EM structure	8AFA	Data File Jmol Viewer 8AFA	Colucci et al. (2023). Colucci E, Anshari ZR, Patiño-Ruiz MF, Nemchinova M, Whittaker J, Slotboom DJ, & Guskov A (2023). Mutation in glutamate transporter homologue GltTk provides insights into pathologic mechanism of episodic ataxia 6. Nat Commun 14 1:1799. PubMed Id: 37002226. doi:10.1038/s41467-023-37503-y.
*Aspartate Transporter Li⁺-Bound State(Glt_Ph): Pyrococcus horikoshii* A Archaea (expressed in E. coli), 2.96 Å** TBOA-bound, 3.20 Å: 2NWW Sodium-bound, 3.29 Å: 2NWX	2NWL	Data File Jmol Viewer 2NWL 2NWW 2NWX	Boudker et al. (2007). Boudker O, Ryan RM, Yernool D, Shimamoto K, & Gouaux E (2007). Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Nature 445 :387-393. PubMed Id: 17230192.
*Aspartate Transporter, substrate-free: Thermococcus kodakarensis* A Archaea (expressed in E. coli), 3.00 Å**	4KY0	Data File Jmol Viewer 4KY0	Jensen et al. (2013). Jensen S, Guskov A, Rempel S, Hänelt I, & Slotboom DJ (2013). Crystal structure of a substrate-free aspartate transporter. Nat Struct Mol Biol 20 :1224-1226. PubMed Id: 24013209. doi:10.1038/nsmb.2663.
*Aspartate Transporter, apo form: Thermococcus kodakarensis* A Archaea (expressed in E. coli), 2.7 Å** with bound aspartate and Na⁺, 2.8 Å: 5E9S	5DWY	Data File Jmol Viewer 5DWY 5E9S	Guskov et al. (2016). Guskov A, Jensen S, Faustino I, Marrink SJ, & Slotboom DJ (2016). Coupled binding mechanism of three sodium ions and aspartate in the glutamate transporter homologue Glt_Tk. Nat Commun 7 :13420. PubMed Id: 27830699. doi:10.1038/ncomms13420.
*MhsT multi-hydrophobic amino acid transporter, occluded inward-facing state: Bacillus halodurans* B Bacteria (expressed in Lactococcus lactis), 2.10 Å** lipidic cubic phase form, 2.60 Å: 4US4	4US3	Data File Jmol Viewer 4US3 4US4	Malinauskaite et al. (2014). Malinauskaite L, Quick M, Reinhard L, Lyons JA, Yano H, Javitch JA, & Nissen P (2014). A mechanism for intracellular release of Na(+) by neurotransmitter/sodium symporters. Nat Struct Mol Biol 21 11:1006-1012. PubMed Id: 25282149. doi:10.1038/nsmb.2894.
Solute Carrier (SLC) Transporter Superfamily Active transporters that use Na⁺ or H⁺ electrochemical gradients Fold Atlas of the Human SLC Superfamily Xie et al. (2022)
*EAAT1 excitatory amino acid transporter 1 in complex with L-Asp and the allosteric inhibitor UCPH101: Homo sapiens* E Eukaryota (expressed in HEK293F cells), 3.25 Å** Member of the solute carrier 1 (SLC1) family of transporters. Engineered protein; thermostabilized. complex with the competitive inhibitor TFB-TBOA and the allosteric inhibitor UCPH101, 3.71 Å: 5MJU cryst-II mutant in complex with L-Asp and the allosteric inhibitor UCPH101, 3.1 Å: 5LM4 cryst-II mutant in complex with L-Asp, 3.32 Å: 5LLU	5LLM	Data File Jmol Viewer 5LLM 5LM4 5MJU 5LLU	Canul-Tec et al. (2017). Canul-Tec JC, Assal R, Cirri E, Legrand P, Brier S, Chamot-Rooke J, & Reyes N (2017). Structure and allosteric inhibition of excitatory amino acid transporter 1. Nature 544 :446-451. PubMed Id: 28424515. doi:10.1038/nature22064.
*EAAT1 excitatory amino acid transporter 1 in complex with L-ASP, three sodium ions and the allosteric inhibitor UCPH101: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.25 Å** E386Q mutant in complex with L-ASP, sodium ions and the allosteric inhibitor UCPH101, 3.65 Å 7AWQ mutant in complex with Rb and Ba and the allosteric inhibitor UCPH101, 3.92 Å 7AWN cryst-II mutant in complex with Rb and Ba ions and the allosteric inhibitor UCPH101, 3.91 Å 7AWP cryst-II mutant in complex with Ba and the allosteric inhibitor UCPH101, 3.70 Å 7AWL cryo-EM: EAAT1 in K⁺ buffer, 3.99 Å 7NPW	7AWM	Data File Jmol Viewer 7AWM 7AWP 7AWQ 7AWN 7AWL 7NPW	Canul-Tec et al. (2022). Canul-Tec JC, Kumar A, Dhenin J, Assal R, Legrand P, Rey M, Chamot-Rooke J, & Reyes N (2022). The ion-coupling mechanism of human excitatory amino acid transporters. EMBO J 41 :e108341. PubMed Id: 34747040. doi:10.15252/embj.2021108341.
*EAAT2 excitatory amino acid transporter 2 in complex with glutamate: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure complex with WAY-213613, 3.40 Å 7XR6	7XR4	Data File Jmol Viewer 7XR4 7XR6	Zhang et al. (2022). Zhang Z, Chen H, Geng Z, Yu Z, Li H, Dong Y, Zhang H, Huang Z, Jiang J, & Zhao Y (2022). Structural basis of ligand binding modes of human EAAT2. Nat Commun 13 1:3329. PubMed Id: 35680945. doi:10.1038/s41467-022-31031-x.
*EAAT2 excitatory amino acid transporter 2, inward facing WAY213613-bound state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.49 Å** cryo-EM structure substrate-free state, 3.58 Å: 7VR8	7VR7	Data File Jmol Viewer 7VR7 7VR8	Kato et al. (2022). Kato T, Kusakizako T, Jin C, Zhou X, Ohgaki R, Quan L, Xu M, Okuda S, Kobayashi K, Yamashita K, Nishizawa T, Kanai Y, & Nureki O (2022). Structural insights into inhibitory mechanism of human excitatory amino acid transporter EAAT2. Nat Commun 13 1:4714. PubMed Id: 35953475. doi:10.1038/s41467-022-32442-6.
*EAAT3 excitatory amino acid transporter 3, inward facing state in the presence of Na⁺: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.85 Å** cryo-EM structure outward facing state, in the presence of glutamate, 3.03 Å: 6X2Z Asymmetric-1o2i, 3.42 Å: 6X3E inward facing apo state, 3.03 Å: 6X3F	6X2L	Data File Jmol Viewer 6X2L 6X2Z 6X3E 6X3F	Qiu et al. (2021). Qiu B, Matthies D, Fortea E, Yu Z, & Boudker O (2021). Cryo-EM structures of excitatory amino acid transporter 3 visualize coupled substrate, sodium, and proton binding and transport. Sci Adv 7 10:eabf5814. PubMed Id: 33658209. doi:10.1126/sciadv.abf5814.
*EAAT3 excitatory amino acid transporter 3, with bound glutamate, intermediate outward-facing state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.80 Å** cryo-EM structure outward-facing state, 3.42 Å: 8CTD with bound K⁺, intermediate outward-facing state, 2.44 Å: 8CUA apo in 300 mM KCl, outward-facing state, 2.94 Å: 8CUD apo, intermediate outward facing state, 2.55 Å: 8CUI apo in 150 mM NMDG-Cl, outward-facing state, 3.04 Å: 8CUJ with bound Na⁺, outward-facing state, 2.44 Å: 8CV2 with bound Na⁺, outward-facing state, 3.04 Å: 8CV3	8CTC	Data File Jmol Viewer 8CTC 8CUI 8CUJ 8CV2 8CV3 8CUD 8CTD 8CUA	Qiu & Boudker (2023). Qiu B, & Boudker O (2023). Symport and antiport mechanisms of human glutamate transporters. Nat Commun 14 1:2579. PubMed Id: 37142617. doi:10.1038/s41467-023-38120-5.
*Neutral amino acid transporter ASCT2, inward-oriented state: Homo sapiens* E Eukaryota (expressed in K. pastoris), 3.85 Å** cryo-EM structure. Member of the SLC1A5 superfamily.	6GCT	Data File Jmol Viewer 6GCT	Garaeva et al. (2018). Garaeva AA, Oostergetel GT, Gati C, Guskov A, Paulino C, & Slotboom DJ (2018). Cryo-EM structure of the human neutral amino acid transporter ASCT2. Nat Struct Mol Biol 25 6:515-521. PubMed Id: 29872227. doi:10.1038/s41594-018-0076-y.
*Neutral amino acid transporter ASCT2, inward-open C467R mutant with bound TBOA: Homo sapiens* E Eukaryota (expressed in P. pastoris), 3.6 Å** cryo-EM structure substrate-free structure, 4.1 Å: 6RVY	6RVX	Data File Jmol Viewer 6RVX 6RVY	Garaeva et al. (2019). Garaeva AA, Guskov A, Slotboom DJ, & Paulino C (2019). A one-gate elevator mechanism for the human neutral amino acid transporter ASCT2. Nat Commun 10 1. PubMed Id: 31366933. doi:10.1038/s41467-019-11363-x.
*Neutral amino acid transporter ASCT2, outward-oriented state (no ligand): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.54 Å** cryo-EM structure with ligand, 3.84 Å: 6MPB	6MP6	Data File Jmol Viewer 6MP6 6MPB	Yu et al. (2019). Yu X, Plotnikova O, Bonin PD, Subashi TA, McLellan TJ, Dumlao D, Che Y, Dong YY, Carpenter EP, West GM, Qiu X, Culp JS, & Han S (2019). Cryo-EM structures of the human glutamine transporter SLC1A5 (ASCT2) in the outward-facing conformation. Elife 8 . PubMed Id: 31580259. doi:10.7554/eLife.48120.
*Neutral amino acid transporter ASCT2, in the presence Lc-BPE (position "up") in the outward-open conformation: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 3.43 Å** cryo-EM structure the presence of Lc-BPE (position "down") in the outward-open conformation, 3.43 Å 7BCS in the presence of the ERA-21 in the outward-open conformation, 3.37 Å 7BCT	7BCQ	Data File Jmol Viewer 7BCQ 7BCS 7BCT	Garibsingh et al. (2021). Garibsingh RA, Ndaru E, Garaeva AA, Shi Y, Zielewicz L, Zakrepine P, Bonomi M, Slotboom DJ, Paulino C, Grewer C, & Schlessinger A (2021). Rational design of ASCT2 inhibitors using an integrated experimental-computational approach. Proc Natl Acad Sci U S A 118 37:e2104093118. PubMed Id: 34507995. doi:10.1073/pnas.2104093118.
*Concentrative nucleoside transporter (CNT) in complex with uridine: Vibrio cholerae* B Bacteria (expressed in E. coli), 2.44 Å** Member of Solute Carrier Transporter Superfamily (SLC28)	3TIJ	Data File Jmol Viewer 3TIJ	Johnson et al. (2012). Johnson ZL, Cheong CG, & Lee SY (2012). Crystal structure of a concentrative nucleoside transporter from Vibrio cholerae at 2.4 Å Nature 483 :489-493. PubMed Id: 22407322. doi:10.1038/nature10882.
*Dicarboxylate/Sodium Symporter, inward facing state: Vibrio cholerae* B Bacteria (expressed in E. coli), 3.20 Å** Member of Solute Carrier Transporter Superfamily (SLC13)	4F35	Data File Jmol Viewer 4F35	Mancusso et al. (2012). Mancusso R, Gregorio GG, Liu Q, & Wang DN (2012). Structure and mechanism of a bacterial sodium-dependent dicarboxylate transporter. Nature 491 :622-626. PubMed Id: 23086149. doi:10.1038/nature11542.
*Dicarboxylate/Sodium Symporter with bound succinate: Vibrio cholerae* B Bacteria (expressed in E. coli), 2.78 Å** with bound citrate, 2.78 Å: 5UL9 humanized version with bound citrate, 2.78 Å: 5ULD humanized version with bound succinate, 2.78 Å: 5ULE Member of Solute Carrier Transporter Superfamily (SLC13)	5UL7	Data File Jmol Viewer 5UL7 5ULD 5UL9 5ULE	Nie et al. (2017). Nie R, Stark S, Symersky J, Kaplan RS, & Lu M (2017). Structure and function of the divalent anion/Na⁺ symporter from Vibrio cholerae and a humanized variant. Nat Commun 8 :15009. PubMed Id: 28436435. doi:10.1038/ncomms15009.
*Dicarboxylate/Sodium Symporter with bound Na⁺ in amphipol: Vibrio cholerae* B Bacteria (expressed in E. coli), 3.16 Å** cryo-EM structure with Fab84 in nanodisc, 3.15 Å: 6WW5 x-ray: in complex with terephthalate, 3.92 Å: 6WTX Member of Solute Carrier Transporter Superfamily (SLC13)	6WU3	Data File Jmol Viewer 6WU3 6WW5 6WTX	Sauer et al. (2020). Sauer DB, Trebesch N, Marden JJ, Cocco N, Song J, Koide A, Koide S, Tajkhorshid E, & Wang DN (2020). Structural basis for the reaction cycle of DASS dicarboxylate transporters. Elife 9 . PubMed Id: 32869741. doi:10.7554/eLife.61350.
*Dicarboxylate antiporter, apo state: Lactobacillus acidophilus* B Bacteria (expressed in E.coli), 3.09 Å** cryo-EM structure alpha-ketoglutarate complex, 3.71 Å: 6WU4 in complex with malate, 3.36 Å: 6WU2 x-ray: in the presence of alpha-ketoglutarate and malate, 2.86 Å: 6WTW Member of Solute Carrier Transporter Superfamily (SLC13)	6WU1	Data File Jmol Viewer 6WU1 6WTW 6WU2 6WU4	Sauer et al. (2020). Sauer DB, Trebesch N, Marden JJ, Cocco N, Song J, Koide A, Koide S, Tajkhorshid E, & Wang DN (2020). Structural basis for the reaction cycle of DASS dicarboxylate transporters. Elife 9 . PubMed Id: 32869741. doi:10.7554/eLife.61350.
*DAT Dopamine transporter in complex with nortriptyline TCA (tricyclic antidepressant): Drosophila melanogaster* E Eukaryota (expressed in HEK293 cells), 2.95 Å** Member of Solute Carrier Transporter Superfamily (SLC6)	4M48	Data File Jmol Viewer 4M48	Penmatsa et al. (2013). Penmatsa A, Wang KH, & Gouaux E (2013). X-ray structure of dopamine transporter elucidates antidepressant mechanism. Nature 503 :85-90. PubMed Id: 24037379. doi:10.1038/nature12533.
*DAT Dopamine transporter in complex with dopamine: Drosophila melanogaster* E Eukaryota (expressed in HEK293 cells), 2.89 Å** in complex with: D-amphetamine, 2.80 Å: 4XP9 methamphetamine, 3.10 Å: 4XP6 3,4-dichlorophenethylamine, 2.95 Å: 4XPA cocaine, 2.80 Å: 4XP4 cocaine analogue-RTI55, 3.30 Å: 4XP5 D121G/S426M mutant with bound cocaine, 3.05 Å: 4XPB D121G/S426M mutant with bound RTI55, 3.27 Å: 4XPF D121G/S426M mutant with bound beta-CFT, 3.21 Å: 4XPG D121G/S426M mutant with bound 3,4-dichlorophenethylamine, 2.90 Å: 4XPH D121G/S426M mutant with EL2 deletion of 162-201 with bound 3,4-dichlorophen ethylamine, 3.36 Å: 4XPT	4XP1	Data File Jmol Viewer 4XP1 4XPG 4XPF 4XP6 4XPB 4XP4 4XPA 4XPT 4XPH 4XP9 4XP5	Wang et al. (2015). Wang KH, Penmatsa A, & Gouaux E (2015). Neurotransmitter and psychostimulant recognition by the dopamine transporter. Nature 521 :322-327. PubMed Id: 25970245. doi:10.1038/nature14431.
*DAT Dopamine transporter in complex with nisoxetine: Drosophila melanogaster* E Eukaryota (expressed in HEK-293S cells), 2.98 Å** in complex with reboxetine, 3.0 Å: 4XNX	4XNU	Data File Jmol Viewer 4XNU 4XNX	Penmatsa et al. (2015). Penmatsa A, Wang KH, & Gouaux E (2015). X-ray structures of Drosophila dopamine transporter in complex with nisoxetine and reboxetine. Nat Struct Mol Biol 22 :506-508. PubMed Id: 25961798. doi:10.1038/nsmb.3029.
DAT Dopamine transporter as surrogate norepinephrine transporter, with subsiteB mutations (D121G/S426M) in substrate-free form: Drosophila melanogaster E Eukaryota (expressed in HEK293 cells), 3.30 Å with NET-like mutations (D121G/S426M/F471L) in L-norepinephrine bound form, 2.88 Å: 6M0Z dopamine transporter in L-norepinephrine bound form, 2.80 Å: 6M2R with subsiteB mutations (D121G/S426M) in S-duloxetine bound form, 3.00 Å: 6M38 with NET-like mutations (D121G/S426M/F471L) in milnacipran bound form, 3.11 Å: 6M3Z with NET-like mutations (D121G/S426M/F471L) in tramadol bound form, 3.25 Å: 6M47	6M0F	Data File Jmol Viewer 6M0F 6M38 6M2R 6M0Z 6M3Z 6M47	Pidathala et al. (2021). Pidathala S, Mallela AK, Joseph D, & Penmatsa A (2021). Structural basis of norepinephrine recognition and transport inhibition in neurotransmitter transporters. Nat Commun 12 1:2199. PubMed Id: 33850134. doi:10.1038/s41467-021-22385-9.
*glycine transporter 1 (GlyT1), inward-open state in complex with a benzoylisoindoline inhibitor: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** GlyT1 is a member of SLC6 superfamily of transporters. in complex with a benzoylisoindoline inhibitor, 3.94 Å: 6ZPL	6ZBV	Data File Jmol Viewer 6ZBV 6ZPL	Shahsavar et al. (2021). Shahsavar A, Stohler P, Bourenkov G, Zimmermann I, Siegrist M, Guba W, Pinard E, Sinning S, Seeger MA, Schneider TR, Dawson RJP, & Nissen P (2021). Structural insights into the inhibition of glycine reuptake. Nature 591 7851:677-681. PubMed Id: 33658720. doi:10.1038/s41586-021-03274-z.
*B⁰AT1 (SLC6A19) in complex with angiotensin-converting enzyme 2 (ACE2), closed conformation: Homo sapiens* E Eukaryota (expressed in HEK293), 2.90 Å** cryo-EM structure open conformation, 4.50 Å: 6M1D SARS-CoV-2 receptor binding domain (RBD) in complex with with ACE2-B⁰AT1, 2.9 Å: 6M17	6M18	Data File Jmol Viewer 6M18 6M1D 6M17	Yan et al. (2020). Yan R, Zhang Y, Li Y, Xia L, Guo Y, & Zhou Q (2020). Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Science 367 6485:1444-1448. PubMed Id: 32132184. doi:10.1126/science.abb2762.
*Coronavirus spike receptor-binding domain complexed with ACE2: SARS-CoV-2* V Viruses (expressed in HEK293 cells), 2.50 Å**	6LZG	Data File Jmol Viewer 6LZG	Wang et al. (2020). Wang Q, Zhang Y, Wu L, Niu S, Song C, Zhang Z, Lu G, Qiao C, Hu Y, Yuen KY, Wang Q, Zhou H, Yan J, & Qi J (2020). Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2. Cell 181 4:894-904.e9. PubMed Id: 32275855. doi:10.1016/j.cell.2020.03.045.
*Coronavirus spike receptor-binding domain complexed with ACE2: SARS-CoV-2* V Viruses (expressed in Trichoplusia ni), 2.45 Å**	6M0J	Data File Jmol Viewer 6M0J	Lan et al. (2020). Lan J, Ge J, Yu J, Shan S, Zhou H, Fan S, Zhang Q, Shi X, Wang Q, Zhang L, & Wang X (2020). Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature 581 7807:215-220. PubMed Id: 32225176. doi:10.1038/s41586-020-2180-5.
*ACE2-bound SARS-CoV-2 trimer spike at pH 7.4: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.93 Å** cryo-EM structure double ACE2-bound SARS-CoV-2 trimer Spike at pH 7.4, 3.62 Å: 7KMZ triple ACE2-bound SARS-CoV-2 trimer spike at pH 7.4, 3.64 Å: 7KMS Focused Refinement using Symmetry Expansion for Triple ACE2-bound SARS-CoV-2, 3.39 Å: 7KMB single ACE2-bound SARS-CoV-2 trimer spike at pH 5.5, 3.85 Å: 7KNE Double ACE2-Bound SARS-CoV-2 Trimer Spike at pH 5.5, 3.74 Å: 7KNH Triple ACE2-bound SARS-CoV-2 Trimer Spike at pH 5.5, 3.91 Å: 7KNI Consensus structure of SARS-CoV-2 spike at pH 5.5, 2.70 Å: 6XM0 SARS-CoV-2 spike at pH 5.5, single RBD up, conformation 1, 2.90 Å: 6XM3 SARS-CoV-2 spike at pH 5.5, single RBD up, conformation 2, 2.90 Å: 6XM4 SARS-CoV-2 spike at pH 5.5, all RBDs down, 3.10 Å: 6XM5 SARS-CoV-2 spike at pH 4.5, 2.50 Å: 7JWY SARS-CoV-2 spike at pH 4.0, 2.40 Å: 6XLU	7KNB	Data File Jmol Viewer 7KNB 6XM5 7KMS 7KNI 6XM4 7KMZ 7KMB 7KNH 6XM0 6XM3 6XLU 7JWY 7KNE	Zhou et al. (2020). Zhou T, Tsybovsky Y, Gorman J, Rapp M, Cerutti G, Chuang GY, Katsamba PS, Sampson JM, Schön A, Bimela J, Boyington JC, Nazzari A, Olia AS, Shi W, Sastry M, Stephens T, Stuckey J, Teng IT, Wang P, Wang S, Zhang B, Friesner RA, Ho DD, Mascola JR, Shapiro L, & Kwong PD (2020). Cryo-EM Structures of SARS-CoV-2 Spike without and with ACE2 Reveal a pH-Dependent Switch to Mediate Endosomal Positioning of Receptor-Binding Domains. Cell Host Microbe 28 6:867-879.e5. PubMed Id: 33271067. doi:10.1016/j.chom.2020.11.004.
*SARS-CoV-2 chimeric receptor-binding domain complexed with ACE2: SARS-CoV-2* V Viruses (expressed in Spodoptera frugiperda), 2.68 Å**	6VW1	Data File Jmol Viewer 6VW1	Shang et al. (2020). Shang J, Ye G, Shi K, Wan Y, Luo C, Aihara H, Geng Q, Auerbach A, & Li F (2020). Structural basis of receptor recognition by SARS-CoV-2. Nature 581 7807:221-224. PubMed Id: 32225175. doi:10.1038/s41586-020-2179-y.
*SARS-CoV-2 S 6P trimer in complex with the ACE2 protein decoy: SARS-CoV-2* V Viruses (expressed in HEK293 cells), 4.10 Å** cryo-EM structure	7KL9	Data File Jmol Viewer 7KL9	Linsky et al. (2020). Linsky TW, Vergara R, Codina N, Nelson JW, Walker MJ, Su W, Barnes CO, Hsiang TY, Esser-Nobis K, Yu K, Reneer ZB, Hou YJ, Priya T, Mitsumoto M, Pong A, Lau UY, Mason ML, Chen J, Chen A, Berrocal T, Peng H, Clairmont NS, Castellanos J, Lin YR, Josephson-Day A, Baric RS, Fuller DH, Walkey CD, Ross TM, Swanson R, Bjorkman PJ, Gale M Jr, Blancas-Mejia LM, Yen HL, & Silva DA (2020). De novo design of potent and resilient hACE2 decoys to neutralize SARS-CoV-2. Science 370 6521:1208-1214. PubMed Id: 33154107. doi:10.1126/science.abe0075.
B⁰AT1 (SLC6A19) in complex with angiotensin-converting enzyme 2 (ACE2) in complex with SARS-CoV-2 spike protein: Homo sapiens, SARS coronavirus 2 E Eukaryota (expressed in HEK293 cells), 8.30 Å cryo-EM structure S protein in active conformation, 3.30 Å: 7DWZ S protein bound with PD of ACE2 in the conformation 2, 3.30 Å: 7DX5 S protein bound with PD of ACE2 in the conformation 3, 3.00 Å: 7DX6 S protein bound with PD of ACE2 in the conformation 1, 3.50 Å: 7DX3 S(p) protein with PD of ACE2 in the conformation 3, 3.60 Å: 7DX9 S protein of SARS-CoV-2 in the locked conformation, 2.70 Å: 7DWY S(p) protein with PD of ACE2 in conformation 1, 3.40 Å: 7DX7 S(p) protein with PD of ACE2 in conformation 2, 2.90 Å: 7DX8 S(D614G) protein of SARS-CoV-2, 3.10 Å: 3.10 Å: 7DX1	7DWX	Data File Jmol Viewer 7DWX 7DX7 7DX1 7DWZ 7DX8 7DWY 7DX6 7DX3 7DX9 7DX5	Yan et al. (2021). Yan R, Zhang Y, Li Y, Ye F, Guo Y, Xia L, Zhong X, Chi X, & Zhou Q (2021). Structural basis for the different states of the spike protein of SARS-CoV-2 in complex with ACE2. Cell Res . PubMed Id: 33737693. doi:10.1038/s41422-021-00490-0.
*B⁰AT1 (SLC6A19) in complex with angiotensin-converting enzyme 2 (ACE2) with bound monoclonal antibody 3E8: Homo sapiens, SARS coronavirus 2* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure	7V61	Data File Jmol Viewer 7V61	Chen et al. (2021). Chen Y, Zhang YN, Yan R, Wang G, Zhang Y, Zhang ZR, Li Y, Ou J, Chu W, Liang Z, Wang Y, Chen YL, Chen G, Wang Q, Zhou Q, Zhang B, & Wang C (2021). ACE2-targeting monoclonal antibody as potent and broad-spectrum coronavirus blocker. Signal Transduct Target Ther 6 1:315. PubMed Id: 34433803. doi:10.1038/s41392-021-00740-y.
*B⁰AT1 (SLC6A19) in complex with angiotensin-converting enzyme 2 (ACE2), with bound glutamine: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure with bound methionine, 3.10 Å: 8I93	8I92	Data File Jmol Viewer 8I92 8I93	Li et al. (2023). Li Y, Chen Y, Zhang Y, Shen Y, Xu K, Liu Y, Wang Z, & Yan R (2023). Structural insight into the substrate recognition and transport mechanism of amino acid transporter complex ACE2-B0AT1 and ACE2-SIT1. Cell Discov 9 1:93. PubMed Id: 37684251. doi:10.1038/s41421-023-00596-2.
*SLC4A4 Na⁺-coupled acid-base transporter NBCe1: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.9 Å** cryo-EM structure	6CAA	Data File Jmol Viewer 6CAA	Huynh et al. (2018). Huynh KW, Jiang J, Abuladze N, Tsirulnikov K, Kao L, Shao X, Newman D, Azimov R, Pushkin A, Zhou ZH, & Kurtz I (2018). CryoEM structure of the human SLC4A4 sodium-coupled acid-base transporter NBCe1. Nat Commun 9 1. PubMed Id: 29500354. doi:10.1038/s41467-018-03271-3.
*SLC4A4 Na⁺-coupled acid-base transporter Bor1p: Saccharomyces mikatae* E Eukaryota (expressed in Saccharomyces cerevisiae), 5.90 Å** cryo-EM structure	5SV9	Data File Jmol Viewer 5SV9	Coudray et al. (2017). Coudray N, L Seyler S, Lasala R, Zhang Z, Clark KM, Dumont ME, Rohou A, Beckstein O, & Stokes DL (2017). Structure of the SLC4 transporter Bor1p in an inward-facing conformation. Protein Sci 26 1:130-145. PubMed Id: 27717063. doi:10.1002/pro.3061.
*SLC4A11 NH₃-stimulated acid-base transporter BTR1, inward-facing state, pH 5.5: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.94 Å** cryo-EM structure R125H mutant, 2.96 Å: 7X1H outward-facing state, 2.94 Å: 7X1I outward-facing state, in presence of NH₄Cl, 2.84 Å: 7X1J	7X1G	Data File Jmol Viewer 7X1G 7X1I 7X1J 7X1H	Lu et al. (2023). Lu Y, Zuo P, Chen H, Shan H, Wang W, Dai Z, Xu H, Chen Y, Liang L, Ding D, Jin Y, & Yin Y (2023). Structural insights into the conformational changes of BTR1/SLC4A11 in complex with PIP2. Nat Commun 14 1:6157. PubMed Id: 37788993. doi:10.1038/s41467-023-41924-0.
*sodium/iodide symporter (NIS, SLC5A5): Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure in complex with iodide and sodium, 3.10 Å: 7UV0 in complex with perrhenate and sodium, 3.20 Å: 7UUZ	7UUV	Data File Jmol Viewer 7UUV 7UV0 7UUZ	Ravera et al. (2022). Ravera S, Nicola JP, Salazar-De Simone G, Sigworth FJ, Karakas E, Amzel LM, Bianchet MA, & Carrasco N (2022). Structural insights into the mechanism of the sodium/iodide symporter. Nature 612 7941:795-801. PubMed Id: 36517601. doi:10.1038/s41586-022-05530-2.
*GABA reuptake transporter 1 in complex with tiagabine, inward-open conformation: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.82 Å** cryo-EM structure GABA transporter (GAT1) is a member of the Solute Carrier 6 (SLC6) transporter family.	7SK2	Data File Jmol Viewer 7SK2	Motiwala et al. (2022). Motiwala Z, Aduri NG, Shaye H, Han GW, Lam JH, Katritch V, Cherezov V, & Gati C (2022). Structural basis of GABA reuptake inhibition. Nature 606 7915:820-826. PubMed Id: 35676483. doi:10.1038/s41586-022-04814-x.
*Dopamine transporter with GABA transporter1-like substitutions in the binding site, in substrate-free form.: Drosophila melanogaster* E Eukaryota (expressed in HEK293 cells), 3.20 Å** in complex with NO711, 2.75 Å: 7WGT in complex with SKF89976a, 2.90 Å: 7WLW	7WGD	Data File Jmol Viewer 7WGD 7WGT 7WLW	Joseph et al. (2022). Joseph D, Nayak SR, & Penmatsa A (2022). Structural insights into GABA transport inhibition using an engineered neurotransmitter transporter. EMBO J 41 15:e110735. PubMed Id: 35796008. doi:10.15252/embj.2022110735.
*SLC7 CAT family amino acid transporter, wild-type complexed with L-Ala: Geobacillus kaustophilus* B Bacteria, 2.86 Å** M321S mutant in complex with L-Arg, 3.13 Å: 6F34	5OQT	Data File Jmol Viewer 5OQT 6F34	Jungnickel et al. (2018). Jungnickel KEJ, Parker JL, & Newstead S (2018). Structural basis for amino acid transport by the CAT family of SLC7 transporters. Nat Commun 9 :550. PubMed Id: 29416041. doi:10.1038/s41467-018-03066-6.
*SLC7/SLC3 heteromeric amino acid transporter (HAT) family, b^[0,+1]AT1-rBAT neutral & basic transport system: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure Homodimeric structure of the rBAT complex, 2.80 Å: 6YUZ Structure of b^[0,+]AT1, 3.40 Å: 6YV1	6YUP	Data File Jmol Viewer 6YUP 6YUZ 6YV1	Wu et al. (2020). Wu D, Grund TN, Welsch S, Mills DJ, Michel M, Safarian S, & Michel H (2020). Structural basis for amino acid exchange by a human heteromeric amino acid transporter. Proc Natl Acad Sci U S A 117 35:21281-21287. PubMed Id: 32817565. doi:10.1073/pnas.2008111117.
*SLC7A5 L-type amino acid transporter LAT1 in complex with 4F2hc (SLC3A2): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.5 Å** cryo-EM structure incubated with JPH203, 3.3 Å: 6IRS	6IRT	Data File Jmol Viewer 6IRT 6IRS	Yan et al. (2019). Yan R, Zhao X, Lei J, & Zhou Q (2019). Structure of the human LAT1-4F2hc heteromeric amino acid transporter complex. Nature 568 7750:127-130. PubMed Id: 30867591. doi:10.1038/s41586-019-1011-z.
*SLC7A5-SLC3A2 L-type amino acid transporter LAT1-4F2hc complex with JX-075: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure with bound JX-078, 2.90 Å: 7DSL with bound JX-119, 3.10 Å: 7DSN with bound 3,5-diiodo-L-tyrosine, 3.40 Å: 7DSQ	7DSK	Data File Jmol Viewer 7DSK 7DSQ 7DSN 7DSL	Yan et al. (2021). Yan R, Li Y, Müller J, Zhang Y, Singer S, Xia L, Zhong X, Gertsch J, Altmann KH, & Zhou Q (2021). Mechanism of substrate transport and inhibition of the human LAT1-4F2hc amino acid transporter. Cell Discov 7 1:16. PubMed Id: 33758168. doi:10.1038/s41421-021-00247-4.
*SLC7A5 L-type amino acid transporter LAT1-CD98hc in complex with MEM-108 Fab: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.31 Å** cryo-EM structure CD98hc extracellular domain bound to HBJ127 Fab and MEM-108 Fab, 4.1 Å 6JMR	6JMQ	Data File Jmol Viewer 6JMQ 6JMR	Lee et al. (2019). Lee Y, Wiriyasermkul P, Jin C, Quan L, Ohgaki R, Okuda S, Kusakizako T, Nishizawa T, Oda K, Ishitani R, Yokoyama T, Nakane T, Shirouzu M, Endou H, Nagamori S, Kanai Y, & Nureki O (2019). Cryo-EM structure of the human L-type amino acid transporter 1 in complex with glycoprotein CD98hc. Nat Struct Mol Biol 26 6:510-517. PubMed Id: 31160781. doi:10.1038/s41594-019-0237-7.
*4F2hc-LAT2 heterodimeric amino acid transporter, in complex with anticalin D11vs: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 3.18 Å** cryo-EM structure	8A6L	Data File Jmol Viewer 8A6L	Jeckelmann et al. (2022). Jeckelmann JM, Lemmin T, Schlapschy M, Skerra A, & Fotiadis D (2022). Structure of the human heterodimeric transporter 4F2hc-LAT2 in complex with Anticalin, an alternative binding protein for applications in single-particle cryo-EM. Sci Rep 12 1:18269. PubMed Id: 36310334. doi:10.1038/s41598-022-23270-1.
*SLC7A8 L-type amino acid transporter LAT2-CD98hc complex, apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.98 Å** cryo-EM structure	7B00	Data File Jmol Viewer 7B00	Rodriguez et al. (2021). Rodriguez CF, Escudero-Bravo P, Díaz L, Bartoccioni P, García-Martín C, Gilabert JG, Boskovic J, Guallar V, Errasti-Murugarren E, Llorca O, & Palacín M (2021). Structural basis for substrate specificity of heteromeric transporters of neutral amino acids. Proc Natl Acad Sci U S A 118 49:e2113573118. PubMed Id: 34848541. doi:10.1073/pnas.2113573118.
*SLC7A9 amino acid transporter b^0,+AT-rBAT complex with bound arginine: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.30 Å** cryo-EM structure ligand-free complex, 2.70 Å: 6LID	6LI9	Data File Jmol Viewer 6LI9 6LID	Yan et al. (2020). Yan R, Li Y, Shi Y, Zhou J, Lei J, Huang J, & Zhou Q (2020). Cryo-EM structure of the human heteromeric amino acid transporter b^0,+AT-rBAT. Sci Adv 6 16. PubMed Id: 32494597. doi:10.1126/sciadv.aay6379.
*SLC7A11 (xCT) antiporter with SLC3A2 subunit: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 6.20 Å** cryo-EM structure	7CCS	Data File Jmol Viewer 7CCS	Oda et al. (2020). Oda K, Lee Y, Wiriyasermkul P, Tanaka Y, Takemoto M, Yamashita K, Nagamori S, Nishizawa T, & Nureki O (2020). Consensus mutagenesis approach improves the thermal stability of system x_c^- transporter, xCT, and enables cryo-EM analyses. Protein Sci 29 12:2398-2407. PubMed Id: 33016372. doi:10.1002/pro.3966.
*SLC7A11 (xCT, xc⁻) cystine antiporter: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure in complex with glutamate, 3.70 Å 7P9U	7P9V	Data File Jmol Viewer 7P9V 7P9U	Parker et al. (2021). Parker JL, Deme JC, Kolokouris D, Kuteyi G, Biggin PC, Lea SM, & Newstead S (2021). Molecular basis for redox control by the human cystine/glutamate antiporter system xc. Nat Commun 12 1:7147. PubMed Id: 34880232. doi:10.1038/s41467-021-27414-1.
*SLC11 (NRAMP/MntH) transition-metal ion transporter in complex with nanobodies: Staphylococcus capitis* B Bacteria (expressed in E. coli), 3.10 Å** Note: supersedes 4WGV in complex with Mn²⁺, 3.40 Å: 5M95 Note: supersedes 4WGW	5M94	Data File Jmol Viewer 5M94 5M95	Ehrnstorfer et al. (2014). Ehrnstorfer IA, Geertsma ER, Pardon E, Steyaert J, & Dutzler R (2014). Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport. Nat Struct Mol Biol 21 11:990-996. PubMed Id: 25326704. doi:10.1038/nsmb.2904.
*SLC11 (NRAMP/MntH) transition-metal ion transporter (DMT1) manganese transporter: Eremococcus coleocola* B Bacteria (expressed in E. coli), 3.3 Å** E129Q mutant, 3.6 Å: 5M8K E129A mutant, 3.9 Å: 5M8A H236A mutant, 3.7 Å: 5M8J	5M87	Data File Jmol Viewer 5M87 5M8K 5M8A 5M8J	Ehrnstorfer et al. (2017). Ehrnstorfer IA, Manatschal C, Arnold FM, Laederach J, & Dutzler R (2017). Structural and mechanistic basis of proton-coupled metal ion transport in the SLC11/NRAMP family. Nat Commun 8 :14033. PubMed Id: 28059071. doi:10.1038/ncomms14033.
*SLC11 (NRAMP/MntH) transition-metal ion transporter (DMT1) in complex with an aromatic bis-isothiourea substituted compound: Eremococcus coleocola* B Bacteria (expressed in E. coli), 3.8 Å**	6TL2	Data File Jmol Viewer 6TL2	Manatschal et al. (2019). Manatschal C, Pujol-Giménez J, Poirier M, Reymond JL, Hediger MA, & Dutzler R (2019). Mechanistic basis of the inhibition of SLC11/NRAMP-mediated metal ion transport by bis-isothiourea substituted compounds. Elife 8 :e51913. PubMed Id: 31804182. doi:10.7554/eLife.51913.
*divalent metal ion transporter (DMT), monomer: Staphylococcus capitis* B Bacteria (expressed in E. coli), 3.78 Å** cryo-EM structure structure determined by NabFab-fiducial assisted cryo-EM homo-dimer, 8.45 Å: 7PHQ	7PIJ	Data File Jmol Viewer 7PIJ 7PHQ	Bloch et al. (2021). Bloch JS, Mukherjee S, Kowal J, Filippova EV, Niederer M, Pardon E, Steyaert J, Kossiakoff AA, & Locher KP (2021). Development of a universal nanobody-binding Fab module for fiducial-assisted cryo-EM studies of membrane proteins. Proc Natl Acad Sci U S A 118 47:e2115435118. PubMed Id: 34782475. doi:10.1073/pnas.2115435118.
*SLC11 (NRAMP/MntH) transition-metal ion transporter in inward facing apo form: Deinococcus radiodurans* B Bacteria (expressed in E. coli), 3.94 Å**	5KTE	Data File Jmol Viewer 5KTE	Bozzi et al. (2016). Bozzi AT, Bane LB, Weihofen WA, Singharoy A, Guillen ER, Ploegh HL, Schulten K, & Gaudet R (2016). Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter. Structure 24 :2102-2114. PubMed Id: 27839948. doi:10.1016/j.str.2016.09.017.
*SLC11 (NRAMP/MntH) transition-metal ion transporter, apo form: Eggerthella lenta* B Bacteria (expressed in E. coli), 3.50 Å** cryo-EM structure magnesium-bound, 4.10 Å 7QIC apo-form, 4.10 Å 7QJI Mn²⁺ soak, 4.60 Å 7QJJ	7QIA	Data File Jmol Viewer 7QIA 7QJI 7QIC 7QJJ	Ramanadane et al. (2022). Ramanadane K, Straub MS, Dutzler R, & Manatschal C (2022). Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family. Elife 11 :e74589. PubMed Id: 35001872. doi:10.7554/eLife.74589.
*NKCC1 cation-chloride cotransporter (SLC12A2 family): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.52 Å** cryo-EM structure	7D10	Data File Jmol Viewer 7D10	Zhang et al. (2021). Zhang S, Zhou J, Zhang Y, Liu T, Friedel P, Zhuo W, Somasekharan S, Roy K, Zhang L, Liu Y, Meng X, Deng H, Zeng W, Li G, Forbush B, & Yang M (2021). The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2. Commun Biol 4 1:226. PubMed Id: 33597714. doi:10.1038/s42003-021-01750-w.
*NKCC1 cation-chloride cotransporter (SLC12A2 family), TM domain: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.55 Å** cryo-EM structure	7ZGO	Data File Jmol Viewer 7ZGO	Neumann et al. (2022). Neumann C, Rosenbaek LL, Flygaard RK, Habeck M, Karlsen JL, Wang Y, Lindorff-Larsen K, Gad HH, Hartmann R, Lyons JA, Fenton RA, & Nissen P (2022). Cryo-EM structure of the human NKCC1 transporter reveals mechanisms of ion coupling and specificity. EMBO J 41 23:e110169. PubMed Id: 36239040. doi:10.15252/embj.2021110169.
*KCC2 cation-chloride cotransporter (SLC12A5 superfamily): Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.80 Å** cryo-EM structure	7D14	Data File Jmol Viewer 7D14	Zhang et al. (2021). Zhang S, Zhou J, Zhang Y, Liu T, Friedel P, Zhuo W, Somasekharan S, Roy K, Zhang L, Liu Y, Meng X, Deng H, Zeng W, Li G, Forbush B, & Yang M (2021). The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2. Commun Biol 4 1:226. PubMed Id: 33597714. doi:10.1038/s42003-021-01750-w.
*KCC2 cation-chloride cotransporter (SLC12A5 superfamily): Homo sapiens* E Eukaryota, 3.40 Å** cryo-EM structure	7D8Z	Data File Jmol Viewer 7D8Z	Xie et al. (2020). Xie Y, Chang S, Zhao C, Wang F, Liu S, Wang J, Delpire E, Ye S, & Guo J (2020). Structures and an activation mechanism of human potassium-chloride cotransporters. Sci Adv 6 50:eabc5883. PubMed Id: 33310850. doi:10.1126/sciadv.abc5883.
*KCC2 cation-chloride cotransporter (SLC12A5 superfamily): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure	6M23	Data File Jmol Viewer 6M23	Chi et al. (2021). Chi X, Li X, Chen Y, Zhang Y, Su Q, & Zhou Q (2021). Cryo-EM structures of the full-length human KCC2 and KCC3 cation-chloride cotransporters. Cell Res 31 4:482-484. PubMed Id: 33199848. doi:10.1038/s41422-020-00437-x.
*KCC3 cation-chloride cotransporter (SLC12A5 superfamily): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure with bound DIOA, 2.70 Å: 6M22	6M1Y	Data File Jmol Viewer 6M1Y 6M22	Chi et al. (2021). Chi X, Li X, Chen Y, Zhang Y, Su Q, & Zhou Q (2021). Cryo-EM structures of the full-length human KCC2 and KCC3 cation-chloride cotransporters. Cell Res 31 4:482-484. PubMed Id: 33199848. doi:10.1038/s41422-020-00437-x.
*NaCT citrate transporter (SLC13A5 superfamily) in complex with citrate: Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.04 Å** cryo-EM structure NaCT-PF2 complex, 3.12 Å: 7JSJ	7JSK	Data File Jmol Viewer 7JSK 7JSJ	Sauer et al. (2021). Sauer DB, Song J, Wang B, Hilton JK, Karpowich NK, Mindell JA, Rice WJ, & Wang DN (2021). Structure and inhibition mechanism of the human citrate transporter NaCT. Nature 591 7848:157-161. PubMed Id: 33597751. doi:10.1038/s41586-021-03230-x.
*SLC15A1 proton-coupled peptide transporter (PepT1) in complex with prodrug valacyclovir: Staphylococcus hominis* B Bacteria (expressed in E. coli), 3.1 Å** in complex with 5-aminolevulinic acid, 2.8 Å: 6H7U in complex with 5-aminolevulinic acid, 2.5 Å: 6HZP	6GZ9	Data File Jmol Viewer 6GZ9 6H7U 6HZP	Minhas & Newstead (2019). Minhas GS, & Newstead S (2019). Structural basis for prodrug recognition by the SLC15 family of proton-coupled peptide transporters. Proc. Natl. Acad. Sci. U.S.A. 116 3:804-809. PubMed Id: 30602453. doi:10.1073/pnas.1813715116.
*DtpA SLC15A1 proton-coupled peptide transporter (PepT1) in complex with valganciclovir: Escherichia coli* B Bacteria, 2.65 Å** alone in MES buffer, 3.29 Å: 6GS1 alone in glycine buffer, 3.30 Å: 6GS7	6GS4	Data File Jmol Viewer 6GS4 6GS1 6GS7	Ural-Blimke et al. (2019). Ural-Blimke Y, Flayhan A, Strauss J, Rantos V, Bartels K, Nielsen R, Pardon E, Steyaert J, Kosinski J, Quistgaard EM, & Löw C (2019). Structure of Prototypic Peptide Transporter DtpA from E. coli in Complex with Valganciclovir Provides Insights into Drug Binding of Human PepT1. J Am Chem Soc 141 6:2404-2412. PubMed Id: 30644743. doi:10.1021/jacs.8b11343.
*SLC15A1 proton-coupled peptide transporter (PepT1) bound to Ala-Phe in the outward facing occluded conformation: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.10 Å** cryo-EM structure bound to Ala-Phe in the outward facing open conformation, 3.50 Å 7PMX apo form, outward facing conformation, 3.90 Å 7PN1	7PMW	Data File Jmol Viewer 7PMW 7PMX 7PN1	Killer et al. (2021). Killer M, Wald J, Pieprzyk J, Marlovits TC, & Löw C (2021). Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes. Sci Adv 7 45:eabk3259. PubMed Id: 34730990. doi:10.1126/sciadv.abk3259.
*SLC15A2 proton-coupled peptide transporter (PepT2): Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure	7NQK	Data File Jmol Viewer 7NQK	Parker et al. (2021). Parker JL, Deme JC, Wu Z, Kuteyi G, Huo J, Owens RJ, Biggin PC, Lea SM, & Newstead S (2021). Cryo-EM structure of PepT2 reveals structural basis for proton-coupled peptide and prodrug transport in mammals. Sci Adv 7 35:eabh3355. PubMed Id: 34433568. doi:10.1126/sciadv.abh3355.
*SLC15A2 proton-coupled peptide transporter (PepT2) bound to AlaPhe, inward facing partially occluded conformation: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.80 Å** cryo-EM structure	7PMY	Data File Jmol Viewer 7PMY	Killer et al. (2021). Killer M, Wald J, Pieprzyk J, Marlovits TC, & Löw C (2021). Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes. Sci Adv 7 45:eabk3259. PubMed Id: 34730990. doi:10.1126/sciadv.abk3259.
*Monocarboxylate transporter 1 (MCT1, SLC16 family)-Basigin-2 complex in outward open state in presence of AZD3965: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** cryo-EM structure in the presence of BAY-8002, 3.00 Å 7CKR the presence of 7ACC2 in the inward-open conformation, 2.95 Å 7CKO D309N mutant in complex with Basigin-2 in the inward-open conformation, 3.30 Å 7DA5	6LYY	Data File Jmol Viewer 6LYY 7CKR 7DA5 7CKO	Wang et al. (2021). Wang N, Jiang X, Zhang S, Zhu A, Yuan Y, Xu H, Lei J, & Yan C (2021). Structural basis of human monocarboxylate transporter 1 inhibition by anti-cancer drug candidates. Cell 184 2:370-383.e13. PubMed Id: 33333023. doi:10.1016/j.cell.2020.11.043.
*Monocarboxylate transporter 1 (MCT1; SLC16 family) in complex with Basigin-2, in the presence of lactate: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.30 Å** cryo-EM structure in the presence of anti-cancer drug candidate AZD3965 in the outward-open conformation, 3.20 Å 6LYY in the presence of anti-cancer drug candidate BAY-8002 in the outward-open conformation, 3.00 Å 7CKR in the presence of anti-cancer drug candidate 7ACC2 in the inward-open conformation, 2.95 Å 7CKO D309N mutant in complex with Basigin-2 in the inward-open conformation, 3.30 Å 7DA5	6LZ0	Data File Jmol Viewer 6LZ0 6LYY	Wang et al. (2021). Wang N, Jiang X, Zhang S, Zhu A, Yuan Y, Xu H, Lei J, & Yan C (2021). Structural basis of human monocarboxylate transporter 1 inhibition by anti-cancer drug candidates. Cell 184 2:370-383.e13. PubMed Id: 33333023. doi:10.1016/j.cell.2020.11.043.
*Monocarboxylate transporter 1 (MCT1; SLC16 family) in complex with embigin, inward-facing state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.63 Å** cryo-EM structure	7YR5	Data File Jmol Viewer 7YR5	Xu et al. (2022). Xu B, Zhang M, Zhang B, Chi W, Ma X, Zhang W, Dong M, Sheng L, Zhang Y, Jiao W, Shan Y, Chang W, Wang P, Wen S, Pei D, Chen L, Zhang X, Yan H, & Ye S (2022). Embigin facilitates monocarboxylate transporter 1 localization to the plasma membrane and transition to a decoupling state. Cell Rep 40 11:111343. PubMed Id: 36103816. doi:10.1016/j.celrep.2022.111343.
*Monocarboxylate transporter 2 (MCT2, SLC16 family): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.80 Å** cryo-EM structure	7BP3	Data File Jmol Viewer 7BP3	Zhang et al. (2020). Zhang B, Jin Q, Xu L, Li N, Meng Y, Chang S, Zheng X, Wang J, Chen Y, Neculai D, Gao N, Zhang X, Yang F, Guo J, & Ye S (2020). Cooperative transport mechanism of human monocarboxylate transporter 2. Nat Commun 11 1:2429. PubMed Id: 32415067. doi:10.1038/s41467-020-16334-1.
*DgoT D-galactonate:proton symporter (SLC17), inward open form: Escherichia coli* B Bacteria, 2.92 Å** E133Q mutant in the outward substrate-bound form, 3.50 Å: 6E9O	6E9N	Data File Jmol Viewer 6E9N 6E9O	Leano et al. (2019). Leano JB, Batarni S, Eriksen J, Juge N, Pak JE, Kimura-Someya T, Robles-Colmenares Y, Moriyama Y, Stroud RM, & Edwards RH (2019). Structures suggest a mechanism for energy coupling by a family of organic anion transporters. PLoS Biol 17 5. PubMed Id: 31083648. doi:10.1371/journal.pbio.3000260.
*vesicular glutamate transporter VGLUT2 (SLC17), luminal (outward) open state: Rattus norvegicus* E Eukaryota (expressed in Spodoptera frugiperda), 3.80 Å** Cryo-EM structure Note: supersedes 6V4D	8SBE	Data File Jmol Viewer 8SBE	Li et al. (2020). Li F, Eriksen J, Finer-Moore J, Chang R, Nguyen P, Bowen A, Myasnikov A, Yu Z, Bulkley D, Cheng Y, Edwards RH, & Stroud RM (2020). Ion transport and regulation in a synaptic vesicle glutamate transporter. Science 368 6493:893-897. PubMed Id: 32439795. doi:10.1126/science.aba9202.
*Reduced folate carrier (RFC) SLC19A1: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.80 Å** cryo-EM structure in complex with methotrexate, 3.30 Å: 7TX6	7TX7	Data File Jmol Viewer 7TX7 7TX6	Wright et al. (2022). Wright NJ, Fedor JG, Zhang H, Jeong P, Suo Y, Yoo J, Hong J, Im W, & Lee SY (2022). Methotrexate recognition by the human reduced folate carrier SLC19A1. Nature 609 7929:1056-1062. PubMed Id: 36071163. doi:10.1038/s41586-022-05168-0.
*Reduced folate carrier (RFC) SLC19A1, apo: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.40 Å** cryo-EM structure with bound 3'3'-CDA, 3.00 Å: 7XQ0 with bound 2'3'-CDAS, 3.40 Å: 7XQ1 with bound 2'3'-cGAMP, 3.30 Å: 7XQ2 with bound 5-MTHF, 3.00 Å: 8GOE with bound PMX, 3.00 Å: 8GOF	7XPZ	Data File Jmol Viewer 7XPZ 7XQ2 7XQ0 7XQ1 8GOF 8GOE	Zhang et al. (2022). Zhang Q, Zhang X, Zhu Y, Sun P, Zhang L, Ma J, Zhang Y, Zeng L, Nie X, Gao Y, Li Z, Liu S, Lou J, Gao A, Zhang L, & Gao P (2022). Recognition of cyclic dinucleotides and folates by human SLC19A1. Nature 612 7938:170-176. PubMed Id: 36265513. doi:10.1038/s41586-022-05452-z.
*SLC20 sodium-dependent phosphate transporter, inward occluded state: Thermotoga maritima* B Bacteria (expressed in Saccharomyces cerevisiae), 2.30 Å**	6L85	Data File Jmol Viewer 6L85	Tsai et al. (2020). Tsai JY, Chu CH, Lin MG, Chou YH, Hong RY, Yen CY, Hsiao CD, & Sun YJ (2020). Structure of the sodium-dependent phosphate transporter reveals insights into human solute carrier SLC20. Sci Adv 6 32. PubMed Id: 32821837. doi:10.1126/sciadv.abb4024.
*Organic cation transporter 3 (OCT3; SLC22A3) in lipid nanodisc: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure in complex with inhibitor decynium-22, 3.55 Å: 7ZHA in complex with inhibitor Corticosterone, 3.67 Å: 7ZH6	7ZH0	Data File Jmol Viewer 7ZH0 7ZHA 7ZH6	Khanppnavar et al. (2022). Khanppnavar B, Maier J, Herborg F, Gradisch R, Lazzarin E, Luethi D, Yang JW, Qi C, Holy M, Jäntsch K, Kudlacek O, Schicker K, Werge T, Gether U, Stockner T, Korkhov VM, & Sitte HH (2022). Structural basis of organic cation transporter-3 inhibition. Nat Commun 13 1:6714. PubMed Id: 36344565. doi:10.1038/s41467-022-34284-8.
*SLC26 proton-coupled fumarate symporter in complex with nanobodies: Deinococcus geothermalis* B Bacteria (expressed in E. coli), 3.20 Å**	5DA0	Data File Jmol Viewer 5DA0	Geertsma et al. (2015). Geertsma ER, Chang YN, Shaik FR, Neldner Y, Pardon E, Steyaert J, & Dutzler R (2015). Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family. Nat Struct Mol Biol 22 :803-808. PubMed Id: 26367249. doi:10.1038/nsmb.3091.
*Solute Carrier 26 family member A9 (SLC26A9) anion transporter, inward facing state: Mus musculus* E Eukaryota (expressed in HEK293s cells), 3.96 Å** cryo-EM structure in an intermediate state, 7.77 Å: 6RTF	6RTC	Data File Jmol Viewer 6RTC 6RTF	Walter et al. (2019). Walter JD, Sawicka M, & Dutzler R (2019). Cryo-EM structures and functional characterization of murine Slc26a9 reveal mechanism of uncoupled chloride transport. Elife 8 . PubMed Id: 31339488. doi:10.7554/eLife.46986. e46986
*Solute Carrier 26 family member A9 (SLC26A9) anion transporter: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.60 Å**	7CH1	Data File Jmol Viewer 7CH1	Chi et al. (2020). Chi X, Jin X, Chen Y, Lu X, Tu X, Li X, Zhang Y, Lei J, Huang J, Huang Z, Zhou Q, & Pan X (2020). Structural insights into the gating mechanism of human SLC26A9 mediated by its C-terminal sequence. Cell Discov 6 . PubMed Id: 32818062. doi:10.1038/s41421-020-00193-7.
*prestin electromotive signal amplifier (SLC26A5) in the presence of NaCl: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.30 Å** cryo-EM structure in nanodisc in the presence of NaCl, 2.70 Å 7LGW in the presence of sodium salicylate and sodium sulfate, 3.43 Å7LH2 in the presence of sodium sulfate, 4.30 Å 7LH3	7LGU	Data File Jmol Viewer 7LGU 7LH3 7LGW 7LH2	Ge et al. (2021). Ge J, Elferich J, Dehghani-Ghahnaviyeh S, Zhao Z, Meadows M, von Gersdorff H, Tajkhorshid E, & Gouaux E (2021). Molecular mechanism of prestin electromotive signal amplification. Cell 184 18:4669-4679.e13. PubMed Id: 34390643. doi:10.1016/j.cell.2021.07.034.
*prestin electromotive signal amplifier (SLC26A5, thermostabilized), in complex with chloride: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.52 Å** cryo-EM structure in complex with sulfate, 3.63 Å: 7V74 in complex with salicylate, 3.57 Å: 7V75	7V73	Data File Jmol Viewer 7V73 7V75 7V74	Futamata et al. (2022). Futamata H, Fukuda M, Umeda R, Yamashita K, Tomita A, Takahashi S, Shikakura T, Hayashi S, Kusakizako T, Nishizawa T, Homma K, & Nureki O (2022). Cryo-EM structures of thermostabilized prestin provide mechanistic insights underlying outer hair cell electromotility. Nat Commun 13 1:6208. PubMed Id: 36266333. doi:10.1038/s41467-022-34017-x.
*prestin electromotive signal amplifier (SLC26A5), sensor up (compact) state: Tursiops truncatus* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure Inhibited I (Chloride + Salicylate), 3.80 Å 7S9A sensor down I (Expanded) state, 4.20 Å 7S9B sensor down II (Expanded II) state, 6.70 Å 7S9C intermediate state, 4.60 Å 7S9D inhibited II (Sulfate +Salicylate), 3.70 Å 7S9E	7S8X	Data File Jmol Viewer 7S8X 7S9D 7S9A 7S9B 7S9E 7S9C	Bavi et al. (2021). Bavi N, Clark MD, Contreras GF, Shen R, Reddy BG, Milewski W, & Perozo E (2021). The conformational cycle of prestin underlies outer-hair cell electromotility. Nature 600 7889:553-558. PubMed Id: 34695838. doi:10.1038/s41586-021-04152-4.
*prestin electromotive signal amplifier (SLC26A5): Meriones unguiculatus* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure	7SUN	Data File Jmol Viewer 7SUN	Butan et al. (2022). Butan C, Song Q, Bai JP, Tan WJT, Navaratnam D, & Santos-Sacchi J (2022). Single particle cryo-EM structure of the outer hair cell motor protein prestin. Nat Commun 13 1:290. PubMed Id: 35022426. doi:10.1038/s41467-021-27915-z.
*concentrative nucleoside transporter CNT3 (SLC29 family): Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.60 Å** cryo-EM structure	6KSW	Data File Jmol Viewer 6KSW	Zhou et al. (2020). Zhou Y, Liao L, Wang C, Li J, Chi P, Xiao Q, Liu Q, Guo L, Sun L, & Deng D (2020). Cryo-EM structure of the human concentrative nucleoside transporter CNT3. PLoS Biol 18 8. PubMed Id: 32776918. doi:10.1371/journal.pbio.3000790.
*Equilibrative nucleoside transporter 1 (ENT1) SLC29 family, in complex with dilazep: Homo sapiens* E Eukaryota (expressed in HEK293s cells), 2.3 Å** merohedrally twinned in complex with NBMPR, 2.9 Å: 6OB6	6OB7	Data File Jmol Viewer 6OB7 6OB6	Wright & Lee (2019). Wright NJ, & Lee SY (2019). Structures of human ENT1 in complex with adenosine reuptake inhibitors. Nat Struct Mol Biol 26 7:599-606. PubMed Id: 31235912. doi:10.1038/s41594-019-0245-7.
*Equilibrative nucleoside transporter 1 (ENT1) SLC29 family, Y190A mutant, in complex with nanobody 19: Plasmodium falciparum* E Eukaryota (expressed in S. frugiperda), 3.64 Å** cryo-EM structure. Member of Solute Carrier Transporter Superfamily (SLC29). in complex with nanobody 48 and inosine, 3.11 Å: 7WN1 GFP fused into between TM10 and TM11, in complex with GSK4, 4.04 Å: 7YDQ	7WN0	Data File Jmol Viewer 7WN0 7WN1 7YDQ	Wang et al. (2023). Wang C, Yu L, Zhang J, Zhou Y, Sun B, Xiao Q, Zhang M, Liu H, Li J, Li J, Luo Y, Xu J, Lian Z, Lin J, Wang X, Zhang P, Guo L, Ren R, & Deng D (2023). Structural basis of the substrate recognition and inhibition mechanism of Plasmodium falciparum nucleoside transporter PfENT1. Nat Commun 14 1:1727. PubMed Id: 36977719. doi:10.1038/s41467-023-37411-1.
*ZnT8 Zn²⁺/H⁺ antiporter, SLC30 family in the presence of Zn²⁺ (one subunit inward facing): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.10 Å** cryo-EM structure D110N D224N mutant, outward-facing conformation, 3.80 Å: 6XPD wild-type, in the presence of zinc. Outward-facing conformation, 4.10 Å: 6XPE	6XPD	Data File Jmol Viewer 6XPD 6XPE 6XPD	Xue et al. (2020). Xue J, Xie T, Zeng W, Jiang Y, & Bai XC (2020). Cryo-EM structures of human ZnT8 in both outward- and inward-facing conformations. Elife 9 :e58823. PubMed Id: 32723473. doi:10.7554/eLife.58823.
*ZnT8 Zn²⁺/H⁺ antiporter, SLC30 family in the presence of Zn²⁺: Xenopus tropicalis* E Eukaryota (expressed in Komagataella pastoris), 3.85 Å** cryo-EM structure at a low pH, 3.72 Å: 7Y5H	7Y5G	Data File Jmol Viewer 7Y5G 7Y5H	Zhang et al. (2022). Zhang S, Fu C, Luo Y, Xie Q, Xu T, Sun Z, Su Z, & Zhou X (2022). Cryo-EM structure of a eukaryotic zinc transporter at a low pH suggests its Zn²⁺-releasing mechanism. J Struct Biol 215 1:107926. PubMed Id: 36464198. doi:10.1016/j.jsb.2022.107926.
*SLC35 superfamily Vrg4 nucleotide sugar transporter, apo form: Saccharomyces cerevisiae* E Eukaryota, 3.22 Å** with bound GDP-mannose, 3.6 Å: 5OGK	5OGE	Data File Jmol Viewer 5OGE 5OGK	Parker & Newstead (2017). Parker JL, & Newstead S (2017). Structural basis of nucleotide sugar transport across the Golgi membrane. Nature 551 7681:521-524. PubMed Id: 29143814. doi:10.1038/nature24464.
*SLC35 superfamily Vrg4 nucleotide sugar transporter, GMP-bound: Saccharomyces cerevisiae* E Eukaryota, 3.39 Å**	6QSK	Data File Jmol Viewer 6QSK	Parker et al. (2019). Parker JL, Corey RA, Stansfeld PJ, & Newstead S (2019). Structural basis for substrate specificity and regulation of nucleotide sugar transporters in the lipid bilayer. Nat Commun 10 1:4657. PubMed Id: 31604945. doi:10.1038/s41467-019-12673-w.
*SLC35 superfamily CMP-sialic acid (CMP-Sia) transporter in complex with CMP, lipidic cubic phase xtals: Mus musculus* E Eukaryota (expressed in Komagataella pastoris), 2.58 Å** in complex with CMP-sialic acid, 2.75 Å: 6OH3 in complex with CMP (hanging drop method), 3.38 Å: 6OH4	6OH2	Data File Jmol Viewer 6OH2 6OH4 6OH3	Ahuja & Whorton (2019). Ahuja S, & Whorton MR (2019). Structural basis for mammalian nucleotide sugar transport. Elife 8 :e45221. PubMed Id: 30985278. doi:10.7554/eLife.45221.
*Serotonin transporter (SERT) ts3 construct with bound paroxetine at central site: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.14 Å** Thermostabilized constructs: ts2: I291A, T439S. ts3:ts2+Y110A ts2 with bound paroxetine at central site, 4.53 Å: 5I6Z ts3 with bound s-citalopram at central site, 3.15 Å: 5I71 ts3 with s-citalopram at central and allosteric sites (soaked), 3.24 Å:5I73 ts3 with Br-citalopram at central site, 3.39 Å: 5I74 ts3 with s-citalopram at central site and Br-citalopram at allosteric site, 3.49 Å: 5I75	5I6X	Data File Jmol Viewer 5I6X 5I75 5I6Z 5I71 5I74 5I73	Coleman et al. (2016). Coleman JA, Green EM, & Gouaux E (2016). X-ray structures and mechanism of the human serotonin transporter. Nature 7599:334-339. PubMed Id: 27049939. doi:10.1038/nature17629.
*Serotonin transporter (SERT) ts2 construct with bound paroxetine at central site: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.62 Å** ts3 construct with fluvoxamine at the central site, 3.8 Å: 6AWP ts3 construct with sertraline at the central site, 3.53 Å: 6AWO ts3 construct with sertraline (anomalous chloride signal structure), 4.05 Å:6AWQ	6AWN	Data File Jmol Viewer 6AWN 6AWQ 6AWP 6AWO	Coleman & Gouaux (2018). Coleman JA, & Gouaux E (2018). Structural basis for recognition of diverse antidepressants by the human serotonin transporter. Nat Struct Mol Biol 25 :170-175. PubMed Id: 29379174. doi:10.1038/s41594-018-0026-8.
*Serotonin transporter (SERT) complexed with paroxetine & 8B6 Fab: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.30 Å** cryo-EM structure complexed with Br-paroxetine, 4.10 Å: 6VRK complexed with I-paroxetine, 3.80 Å: 6VRL Br-paroxetine complexed with transporter at the central site, 4.70 Å: 6W2B I-paroxetine complexed with the transporter at the central site, 6.30 Å: 6W2C	6VRH	Data File Jmol Viewer 6VRH 6VRL 6W2B 6VRK 6W2C	Coleman et al. (2020). Coleman JA, Navratna V, Antermite D, Yang D, Bull JA, & Gouaux E (2020). Chemical and structural investigation of the paroxetine-human serotonin transporter complex. Elife 9 . PubMed Id: 32618269. doi:10.7554/eLife.56427.
*Serotonin transporter (SERT) complexed with vilazodone and imipramine: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.65 Å** cryo-EM structure	7LWD	Data File Jmol Viewer 7LWD	Plenge et al. (2021). Plenge P, Yang D, Salomon K, Laursen L, Kalenderoglou IE, Newman AH, Gouaux E, Coleman JA, & Loland CJ (2021). The antidepressant drug vilazodone is an allosteric inhibitor of the serotonin transporter. Nat Commun 12 1:5063. PubMed Id: 34417466. doi:10.1038/s41467-021-25363-3.
*CitS Citrate symporter: Salmonella enterica* B Bacteria (expressed in E. coli), 2.5 Å** The CitS dimer reveals three different conformations of the active protomer	5A1S	Data File Jmol Viewer 5A1S	Wöhlert et al. (2015). Wöhlert D, Grötzinger MJ, Kühlbrandt W, & Yildiz Ö (2015). Mechanism of Na⁺-dependent citrate transport from the structure of an asymmetrical CitS dimer. Elife 4 :e09375. PubMed Id: 26636752. doi:10.7554/eLife.09375.
*SLC38A9 lysosomal amino acid transporter, cytosol-open state: Danio rerio* E Eukaryota (expressed in S. frugiperda), 3.17 Å**	6C08	Data File Jmol Viewer 6C08	Lei et al. (2018). Lei HT, Ma J, Sanchez Martinez S, & Gonen T (2018). Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state. Nat Struct Mol Biol 25 6:522-527. PubMed Id: 29872228. doi:10.1038/s41594-018-0072-2.
*SLC38A9 lysosomal amino acid transporter in the N-terminal plugged form: Danio rerio* E Eukaryota (expressed in Spodoptera frugiperda), 3.40 Å** cryo-EM structure	7KGV	Data File Jmol Viewer 7KGV	Lei et al. (2021). Lei HT, Mu X, Hattne J, & Gonen T (2021). A conformational change in the N terminus of SLC38A9 signals mTORC1 activation. Structure 29 5:426-432.e8. PubMed Id: 33296665. doi:10.1016/j.str.2020.11.014.
*Zrt/Irt-like protein (SLC39a), apo state: Bordetella bronchiseptica* B Bacteria (expressed in E. coli), 2.75 Å**	8CZJ	Data File Jmol Viewer 8CZJ	Zhang et al. (2023). Zhang Y, Jiang Y, Gao K, Sui D, Yu P, Su M, Wei GW, & Hu J (2023). Structural insights into the elevator-type transport mechanism of a bacterial ZIP metal transporter. Nat Commun 14 1:385. PubMed Id: 36693843. doi:10.1038/s41467-023-36048-4.
*Zrt/Irt-like protein (SLC39a), inward-facing, inhibited conformation: Bordetella bronchiseptica* B Bacteria (expressed in E. coli), 3.05 Å** cryo-EM structure	8GHT	Data File Jmol Viewer 8GHT	Pang et al. (2023). Pang C, Chai J, Zhu P, Shanklin J, & Liu Q (2023). Structural mechanism of intracellular autoregulation of zinc uptake in ZIP transporters. Nat Commun 14 1:3404. PubMed Id: 37296139. doi:10.1038/s41467-023-39010-6.
*Choline-like transporter SLC44: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.86 Å** cryo-EM structure	7WWB	Data File Jmol Viewer 7WWB	Xie et al. (2022). Xie T, Chi X, Huang B, Ye F, Zhou Q, & Huang J (2022). Rational exploration of fold atlas for human solute carrier proteins. Structure 30 9:1321-1330.e5. PubMed Id: 35700727. doi:10.1016/j.str.2022.05.015.
*proton coupled folate transporter (SLC46A1), outward open at pH 7.5: Gallus gallus* E Eukaryota (expressed in Saccharomyces cerevisiae), 3.20 Å** cryo-EM structure at pH 6.0 bound to pemetrexed, 3.30 Å: 7BC7	7BC6	Data File Jmol Viewer 7BC6 7BC7	Parker et al. (2021). Parker JL, Deme JC, Kuteyi G, Wu Z, Huo J, Goldman ID, Owens RJ, Biggin PC, Lea SM, & Newstead S (2021). Structural basis of antifolate recognition and transport by PCFT. Nature 595 7865:130-134. PubMed Id: 34040256. doi:10.1038/s41586-021-03579-z.
*sulfate transporter AtSULTR4;1 (SLC26): Arabidopsis thaliana* E Eukaryota (expressed in Trichoplusia ni), 2.75 Å** cryo-EM structure	7LHV	Data File Jmol Viewer 7LHV	Wang et al. (2021). Wang L, Chen K, & Zhou M (2021). Structure and function of an Arabidopsis thaliana sulfate transporter. Nat Commun 12 1:4455. PubMed Id: 34294705. doi:10.1038/s41467-021-24778-2.
*SIT1 (SLC6A20) in complex with angiotensin-converting enzyme 2 (ACE2), with bound proline: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	8I91	Data File Jmol Viewer 8I91	Li et al. (2023). Li Y, Chen Y, Zhang Y, Shen Y, Xu K, Liu Y, Wang Z, & Yan R (2023). Structural insight into the substrate recognition and transport mechanism of amino acid transporter complex ACE2-B0AT1 and ACE2-SIT1. Cell Discov 9 1:93. PubMed Id: 37684251. doi:10.1038/s41421-023-00596-2.
*OATP1B1 organic anion transporting polypeptide (SLC21A6): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure	8PHW	Data File Jmol Viewer 8PHW	Ciută et al. (2023). Ciută AD, Nosol K, Kowal J, Mukherjee S, Ramírez AS, Stieger B, Kossiakoff AA, & Locher KP (2023). Structure of human drug transporters OATP1B1 and OATP1B3. Nat Commun 14 1:5774. PubMed Id: 37723174. doi:10.1038/s41467-023-41552-8.
*OATP1B3 organic anion transporting polypeptide (SLC21A8): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.97 Å** cryo-EM structure	8PG0	Data File Jmol Viewer 8PG0	Ciută et al. (2023). Ciută AD, Nosol K, Kowal J, Mukherjee S, Ramírez AS, Stieger B, Kossiakoff AA, & Locher KP (2023). Structure of human drug transporters OATP1B1 and OATP1B3. Nat Commun 14 1:5774. PubMed Id: 37723174. doi:10.1038/s41467-023-41552-8.
Translocator Protein (18 kDA) TSPO Principally an outer mitochondrial membrane protein that binds to cholesterol and drug ligands, but occurs in diverse organisms Previously referred to as a peripheral-type benzodiazepine receptor (PBR). In mitochondria, it is part of large multimeric complex located in the outer mitochondrial membrane, and is closely associated with VDAC.
*Mitochondrial translocator protein (TSPO) in complex with PK11195: Mus musculus* E Eukaryota (expressed in E. coli), NMR Structure**	2MGY	Data File Jmol Viewer 2MGY	Jaremko et al. (2014). Jaremko L, Jaremko M, Giller K, Becker S, & Zweckstetter M (2014). Structure of the mitochondrial translocator protein in complex with a diagnostic ligand. Science 343 :1363-1366. PubMed Id: 24653034. doi:10.1126/science.1248725.
*Translocator protein (TSPO), apo type 2 monomer: Bacillus cereus* B Bacteria (expressed in E. coli), 1.70 Å** Type 1 monomer, 2.00 Å: 4RYN Iodo type 1 monomer, 2.80 Å: 4RYM Apo dimer, 4.10 Å: 4RYJ Dimer with bound PK11195, 3.5 Å: 4RYI	4RYQ	Data File Jmol Viewer 4RYQ 4RYN 4RYM 4RYI 4RYJ	Guo et al. (2015). Guo Y, Kalathur RC, Liu Q, Kloss B, Bruni R, Ginter C, Kloppmann E, Rost B, & Hendrickson WA (2015). Protein structure. Structure and activity of tryptophan-rich TSPO proteins. Science 347 6221:551-555. PubMed Id: 25635100. doi:10.1126/science.aaa1534.
*Translocator protein (TSPO), A139T SeMet1 C121: Rhodobacter sphaeroides* B Bacteria (expressed in E. coli), 1.80 Å** Wild-type, P2₁ space group, 2.50 Å: 4UC3 A139T SeMet2, P2₁2₁2₁, 2.40 Å: 4UC2	4UC1	Data File Jmol Viewer 4UC1 4UC3 4UC2	Li et al. (2015). Li F, Liu J, Zheng Y, Garavito RM, & Ferguson-Miller S (2015). Protein structure. Crystal structures of translocator protein (TSPO) and mutant mimic of a human polymorphism. Science 347 6221:555-558. PubMed Id: 25635101. doi:10.1126/science.1260590.
Ca²⁺:Cation Antiporter (CaCA) Family
*Sodium/Calcium Exchanger (NCX), Lipidic Cubic Phase Crystallization: Methanocaldococcus jannaschii* A Archaea (expressed in E. coli), 1.90 Å** Structure determined using conventional crystallization, 3.50 Å: 3V5S	3V5U	Data File Jmol Viewer 3V5U 3V5S	Liao et al. (2012). Liao J, Li H, Zeng W, Sauer DB, Belmares R, & Jiang Y (2012). Structural insight into the ion-exchange mechanism of the sodium/calcium exchanger. Science 335 :686-690. PubMed Id: 22323814. doi:10.1126/science.1215759.
*Vcx1 Ca²⁺/H⁺ (CaX) antiporter: Saccharomyces cerevisiae* E Eukaryota, 2.30 Å**	4K1C	Data File Jmol Viewer 4K1C	Waight et al. (2013). Waight AB, Pedersen BP, Schlessinger A, Bonomi M, Chau BH, Roe-Zurz Z, Risenmay AJ, Sali A, & Stroud RM (2013). Structural basis for alternating access of a eukaryotic calcium/proton exchanger. Nature 499 :107-110. PubMed Id: 23685453. doi:10.1038/nature12233.
*Ca²⁺/H⁺ (CaX) antiporter: Archaeoglobus fulgidus* A Archaea (expressed in E. coli), 2.30 Å**	4KPP	Data File Jmol Viewer 4KPP	Nishizawa et al. (2013). Nishizawa T, Kita S, Maturana AD, Furuya N, Hirata K, Kasuya G, Ogasawara S, Dohmae N, Iwamoto T, Ishitani R, & Nureki O (2013). Structural Basis for the Counter-Transport Mechanism of a H⁺/Ca²⁺ Exchanger. Science 341 :168-172. PubMed Id: 23704374.
*YfkE Ca²⁺/H⁺ (CaX) antiporter: Bacillus subtilis* B Bacteria (expressed in E. coli), 3.05 Å** Selenium substituted structure, 3.00 Å: 4KJR	4KJS	Data File Jmol Viewer 4KJS 4KJR	Wu et al. (2013). Wu M, Tong S, Waltersperger S, Diederichs K, Wang M, & Zheng L (2013). Crystal structure of Ca²⁺/H⁺ antiporter protein YfkE reveals the mechanisms of Ca²⁺ efflux and its pH regulation. Proc. Natl. Acad. Sci. U.S.A. 110 28:11367-11372. PubMed Id: 23798403. doi:10.1073/pnas.1302515110.
Nucleobase-Cation-Symport-1 (NCS1) Family
*Mhp1 Benzyl-hydantoin transporter (without substrate); outward-facing conformation: Microbacterium liquefaciens* B Bacteria (expressed in E. coli), 2.85 Å** With hydantion substrate; closed conformation, 4.0 Å: 2JLO.	2JLN	Data File Jmol Viewer 2JLN 2JLO	Weyand et al. (2008). Weyand S, Shimamura T, Yajima S, Suzuki S, Mirza O, Krusong K, Carpenter EP, Rutherford NG, Hadden JM, O'Reilly J, Ma P, Saidijam M, Patching SG, Hope RJ, Norbertczak HT, Roach PC, Iwata S, Henderson PJ, & Cameron AD (2008). Structure and Molecular Mechanism of a Nucleobase-Cation-Symport-1 Family Transporter. Science 322 :709-713. PubMed Id: 18927357.
*Mhp1 Benzyl-hydantoin transporter; inward-facing conformation: Microbacterium liquefaciens* B Bacteria (expressed in E. coli), 3.8 Å**	2X79	Data File Jmol Viewer 2X79	Shimamura et al. (2010). Shimamura T, Weyand S, Beckstein O, Rutherford NG, Hadden JM, Sharples D, Sansom MS, Iwata S, Henderson PJ, & Cameron AD (2010). Molecular basis of alternating access membrane transport by the sodium-hydantoin transporter Mhp1. Science 328 :470-473. PubMed Id: 20413494.
Nucleobase-Cation-Symport-2 (NCS2) Family also known as nucleobase/ascorbate transporter (NAT)
*UraA uracil/H⁺ symporter: Escherichia coli* B Bacteria, 2.78 Å** First example of a NAT/NCS2 protein. It has 14 transmembrane segments divided into two inverted repeats.	3QE7	Data File Jmol Viewer 3QE7	Lu et al. (2011). Lu F, Li S, Jiang Y, Jiang J, Fan H, Lu G, Deng D, Dang S, Zhang X, Wang J, & Yan N (2011). Structure and mechanism of the uracil transporter UraA Nature 472 :243-246. PubMed Id: 21423164. doi:10.1038/nature09885.
*UapA purine/H⁺ symporter in complex with Xanthine: Aspergillus nidulans* E Eukaryota (expressed in S. cerevisiae), 3.7 Å** The protein has 14 TM segments. Dimerization may be important in transport.	5I6C	Data File Jmol Viewer 5I6C	Alguel et al. (2016). Alguel Y, Amillis S, Leung J, Lambrinidis G, Capaldi S, Scull NJ, Craven G, Iwata S, Armstrong A, Mikros E, Diallinas G, Cameron AD, & Byrne B (2016). Structure of eukaryotic purine/H⁺ symporter UapA suggests a role for homodimerization in transport activity. Nat Commun 7 :11336. PubMed Id: 27088252. doi:10.1038/ncomms11336.
*Sodium-dependent vitamin C transporter (SVCT1) transporter: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure in an apo state, 3.50 Å: 7YTY	7YTW	Data File Jmol Viewer 7YTW 7YTY	Wang et al. (2023). Wang M, He J, Li S, Cai Q, Zhang K, & She J (2023). Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter. Nat Commun 14 1:1361. PubMed Id: 36914666. doi:10.1038/s41467-023-37037-3.
*AZG1 aza-guanine resistant protein 1, apo form at pH 7.4: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 2.70 Å** cryo-EM structure T440Y mutant, 2.90 Å: 8WO7 with bound 6-BAP, 2.70 Å: 8IRN with bound trans-zeatin, 2.70 Å: 8IRO with bound kinetin, 2.80 Å: 8IRP with bound adenine at pH 5.5, 2.60 Å: 8IRM with bound trans-zeatin at pH 5.5, 3.30 Å: 8WMQ	8IRL	Data File Jmol Viewer 8IRL 8WO7 8IRO 8IRN 8WMQ 8IRP 8IRM	Xu et al. (2024). Xu L, Jia W, Tao X, Ye F, Zhang Y, Ding ZJ, Zheng SJ, Qiao S, Su N, Zhang Y, Wu S, & Guo J (2024). Structures and mechanisms of the Arabidopsis cytokinin transporter AZG1. Nat Plants 10 1:180-191. PubMed Id: 38172575. doi:10.1038/s41477-023-01590-y.
Solute Carrier Family 4 (anion exchanger)
*Erythrocyte Band 3 anion exchanger: Homo sapiens* E Eukaryota, 3.5 Å**	4YZF	Data File Jmol Viewer 4YZF	Arakawa et al. (2015). Arakawa T, Kobayashi-Yurugi T, Alguel Y, Iwanari H, Hatae H, Iwata M, Abe Y, Hino T, Ikeda-Suno C, Kuma H, Kang D, Murata T, Hamakubo T, Cameron AD, Kobayashi T, Hamasaki N, & Iwata S (2015). Crystal structure of the anion exchanger domain of human erythrocyte band 3. Science 350 :680-684. PubMed Id: 26542571. doi:10.1126/science.aaa4335.
*Band 3 cytoplasmic domain: Homo sapiens* E Eukaryota (expressed in E. coli), 2.60 Å**	1HYN	Data File Jmol Viewer 1HYN	Zhang et al. (2000). Zhang D, Kiyatkin A, Bolin JT, & Low PS (2000). Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood 96 :2925-2933. PubMed Id: 11049968.
*Erythrocyte Band 3 anion exchanger complex. Band 3-Glycophorin A complex, outward facing: Homo sapiens* E Eukaryota, 2.35 Å** cryo-EM structure Ankyrin-1 complex, class 2 local refinement of AQP1 (C4 symmetry applied), 2.40 Å: 7UZE RhAG-RhCE-ANK1(AR1-5), local consensus refinement, 2.17 Å: 7UZQ Protein 4.2 (local refinement from consensus reconstruction of ankyrin complex classes), 2.20 Å: 7UZS Ankyrin-1 (N-terminal region of membrane binding domain, local refinement from consensus reconstruction; bound to N-terminal peptide from band 3, 2.30 Å:7UZU Band 3-I (local refinement) cytoplasmic domains, 2.50 Å: 7UZV Band 3-I-TM local refinement, ankyrin-1 complex consensus reconstruction, 2.80 Å: 7V07 ankyrin-1 (N-terminal half), class 1 of ankyrin-1 complex, 2.70 Å: 7V0M protein 4.2, class 1 of ankyrin-1 complex, 2.50 Å: 7V0Q RhAG/CE trimer, class 1 of ankyrin-1 complex, 2.50 Å: 7V0S Band 3-I cytoplasmic domains, class 1 of ankyrin-1, 2.70 Å: 7V0T Band 3-II cytoplasmic domains, class 1 of ankyrin-1 complex, 3.00 Å: 7V0U ankyrin-1 (C-terminal half), class 1 of ankyrin-1 complex, 3.00 Å: 7V0X Band 3-III cytoplasmic domains, class 1 of ankyrin-1 complex, 3.00 Å: 7V0Y Band 3-III cytoplasmic domains, class 1 of ankyrin-1, 3.30 Å: 7V19 Band 3-I transmembrane domains, class 1 of ankyrin-1 complex, 3.20 Å: 8CRQ Band 3-III transmembrane domains, class 1 of ankyrin-1 complex, 3.00 Å: 8CRR Rh trimer, glycophorin B and Band3-III transmembrane region, class 1a of ankyrin-1 complex, 3.00 Å: 8CRT Composite reconstruction of Class 1 of the erythrocyte ankyrin-1 complex, 2.74 Å: 8CS9 Sub-tomogram averaging of erythrocyte ankyrin-1 complex, 25 Å: 8CSL Anykyrin-1 (N-terminal half of membrane binding domain) in Class 2 of ankyrin-1 complex, 2.70 Å: 8CSV protein 4.2 in Class 2 of ankyrin-1 complex, 2.50 Å: 8CSW RhAG/CE trimer in class 2 of ankyrin-1 complex, 2.40 Å: 8CSX cytoplasmic domains of band3-I in class 2 of ankyrin-1 complex, 2.70 Å: 8CSY AQP1 tetramer in Class 2 of ankyrin-1 complex, 3.10 Å: 8CT2 band3-I transmembrane region from class 2 of ankyrin-1 complex, 3.30 Å: 8CT3 Class 2 of ankyrin-1 complex (Composite map), 2.90 Å: 8CTE	7UZ3	Data File Jmol Viewer 7UZ3 8CSL 8CSX 8CT2 8CSW 7UZE 8CRQ 7V19 8CRT 7UZU 7V0X 8CS9 8CSY 7V0U 7UZQ 8CRR 7V07 7UZS 8CSV 7UZV 8CTE 8CT3 7V0S 7V0M 7V0Q 7V0Y 7V0T	Vallese et al. (2022). Vallese F, Kim K, Yen LY, Johnston JD, Noble AJ, Calì T, & Clarke OB (2022). Architecture of the human erythrocyte ankyrin-1 complex. Nat Struct Mol Biol 29 7:706-718. PubMed Id: 35835865. doi:10.1038/s41594-022-00792-w.
*Band 3 (AE1) anion exchanger dimer, inward facing-inward facing, TM domain: Bos taurus* E Eukaryota, 4.40 Å** cryo-EM structure full length protein, 6.30 Å: 8EEQ inward-outward conformation, 6.00 Å: 8E34	8D9N	Data File Jmol Viewer 8D9N 8E34 8EEQ	Zhekova et al. (2022). Zhekova HR, Jiang J, Wang W, Tsirulnikov K, Kayık G, Khan HM, Azimov R, Abuladze N, Kao L, Newman D, Noskov SY, Tieleman DP, Hong Zhou Z, Pushkin A, & Kurtz I (2022). CryoEM structures of anion exchanger 1 capture multiple states of inward- and outward-facing conformations. Commun Biol 5 1:1372. PubMed Id: 36517642. doi:10.1038/s42003-022-04306-8.
*non-erythroid band 3-like protein (AE2) anion exchanger 2, acidic KNO₃ condition: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.32 Å** cryo-EM structure basic KNO₃ condition, outward-facing state, 3.09 Å: 8GVF with bound inhibitor DIDS, 3.08 Å: 8GV8 with bound Cl^- ion, 3.06 Å: 8GV9 with bound bicarbonate, 2.89 Å: 8GVC asymmetrical state, 3.17 Å: 8GVE	8GVH	Data File Jmol Viewer 8GVH 8GV9 8GVE 8GVF 8GVC 8GV8	Zhang et al. (2023). Zhang Q, Jian L, Yao D, Rao B, Xia Y, Hu K, Li S, Shen Y, Cao M, Qin A, Zhao J, & Cao Y (2023). The structural basis of the pH-homeostasis mediated by the Cl-/HCO3- exchanger, AE2. Nat Commun 14 1:1812. PubMed Id: 37002221. doi:10.1038/s41467-023-37557-y.
*non-erythroid band 3-like protein (AE2) anion exchanger 2 with bound PIP₂, inward-facing conformation: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure R932A/K1147A/H1148A mutant, inward-facing conformation, resting state, 3.30 Å: 8JNJ	8JNI	Data File Jmol Viewer 8JNI 8JNJ	Zhang et al. (2024). Zhang W, Ding D, Lu Y, Chen H, Jiang P, Zuo P, Wang G, Luo J, Yin Y, Luo J, & Yin Y (2024). Structural and functional insights into the lipid regulation of human anion exchanger 2. Nat Commun 15 1:759. PubMed Id: 38272905. doi:10.1038/s41467-024-44966-0.
Betaine/Choline/Carnitine Transporter (BCCT) Family
*BetP glycine betaine transporter: Corynebacterium glutamicum* B Bacteria (expressed in E. coli), 3.35 Å** A Na⁺-coupled symporter in an intermediate state. Formerly PDB 2W8A.	2WIT	Data File Jmol Viewer 2WIT	Ressl et al. (2009). Ressl S, Terwisscha van Scheltinga AC, Vonrhein C, Ott V, & Ziegler C (2009). Molecular basis of transport and regulation in the Na⁺/betaine symporter BetP. Nature 458 :47-52. PubMed Id: 19262666.
*BetP glycine betaine transporter in outward-facing conformation: Corynebacterium glutamicum* B Bacteria (expressed in E. coli), 3.25 Å** BetP with asymmetric protomers, 3.10 Å: 4AIN	4DOJ	Data File Jmol Viewer 4DOJ 4AIN	Perez et al. (2012). Perez C, Koshy C, Yildiz O, & Ziegler C (2012). Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP. Nature 490 :126-130. PubMed Id: 22940865. doi:10.1038/nature11403.
*BetP glycine betaine transporter with bound lipids: Corynebacterium glutamicum* B Bacteria (expressed in E. coli), 2.70 Å**	4C7R	Data File Jmol Viewer 4C7R	Koshy et al. (2013). Koshy C, Schweikhard ES, Gärtner RM, Perez C, Yildiz O, & Ziegler C (2013). Structural evidence for functional lipid interactions in the betaine transporter BetP. EMBO J 32 :3096-3105. PubMed Id: 24141878. doi:10.1038/emboj.2013.226.
*CaiT carnitine transporter: Escherichia coli* B Bacteria, 3.15 Å** This is a precursor/product antiporter that catalyzes the exchange of L-carnitine wtih γ-butyrobetaine. The protein is a homotrimer with each monomer containing 12 transmembrane helices.	3HFX	Data File Jmol Viewer 3HFX	Tang et al. (2010). Tang L, Bai L, Wang WH, & Jiang T (2010). Crystal structure of the carnitine transporter and insights into the antiport mechanism. Nat Struct Mol Biol 17 :492-496. PubMed Id: 20357772.
*CaiT carnitine transporter: Escherichia coli* B Bacteria, 3.50 Å** Fully-open inward-facing conformation.	2WSX	Data File Jmol Viewer 2WSX	Schulze et al. (2010). Schulze S, Köster S, Geldmacher U, Terwisscha van Scheltinga AC, & Kühlbrandt W. (2010). Structural basis of Na⁺-independent and cooperative substrate/product antiport in CaiT. Nature 467 :233-236. PubMed Id: 20829798.
*CaiT carnitine transporter: Proteus mirabilis* B Bacteria, 2.3 Å** Fully-open inward-facing conformation.	2WSW	Data File Jmol Viewer 2WSW	Schulze et al. (2010). Schulze S, Köster S, Geldmacher U, Terwisscha van Scheltinga AC, & Kühlbrandt W. (2010). Structural basis of Na⁺-independent and cooperative substrate/product antiport in CaiT. Nature 467 :233-236. PubMed Id: 20829798.
*CaiT carnitine transporter, R262E mutant with bound γ-butyrobetaine: Proteus mirabilis* B Bacteria (expressed in E. coli), 3.29 Å**	4M8J	Data File Jmol Viewer 4M8J	Kalayil et al. (2013). Kalayil S, Schulze S, & Kühlbrandt W (2013). Arginine oscillation explains Na+ independence in the substrate/product antiporter CaiT. Proc Natl Acad Sci USA 110 43:17296-17301. PubMed Id: 24101465. doi:10.1073/pnas.1309071110.
Amino Acid/Polyamine/Organocation (APC) Superfamily
*AdiC Arginine:Agmatine Antiporter: Escherichia coli* B Bacteria, 3.61 Å** 3LRB is a re-refinement of the original 3H5B structure, which contained a register shift of 3-4 amino acids relative to 3NCY and 3GIA (below).	3LRB	Data File Jmol Viewer 3LRB	Gao et al. (2009). Gao X, Lu F, Zhou L, Dang S, Sun L, Li X, Wang J, & Shi Y. (2009). Structure and mechanism of an amino acid antiporter. Science 324 :1565-1568. PubMed Id: 19478139.
*AdiC Arginine:Agmatine Antiporter (N22A, L123W mutant) with bound Arginine: Escherichia coli* B Bacteria, 3.0 Å** Outward-facing occluded state	3L1L	Data File Jmol Viewer 3L1L	Gao et al. (2010). Gao X, Zhou L, Jiao X, Lu F, Yan C, Zeng X, Wang J, & Shi Y (2010). Mechanism of substrate recognition and transport by an amino acid antiporter. Nature 463 :828-832. PubMed Id: 20090677.
*AdiC Arginine:Agmatine Antiporter (N101A mutant) with bound Arginine: Escherichia coli* B Bacteria, 3.0 Å** Reveals AdiC in the open-to-out conformation.	3OB6	Data File Jmol Viewer 3OB6	Kowalczyk et al. (2011). Kowalczyk L, Ratera M, Paladino A, Bartoccioni P, Errasti-Murugarren E, Valencia E, Portella G, Bial S, Zorzano A, Fita I, Orozco M, Carpena X, Vázquez-Ibar JL, & Palacín M (2011). Molecular basis of substrate-induced permeation by an amino acid antiporter. Proc Natl Acad Sci USA 108 :3935-3940. PubMed Id: 21368142.
*AdiC Arginine:Agmatine Antiporter in complex with agmatine: Escherichia coli* B Bacteria, 2.59 Å** apo protein, 2.21 Å: 5J4I	5J4N	Data File Jmol Viewer 5J4N 5J4I	Ilgü et al. (2016). Ilgü H, Jeckelmann JM, Gapsys V, Ucurum Z, de Groot BL, & Fotiadis D (2016). Insights into the molecular basis for substrate binding and specificity of the wild-type L-arginine/agmatine antiporter AdiC. Proc. Natl. Acad. Sci. U.S.A. 113 37:10358-10363. PubMed Id: 27582465. doi:10.1073/pnas.1605442113.
*AdiC Arginine:Agmatine Antiporter, outward open substrate-free state: Escherichia coli* E Eukaryota, 1.69 Å**	7O82	Data File Jmol Viewer 7O82	Ilgü et al. (2021). Ilgü H, Jeckelmann JM, Kalbermatter D, Ucurum Z, Lemmin T, & Fotiadis D (2021). High-resolution structure of the amino acid transporter AdiC reveals insights into the role of water molecules and networks in oligomerization and substrate binding. BMC Biol 19 1:179. PubMed Id: 34461897. doi:10.1186/s12915-021-01102-4.
*AdiC Arginine:Agmatine Antiporter (with Fab fragment): Salmonella enterica* B Bacteria (expressed in E. coli), 3.2 Å** PDB ID was originally 3HQK, which has been superseded by 3NCY.	3NCY	Data File Jmol Viewer 3NCY	Fang et al. (2009). Fang Y, Jayaram H, Shane T, Kolmakova-Partensky L, Wu F, Williams C, Xiong Y, & Miller C (2009). Structure of a prokaryotic virtual proton pump at 3.2 Å resolution. Nature 460 :1040-1043. PubMed Id: 19578361.
*apo ApcT Na⁺-independent Amino Acid Transporter: Methanocaldococcus jannaschii* A Archaea (expressed in E. coli), 2.35 Å** ApcT-7F11 Fab complex, 2.50 Å: 3GI9 ApcT-K158A/7F11 Fab complex, 2.60 Å: 3GI8	3GIA	Data File Jmol Viewer 3GIA 3GI9 3GI8	Shaffer et al. (2009). Shaffer PL, Goehring A, Shankaranarayanan A, & Gouaux E (2009). Structure and Mechanism of a Na⁺-independent amino acid transporter. Science 325 :1010-1014. PubMed Id: 19608859.
*GadC glutamate-GABA antiporter: Escherichia coli* B Bacteria, 3.10 Å** Structure at 3.19 Å: 4DJI	4DJK	Data File Jmol Viewer 4DJK 4DJI	Ma et al. (2012). Ma D, Lu P, Yan C, Fan C, Yin P, Wang J, & Shi Y (2012). Structure and mechanism of a glutamate-GABA antiporter. Nature 483 :632-636. PubMed Id: 22407317. doi:10.1038/nature10917.
*AgcS sodium/alanine symporter with bound L-alanine: Methanococcus maripaludis* B Bacteria (expressed in E. coli), 3.24 Å** with bound D-alanine, 3.3 Å: 6CSF	6CSE	Data File Jmol Viewer 6CSE 6CSF	Ma et al. (2019). Ma J, Lei HT, Reyes FE, Sanchez-Martinez S, Sarhan MF, Hattne J, & Gonen T (2019). Structural basis for substrate binding and specificity of a sodium-alanine symporter AgcS. Proc Natl Acad Sci USA 116 6:2086-2090. PubMed Id: 30659158. doi:10.1073/pnas.1806206116.
*BasC alanine-serine-cysteine exchanger, open-inward conformation: Carnobacterium sp. AT7* B Bacteria (expressed in E. coli), 2.92 Å** in complex with 2-AIB, 3.4 Å: 6F2W	6F2G	Data File Jmol Viewer 6F2G 6F2W	Errasti-Murugarren et al. (2019). Errasti-Murugarren E, Fort J, Bartoccioni P, Díaz L, Pardon E, Carpena X, Espino-Guarch M, Zorzano A, Ziegler C, Steyaert J, Fernández-Recio J, Fita I, & Palacín M (2019). L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction. Nat Commun 10 1:1807. PubMed Id: 31000719. doi:10.1038/s41467-019-09837-z.
*NKCC1 cation-chloride cotransporter (CCC) transmembrane domain: Danio rerio* E Eukaryota (expressed in Spodoptera frugiperda), 2.9 Å** cryo-EM structure C-terminal domain (CTD), 3.8 Å: 6NPJ TM domain, 3.6 Å: 6NPK NKCC1 structure, 2.9 Å: 6NPL	6NPH	Data File Jmol Viewer 6NPH 6NPJ 6NPK 6NPL	Chew et al. (2019). Chew TA, Orlando BJ, Zhang J, Latorraca NR, Wang A, Hollingsworth SA, Chen DH, Dror RO, Liao M, & Feng L (2019). Structure and mechanism of the cation-chloride cotransporter NKCC1. Nature 572 7770:488-492. PubMed Id: 31367042. doi:10.1038/s41586-019-1438-2.
*NKCC1 cation-chloride cotransporter (CCC), partially loaded, inward open state: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.46 Å** cryo-EM structure	6PZT	Data File Jmol Viewer 6PZT	Yang et al. (2020). Yang X, Wang Q, & Cao E (2020). Structure of the human cation-chloride cotransporter NKCC1 determined by single-particle electron cryo-microscopy. Nat Commun 11 1:1016. PubMed Id: 32081947. doi:10.1038/s41467-020-14790-3.
*KCC1 cation-chloride cotransporter (CCC) in glyo-diosgenin (GDN) detergent, 150 mM KCl: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.9 Å** cryo-EM structure in nano-discs, 150 mM KCl, 2.9 Å: 6KKT in GDN, 150 mM NaCl, 3.5 Å: 6KKU	6KKR	Data File Jmol Viewer 6KKR 6KKU 6KKT	Liu et al. (2019). Liu S, Chang S, Han B, Xu L, Zhang M, Zhao C, Yang W, Wang F, Li J, Delpire E, Ye S, Bai XC, & Guo J (2019). Cryo-EM structures of the human cation-chloride cotransporter KCC1. Science 366 6464:505-508. PubMed Id: 31649201. doi:10.1126/science.aay3129.
*KCC1 Δ19 cation-chloride cotransporter (CCC) in NaCl (Reference Map): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.12 Å** cryo-EM structure Subclass 1, 3.72 Å: 7AIQ Subclass 2, 3.66 Å: 7AIR	7AIP	Data File Jmol Viewer 7AIP 7AIR 7AIQ	Chi et al. (2021). Chi G, Ebenhoch R, Man H, Tang H, Tremblay LE, Reggiano G, Qiu X, Bohstedt T, Liko I, Almeida FG, Garneau AP, Wang D, McKinley G, Moreau CP, Bountra KD, Abrusci P, Mukhopadhyay SMM, Fernandez-Cid A, Slimani S, Lavoie JL, Burgess-Brown NA, Tehan B, DiMaio F, Jazayeri A, Isenring P, Robinson CV, & Dürr KL (2021). Phospho-regulation, nucleotide binding and ion access control in potassium-chloride cotransporters. EMBO J 40 14:e107294. PubMed Id: 34031912. doi:10.15252/embj.2020107294.
*KCC1 cation-chloride cotransporter (CCC) with bound VU0463271, outward-open state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure in 140 mM KCl, inward-open state, 3.25 Å: 7TTH	7TTI	Data File Jmol Viewer 7TTI 7TTH	Zhao et al. (2022). Zhao Y, Shen J, Wang Q, Ruiz Munevar MJ, Vidossich P, De Vivo M, Zhou M, & Cao E (2022). Structure of the human cation-chloride cotransport KCC1 in an outward-open state. Proc Natl Acad Sci U S A 119 27:e2109083119. PubMed Id: 35759661. doi:10.1073/pnas.2109083119.
*KCC3 cation-chloride cotransporter (CCC): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure	7D90	Data File Jmol Viewer 7D90	Xie et al. (2020). Xie Y, Chang S, Zhao C, Wang F, Liu S, Wang J, Delpire E, Ye S, & Guo J (2020). Structures and an activation mechanism of human potassium-chloride cotransporters. Sci Adv 6 50:eabc5883. PubMed Id: 33310850. doi:10.1126/sciadv.abc5883.
*KCC3b cation-chloride cotransporter (CCC), wild-type in NaCl: homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.64 Å** cryo-EM structure S45D/T940D/T997D mutant in KCl, 4.08 Å: 6Y5V S45D/T940D/T997D mutant in NaCl (Reference Map), 3.20 Å: 7AIN S45D/T940D/T997D mutant in NaCl (Subclass), 3.31 Å:7AIO	7NGB	Data File Jmol Viewer 7NGB 7AIN 6Y5V 7AIO	Chi et al. (2021). Chi G, Ebenhoch R, Man H, Tang H, Tremblay LE, Reggiano G, Qiu X, Bohstedt T, Liko I, Almeida FG, Garneau AP, Wang D, McKinley G, Moreau CP, Bountra KD, Abrusci P, Mukhopadhyay SMM, Fernandez-Cid A, Slimani S, Lavoie JL, Burgess-Brown NA, Tehan B, DiMaio F, Jazayeri A, Isenring P, Robinson CV, & Dürr KL (2021). Phospho-regulation, nucleotide binding and ion access control in potassium-chloride cotransporters. EMBO J 40 14:e107294. PubMed Id: 34031912. doi:10.15252/embj.2020107294.
*KCC4 cation-chloride cotransporter (CCC): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure	7D99	Data File Jmol Viewer 7D99	Xie et al. (2020). Xie Y, Chang S, Zhao C, Wang F, Liu S, Wang J, Delpire E, Ye S, & Guo J (2020). Structures and an activation mechanism of human potassium-chloride cotransporters. Sci Adv 6 50:eabc5883. PubMed Id: 33310850. doi:10.1126/sciadv.abc5883.
*KCC4 cation-chloride cotransporter (CCC) in nanodiscs: mus musculus* E Eukaryota (expressed in Sf9 cells), 3.65 Å** cryo-EM structure	6UKN	Data File Jmol Viewer 6UKN	Reid et al. (2020). Reid MS, Kern DM, & Brohawn SG (2020). Cryo-EM structure of the potassium-chloride cotransporter KCC4 in lipid nanodiscs. Elife 9 . PubMed Id: 32286222. doi:10.7554/eLife.52505.
*KimA K⁺/H⁺ symporter, inward-facing occluded state: Bacillus subtilis* B Bacteria (expressed in E. coli), 3.7 Å** cryo-EM structure Defining member of the K⁺ uptake (KUP) family	6S3K	Data File Jmol Viewer 6S3K	Tascón et al. (2020). Tascón I, Sousa JS, Corey RA, Mills DJ, Griwatz D, Aumüller N, Mikusevic V, Stansfeld PJ, Vonck J, & Hänelt I (2020). Structural basis of proton-coupled potassium transport in the KUP family. Nat Commun 11 1:626. PubMed Id: 32005818. doi:10.1038/s41467-020-14441-7.
*KimA K⁺/H⁺ symporter with bound cyclic-di-AMP in amphipols: Bacillus subtilis* B Bacteria, 3.80 Å** cryo-EM structure in DDM, 3.30 Å: 8B70	8B71	Data File Jmol Viewer 8B71 8B70	Fuss et al. (2023). Fuss MF, Wieferig JP, Corey RA, Hellmich Y, Tascón I, Sousa JS, Stansfeld PJ, Vonck J, & Hänelt I (2023). Cyclic di-AMP traps proton-coupled K+ transporters of the KUP family in an inward-occluded conformation. Nat Commun 14 1:3683. PubMed Id: 37344476. doi:10.1038/s41467-023-38944-1.
*NCC sodium-chloride cotransporter (SLC12 superfamily), full length: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.85 Å** cryo-EM structure NCC sodium-chloride cotransporter, 3.75 Å: 7YG0 C-terminal domain, 3.77 Å: 7YG1	7Y6I	Data File Jmol Viewer 7Y6I 7YG0 7YG1	Nan et al. (2022). Nan J, Yuan Y, Yang X, Shan Z, Liu H, Wei F, Zhang W, & Zhang Y (2022). Cryo-EM structure of the human sodium-chloride cotransporter NCC. Sci Adv 8 45:eadd7176. PubMed Id: 36351028. doi:10.1126/sciadv.add7176.
*NCC cation-chloride cotransporter (CCC): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.02 Å** cryo-EM structure Subclass 1, 2.95 Å: 8FHO Subclass 2, 3.00 Å: 8FHN Subclass 3-1, 3.04 Å: 8FHP Subclass 3-2, 2.81 Å: 8FHQ Subclass 3-3, 2.90 Å: 8FHR	8FHT	Data File Jmol Viewer 8FHT 8FHR 8FHP 8FHN 8FHO 8FHQ	Fan et al. (2023). Fan M, Zhang J, Lee CL, Zhang J, & Feng L (2023). Structure and thiazide inhibition mechanism of the human Na-Cl cotransporter. Nature 614 7949:788-793. PubMed Id: 36792826. doi:10.1038/s41586-023-05718-0.
Cation Diffusion Facilitator (CDF) Family
*YiiP Zinc Transporter: Escherichia coli* B Bacteria, 3.8 Å** 9-18, 2005)	2QFI	Data File Jmol Viewer 2QFI	Lu & Fu (2007). Lu M & Fu D (2007). Structure of the zinc transporter YiiP. Science 317 :1746-1748. PubMed Id: 17717154.
*YiiP Zinc Transporter: Escherichia coli* B Bacteria, 2.9 Å** 9-18, 2005)	3H90	Data File Jmol Viewer 3H90	Lu et al. (2009). Lu M, Chai J, & Fu D (2009). Structural basis for autoregulation of the zinc transporter YiiP. Nat Struct Mol Biol 16 :1063-1067. PubMed Id: 19749753.
*YiiP Zinc Transporter: Shewanella oneidensis* B Bacteria (expressed in E. coli), 4.1 Å** cryo-EM structure. Structure defines the differences between inward- and outward-facing conformations.	5VRF	Data File Jmol Viewer 5VRF	Lopez-Redondo et al. (2018). Lopez-Redondo ML, Coudray N, Zhang Z, Alexopoulos J, & Stokes DL (2018). Structural basis for the alternating access mechanism of the cation diffusion facilitator YiiP. Proc Natl Acad Sci USA 115 12:3042-3047. PubMed Id: 29507252. doi:10.1073/pnas.1715051115.
Antiporters
*NhaA Na⁺/H⁺ antiporter: Escherichia coli* B Bacteria, 3.45 Å**	1ZCD	Data File Jmol Viewer 1ZCD Na+_H+_antiporter	Hunte et al. (2005). Hunte C, Screpanti E, Venturi M, Rimon A, Padan E, & Michel H (2005). Structure of a Na(+)/H(+) antiporter and insights into mechanism of action and regulation by pH. Nature 435 :1197-1202. PubMed Id: 15988517.
*NhaA Na⁺/H⁺ antiporter: Escherichia coli* B Bacteria, by electron crystallography** Difference maps show structural changes with changes in pH.	3FI1	Data File Jmol Viewer 3FI1	Appel et al. (2009). Appel M, Hizlan D, Vinothkumar KR, Ziegler C, Kühlbrandt W (2009). Conformations of NhaA, the Na/H exchanger from Escherichia coli, in the pH-activated and ion-translocating states. J Mol Biol 386 :351-365. PubMed Id: 19135453.
*NhaA Na⁺/H⁺ antiporter in dimeric state (inward-facing): Escherichia coli* B Bacteria, 3.70 Å** triple mutant (A109T, Q277G, L296M), 3.50 Å: 4ATV	4AU5	Data File Jmol Viewer 4AU5 4ATV	Lee et al. (2014). Lee C, Yashiro S, Dotson DL, Uzdavinys P, Iwata S, Sansom MS, von Ballmoos C, Beckstein O, Drew D, & Cameron AD (2014). Crystal structure of the sodium-proton antiporter NhaA dimer and new mechanistic insights. J Gen Physiol 144 6:529-544. PubMed Id: 25422503. doi:10.1085/jgp.201411219.
*NhaA Na⁺/H⁺ antiporter at pH 6.5: Escherichia coli* B Bacteria, 2.20 Å**	7S24	Data File Jmol Viewer 7S24	Winkelmann et al. (2022). Winkelmann I, Uzdavinys P, Kenney IM, Brock J, Meier PF, Wagner LM, Gabriel F, Jung S, Matsuoka R, von Ballmoos C, Beckstein O, & Drew D (2022). Crystal structure of the Na⁺/H⁺ antiporter NhaA at active pH reveals the mechanistic basis for pH sensing. Nat Commun 13 1:6383. PubMed Id: 36289233. doi:10.1038/s41467-022-34120-z.
*NapA Na⁺/H⁺ antiporter: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.98 Å**	4BWZ	Data File Jmol Viewer 4BWZ	Lee et al. (2013). Lee C, Kang HJ, von Ballmoos C, Newstead S, Uzdavinys P, Dotson DL, Iwata S, Beckstein O, Cameron AD, & Drew D (2013). A two-domain elevator mechanism for sodium/proton antiport. Nature 501 :573-577. PubMed Id: 23995679. doi:10.1038/nature12484.
*NapA Na⁺/H⁺ antiporter, outward facing: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.3 Å** inward facing, 3.7 Å: 5BZ2	5BZ3	Data File Jmol Viewer 5BZ3 5BZ2	Coincon et al. (2016). Coincon M, Uzdavinys P, Nji E, Dotson DL, Winkelmann I, Abdul-Hussein S, Cameron AD, Beckstein O, & Drew D (2016). Crystal structures reveal the molecular basis of ion translocation in sodium/proton antiporters. Nat Struct Mol Biol 23 :248-255. PubMed Id: 26828964. doi:10.1038/nsmb.3164.
*NhaP Na⁺/H⁺ antiporter, pH 8: Pyrococcus abyssi* A Archaea (expressed in E. coli), 3.15 Å** pH 4 structure, 3.50 Å: 4CZ9 with bound thalium ion, 3.20 Å: 4CZA	4CZ8	Data File Jmol Viewer 4CZ8 4CZA 4CZ9	Wöhlert et al. (2014). Wöhlert D, Kühlbrandt W, & Yildiz Ö (2014). Structure and substrate ion binding in the sodium/proton antiporter PaNhaP. Elife 3 :e03579. PubMed Id: 25426802. doi:10.7554/eLife.03579.
*NhaP1 Na⁺/H⁺ antiporter, pH 8: Methanocaldococcus jannaschii* A Archaea (expressed in E. coli), 3.50 Å** EM 2D crystal reconstruction structure, pH 4. In-plane resolution 6 Å: 4D0A	4CZB	Data File Jmol Viewer 4CZB 4D0A	Paulino et al. (2014). Paulino C, Wöhlert D, Kapotova E, Yildiz Ö, & Kühlbrandt W (2014). Structure and transport mechanism of the sodium/proton antiporter MjNhaP1. Elife 3 :e03583. PubMed Id: 25426803. doi:10.7554/eLife.03583.
*Mitochondrial ADP/ATP Carrier: Bos taurus heart mitochondria* E Eukaryota, 2.2 Å** Monomeric, in complex with carboxyatractyloside inhibitor.	1OKC	Data File Jmol Viewer 1OKC ADP/ATP carrier protein	Pebay-Peyroula et al. (2003). Pebay-Peyroula E, Dahout-Gonzalez C, Kahn R, Trezeguet V, Lauquin GJ, & Brandolin G (2003). Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside. Nature 426 :39-44. PubMed Id: 14603310.
*Mitochondrial ADP/ATP Carrier: Bos taurus heart mitochondria* E Eukaryota, 2.8 Å** Biological dimer with endogenous cardiolipins.	2C3E	Data File Jmol Viewer 2C3E	Nury et al. (2005). Nury H, Dahout-Gonzalez C, Trézéguet V, Lauquin G, Brandolin G, & Pebay-Peyroula E (2005). Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers. FEBS Lett 579 :13561-13556. PubMed Id: 16226253.
*Mitochondrial ADP/ATP Carrier; isoform 2 inhibited by carboxyatractyloside (C222₁ crystal form): Saccharomyces cerevisiae* E Eukaryota, 2.49 Å** isoform 2 inhibited by carboxyatractyloside (P2₁2₁2₁ crystal form), 3.20 Å: 4C9H isoform 3 inhibited by carboxyatractyloside (P2₁ crystal form), 3.20 Å: 4C9Q isoform 3 inhibited by carboxyatractyloside (P2₁2₁2₁ crystal form), 3.40 Å: 4C9J	4C9G	Data File Jmol Viewer 4C9G 4C9J 4C9Q 4C9H	Ruprecht et al. (2014). Ruprecht JJ, Hellawell AM, Harding M, Crichton PG, McCoy AJ, & Kunji ER (2014). Structures of yeast mitochondrial ADP/ATP carriers support a domain-based alternating-access transport mechanism. Proc. Natl. Acad. Sci. U.S.A. 111 :E426-E434. PubMed Id: 24474793. doi:10.1073/pnas.1320692111.
*Mitochondrial ADP/ATP carrier, bongkrekic acid-inhibited: Myceliophthora thermophila* E Eukaryota (expressed in S. cerevisiae), 3.3 Å**	6GCI	Data File Jmol Viewer 6GCI	Ruprecht et al. (2019). Ruprecht JJ, King MS, Zögg T, Aleksandrova AA, Pardon E, Crichton PG, Steyaert J, & Kunji ERS (2019). The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier. Cell 176 3:435-447.e15. PubMed Id: 30611538. doi:10.1016/j.cell.2018.11.025.
*UCP1 mitochondrial uncoupling protein 1: Homo sapiens* E Eukaryota (expressed in S. cerevisiae), 3.80 Å** cryo-EM structure	8G8W	Data File Jmol Viewer 8G8W	Jones et al. (2023). Jones SA, Gogoi P, Ruprecht JJ, King MS, Lee Y, Zögg T, Pardon E, Chand D, Steimle S, Copeman DM, Cotrim CA, Steyaert J, Crichton PG, Moiseenkova-Bell V, & Kunji ERS (2023). Structural basis of purine nucleotide inhibition of human uncoupling protein 1. Sci Adv 9 22:eadh4251. PubMed Id: 37256948. doi:10.1126/sciadv.adh4251.
*UCP1 mitochondrial uncoupling protein 1, nucleotide-free state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.51 Å** cryo-EM structure ATP-bound state, 2.57 Å: 8HBW DNP-bound state, 2.51 Å: 8J1N	8HBV	Data File Jmol Viewer 8HBV 8J1N 8HBW	Kang & Chen (2023). Kang Y, & Chen L (2023). Structural basis for the binding of DNP and purine nucleotides onto UCP1. Nature 620 7972:226-231. PubMed Id: 37336486. doi:10.1038/s41586-023-06332-w.
*UCP2 mitochondrial uncoupling protein 2: Mus musculus* E Eukaryota (expressed in E. coli), NMR structure** Solved by a combination of NMR residual dipolar couplings, paramagnetic relaxation enhancement, and molecular fragment replacement.	2LCK	Data File Jmol Viewer 2LCK	Berardi et al. (2011). Berardi MJ, Shih WM, Harrison SC, & Chou JJ (2011). Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching Nature 476 :109-113. PubMed Id: 21785437. doi:10.1038/nature10257.
*Multiple resistance & pH adaptation (Mrp) complex Na⁺/H⁺ antiporter: Dietzia sp. DQ12-45-1b* B Bacteria (expressed in E. coli), 3.00 Å** cryo-EM structure	7D3U	Data File Jmol Viewer 7D3U	Li et al. (2020). Li B, Zhang K, Nie Y, Wang X, Zhao Y, Zhang XC, & Wu XL (2020). Structure of the Dietzia Mrp complex reveals molecular mechanism of this giant bacterial sodium proton pump. Proc Natl Acad Sci U S A 117 49:31166-31176. PubMed Id: 33229520. doi:10.1073/pnas.2006276117.
*Multiple resistance & pH adaptation (Mrp) complex Na⁺/H⁺ antiporter: Alkalihalobacillus pseudofirmus* B Bacteria (expressed in E. coli), 2.24 Å** cryo-EM structure	7QRU	Data File Jmol Viewer 7QRU	Lee et al. (2022). Lee Y, Haapanen O, Altmeyer A, Kühlbrandt W, Sharma V, & Zickermann V (2022). Ion transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations. Nat Commun 13 1:6091. PubMed Id: 36241630. doi:10.1038/s41467-022-33640-y.
*Na⁺/H⁺ exchanger NHE9 (SLC9A9), inward-facing conformation: Equus caballus* E Eukaryota (expressed in S. cerevisiae), 3.51 Å** cryo-EM structure without C-terminal regulatory domain, 3.19 Å: 6Z3Z	6Z3Y	Data File Jmol Viewer 6Z3Y 6Z3Z	Winkelmann et al. (2020). Winkelmann I, Matsuoka R, Meier PF, Shutin D, Zhang C, Orellana L, Sexton R, Landreh M, Robinson CV, Beckstein O, & Drew D (2020). Structure and elevator mechanism of the mammalian sodium/proton exchanger NHE9. EMBO J 39 :e105908. PubMed Id: 33118634. doi:10.15252/embj.2020105908.
*Na⁺/H⁺ exchanger NHA2 (SLC9B2) in detergent with N-terminal extension helix: Bison bison* E Eukaryota (expressed in Saccharomyces cerevisiae), 3.15 Å** cryo-EM structure in detergent, 3.04 Å 7P1J in nano disc, 3.64 Å 7P1K	7P1I	Data File Jmol Viewer 7P1I 7P1K 7P1J	Matsuoka et al. (2022). Matsuoka R, Fudim R, Jung S, Zhang C, Bazzone A, Chatzikyriakidou Y, Robinson CV, Nomura N, Iwata S, Landreh M, Orellana L, Beckstein O, & Drew D (2022). Structure, mechanism and lipid-mediated remodeling of the mammalian Na⁺/H⁺ exchanger NHA2. Nat Struct Mol Biol 29 2:108-120. PubMed Id: 35173351. doi:10.1038/s41594-022-00738-2.
*sperm-specific Na⁺/H⁺ exchanger (SLC91C1): Strongylocentrotus purpuratus* E Eukaryota (expressed in HEK293 cells), 3.08 Å** cryo-EM structure in GDN, 3.22 Å: 8OTQ in presence of cAMP, 3.68 Å: 8OTW	8OTX	Data File Jmol Viewer 8OTX 8OTW 8OTQ	Yeo et al. (2023). Yeo H, Mehta V, Gulati A, & Drew D (2023). Structure and electromechanical coupling of a voltage-gated Na⁺/H⁺ exchanger. Nature 623 7985:193-201. PubMed Id: 37880360. doi:10.1038/s41586-023-06518-2.
*Na⁺/H⁺ exchanger NHE1-CHP1 complex, under pH 7.5: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure under pH 6.5, 3.40 Å: 7DSV under pH 7.5, bound by cariporide, 3.50 Å: 7DSX	7DSW	Data File Jmol Viewer 7DSW 7DSX 7DSV	Dong et al. (2021). Dong Y, Gao Y, Ilie A, Kim D, Boucher A, Li B, Zhang XC, Orlowski J, & Zhao Y (2021). Structure and mechanism of the human NHE1-CHP1 complex. Nat Commun 12 1:3474. PubMed Id: 34108458. doi:10.1038/s41467-021-23496-z.
Apical Sodium-Dependent Bile Acid Transporters (ASBT) Closely related to sodium taurocholate co-transporting polypeptide (NTCP). Both proteins are members of SLC10 solute carrier family
*Bacterial homologue of ASBT (ASBT_NM) with bound taurocholate: Neisseria meningitidis* B Bacteria (expressed in E. coli), 2.20 Å** Derivatized Cys mutant soaked in mercury acetate, 2.20 Å: 3ZUX The protein is structurally similar to the NhaA Na⁺/H⁺ antiporter 1ZCD	3ZUY	Data File Jmol Viewer 3ZUY 3ZUX	Hu et al. (2011). Hu NJ, Iwata S, Cameron AD, & Drew D (2011). Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT. Nature 478 :408-411. PubMed Id: 21976025. doi:10.1038/nature10450.
*Bacterial homologue of ASBT (ASBT_Yf), inward-open conformation: Yersinia frederiksenii* B Bacteria (expressed in E. coli), 1.95 Å** E254A mutant, probable outward-open conformation, 2.50 Å: 4N7X	4N7W	Data File Jmol Viewer 4N7W 4N7X	Zhou et al. (2014). Zhou X, Levin EJ, Pan Y, McCoy JG, Sharma R, Kloss B, Bruni R, Quick M, & Zhou M (2014). Structural basis of the alternating-access mechanism in a bile acid transporter. Nature 505 :569-573. PubMed Id: 24317697. doi:10.1038/nature12811.
*Bacterial homologue of ASBT (ASBT_γf), P10C-S291C mutant, inward-facing state complexed with citrate: Yersinia frederiksenii* B Bacteria (expressed in E. coli), 1.85 Å** inward-facing apo-state, 2.81 Å: 6LH0 inward-facing state complexed with sulfate, 2.43 Å: 6LGZ inward-facing state complexed with glycine and sodium, 2.25 Å: 6LGY	6LGV	Data File Jmol Viewer 6LGV 6LGZ 6LGY 6LH0	Wang et al. (2021). Wang X, Lyu Y, Ji Y, Sun Z, & Zhou X (2021). Substrate binding in the bile acid transporter ASBT_γf from Yersinia frederiksenii. Acta Crystallogr D Struct Biol 77 :117-125. PubMed Id: 33404531. doi:10.1107/S2059798320015004.
*Bacterial homologue of ASBT (ASBT_Yf), cysteine-pair mutant (Y113C-P190C), outward facing state: Yersinia frederiksenii* B Bacteria (expressed in E. coli), 2.86 Å** before disulfide bond formation, 3.20 Å: 7CYG cysteine-pair mutant (V110C-I197C) before disulfide bond formation, 2.79 Å: 7CYK	6LH1	Data File Jmol Viewer 6LH1 7CYG 7CYK	Wang et al. (2021). Wang X, Lyu Y, Ji Y, Sun Z, & Zhou X (2021). An engineered disulfide bridge traps and validates an outward-facing conformation in a bile acid transporter. Acta Crystallogr D Struct Biol 77 :108-116. PubMed Id: 33404530. doi:10.1107/S205979832001517X.
*sodium taurocholate co-transporting polypeptide (NTCP) transporter: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.30 Å** cryo-EM structure	7FCI	Data File Jmol Viewer 7FCI	Park et al. (2022). Park JH, Iwamoto M, Yun JH, Uchikubo-Kamo T, Son D, Jin Z, Yoshida H, Ohki M, Ishimoto N, Mizutani K, Oshima M, Muramatsu M, Wakita T, Shirouzu M, Liu K, Uemura T, Nomura N, Iwata S, Watashi K, Tame JRH, Nishizawa T, Lee W, & Park SY (2022). Structural insights into the HBV receptor and bile acid transporter NTCP. Nature 606 7916:1027-1031. PubMed Id: 35580630. doi:10.1038/s41586-022-04857-0.
*sodium taurocholate co-transporting polypeptide (NTCP) transporter in complex with nanobody 87: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.70 Å** cryo-EM structure in complex with Megabody 91, 3.30 Å 7PQQ	7PQG	Data File Jmol Viewer 7PQG 7PQQ	Goutam et al. (2022). Goutam K, Ielasi FS, Pardon E, Steyaert J, & Reyes N (2022). Structural basis of sodium-dependent bile salt uptake into the liver. Nature 606 7916:1015-1020. PubMed Id: 35545671. doi:10.1038/s41586-022-04723-z.
*sodium taurocholate co-transporting polypeptide (NTCP) transporter in complex with Fab and nanobody: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.88 Å** cryo-EM structure	7ZYI	Data File Jmol Viewer 7ZYI	Liu et al. (2022). Liu H, Irobalieva RN, Bang-Sørensen R, Nosol K, Mukherjee S, Agrawal P, Stieger B, Kossiakoff AA, & Locher KP (2022). Structure of human NTCP reveals the basis of recognition and sodium-driven transport of bile salts into the liver. Cell Res 32 8:773-776. PubMed Id: 35726088. doi:10.1038/s41422-022-00680-4.
*sodium taurocholate co-transporting polypeptide (NTCP), in complex with YN69202Fab: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.41 Å** cryo-EM structure in presence of myristoylated preS1 peptide, 3.32 Å: 7VAG wild-type, 3.32 Å: 7WSI	7VAD	Data File Jmol Viewer 7VAD 7WSI 7VAG	Asami et al. (2022). Asami J, Kimura KT, Fujita-Fujiharu Y, Ishida H, Zhang Z, Nomura Y, Liu K, Uemura T, Sato Y, Ono M, Yamamoto M, Noda T, Shigematsu H, Drew D, Iwata S, Shimizu T, Nomura N, & Ohto U (2022). Structure of the bile acid transporter and HBV receptor NTCP. Nature 606 7916:1021-1026. PubMed Id: 35580629. doi:10.1038/s41586-022-04845-4.
*sodium taurocholate co-transporting polypeptide (NTCP), in complex with YN69202Fab: Bos taurus* E Eukaryota (expressed in S. frugiperda), 3.55 Å** cryo-EM structure	7VAE	Data File Jmol Viewer 7VAE	Asami et al. (2022). Asami J, Kimura KT, Fujita-Fujiharu Y, Ishida H, Zhang Z, Nomura Y, Liu K, Uemura T, Sato Y, Ono M, Yamamoto M, Noda T, Shigematsu H, Drew D, Iwata S, Shimizu T, Nomura N, & Ohto U (2022). Structure of the bile acid transporter and HBV receptor NTCP. Nature 606 7916:1021-1026. PubMed Id: 35580629. doi:10.1038/s41586-022-04845-4.
*sodium taurocholate co-transporting polypeptide (NTCP), in complex with YN69202Fab: Mus musculus* E Eukaryota (expressed in S. frugiperda), 3.11 Å** cryo-EM structure	7VAF	Data File Jmol Viewer 7VAF	Asami et al. (2022). Asami J, Kimura KT, Fujita-Fujiharu Y, Ishida H, Zhang Z, Nomura Y, Liu K, Uemura T, Sato Y, Ono M, Yamamoto M, Noda T, Shigematsu H, Drew D, Iwata S, Shimizu T, Nomura N, & Ohto U (2022). Structure of the bile acid transporter and HBV receptor NTCP. Nature 606 7916:1021-1026. PubMed Id: 35580629. doi:10.1038/s41586-022-04845-4.
Energy-Coupling Factor (ECF) Transporters
*RibU, S Component of the Riboflavin Transporter: Staphylococcus aureus* B Bacteria (expressed in E. coli), 3.6 Å**	3P5N	Data File Jmol Viewer 3P5N	Zhang et al. (2010). Zhang P, Wang J, & Shi Y (2010). Structure and mechanism of the S component of a bacterial ECF transporter. Nature 468 :717-720. PubMed Id: 20972419.
*ThiT, S component of the Thiamin Transporter: Lactococcus lactis* B Bacteria, 2.00 Å**	3RLB	Data File Jmol Viewer 3RLB	Erkens et al. (2011). Erkens GB, Berntsson RP, Fulyani F, Majsnerowska M, Vujčić-Žagar A, Ter Beek J, Poolman B, & Slotboom DJ (2011). The structural basis of modularity in ECF-type ABC transporters. Nat Struct Mol Biol 18 :755-760. PubMed Id: 21706007. doi:10.1038/nsmb.2073.
*BioY, S component of the Biotin Transporter: Lactococcus lactis* B Bacteria, 2.09 Å**	4DVE	Data File Jmol Viewer 4DVE	Berntsson et al. (2012). Berntsson RP, ter Beek J, Majsnerowska M, Duurkens RH, Puri P, Poolman B, & Slotboom DJ (2012). Structural divergence of paralogous S components from ECF-type ABC transporters. Proc Natl Acad Sci USA 109 :13990-13995. PubMed Id: 22891302. doi:10.1073/pnas.1203219109.
*Folate ECF transporter complex: Lactobacillus brevis* B Bacteria (expressed in E. coli), 3.00 Å** Structure of the intact transporter consisting of FolT, EcfT, EcfA, and EcfA'.	4HUQ	Data File Jmol Viewer 4HUQ	Xu et al. (2013). Xu K, Zhang M, Zhao Q, Yu F, Guo H, Wang C, He F, Ding J, & Zhang P (2013). Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis. Nature 497 :268-271. PubMed Id: 23584589. doi:10.1038/nature12046.
*ECF transporter complex: Lactobacillus brevis* B Bacteria (expressed in E. coli), 3.53 Å** Thought to be specific for hydroxymethylpyrimidine (HMP).	4HZU	Data File Jmol Viewer 4HZU	Wang et al. (2013). Wang T, Fu G, Pan X, Wu J, Gong X, Wang J, & Shi Y (2013). Structure of a bacterial energy-coupling factor transporter. Nature 497 :272-276. PubMed Id: 23584587.
*Folate ECF transporter, apo form: Lactobacillus delbrueckii* B Bacteria (expressed in E. coli), 3.0 Å** AMPPNP bound state, 3.3 Å: 5D3M Substrate bound S-component, 3.01 Å: 5D0Y	5JSZ	Data File Jmol Viewer 5JSZ 5D3M 5D0Y	Swier et al. (2016). Swier LJ, Guskov A, & Slotboom DJ (2016). Structural insight in the toppling mechanism of an energy-coupling factor transporter. Nat Commun 7 :11072. PubMed Id: 27026363. doi:10.1038/ncomms11072.
*Folate ECF transporter complex in MSP2N2 lipid nanodiscs: Lactobacillus delbrueckii* B Bacteria (expressed in E. coli), 2.20 Å** cryo-EM structure complex in DDM micelles, 3.40 Å 7NNT	7NNU	Data File Jmol Viewer 7NNU 7NNT	Thangaratnarajah et al. (2021). Thangaratnarajah C, Rheinberger J, Paulino C, & Slotboom DJ (2021). Insights into the bilayer-mediated toppling mechanism of a folate-specific ECF transporter by cryo-EM. Proc Natl Acad Sci U S A 118 34:e2105014118. PubMed Id: 34408021. doi:10.1073/pnas.2105014118.
*ECF-PanT energy-coupling factor pantothenate transporter: Lactobacillus brevis* B Bacteria, 3.23 Å**	4RFS	Data File Jmol Viewer 4RFS	Zhang et al. (2014). Zhang M, Bao Z, Zhao Q, Guo H, Xu K, Wang C, & Zhang P (2014). Structure of a pantothenate transporter and implications for ECF module sharing and energy coupling of group II ECF transporters. Proc Natl Acad Sci USA 111 52:18560-18565. PubMed Id: 25512487. doi:10.1073/pnas.1412246112.
*ECF-PanT energy-coupling factor pantothenate transporter in complex with a nanobody: Lactobacillus delbrueckii* B Bacteria (expressed in E. coli), 2.80 Å**	6ZG3	Data File Jmol Viewer 6ZG3	Setyawati et al. (2020). Setyawati I, Stanek WK, Majsnerowska M, Swier LJYM, Pardon E, Steyaert J, Guskov A, & Slotboom DJ (2020). In vitro reconstitution of dynamically interacting integral membrane subunits of energy-coupling factor transporters. Elife 9 :e64389. PubMed Id: 33350937. doi:10.7554/eLife.64389.
*BtuM cobalamin transporter: Thiobacillus denitrificans* B Bacteria (expressed in E. coli), 2.01 Å**	6FFV	Data File Jmol Viewer 6FFV	Rempel et al. (2018). Rempel S, Colucci E, de Gier JW, Guskov A, & Slotboom DJ (2018). Cysteine-mediated decyanation of vitamin B12 by the predicted membrane transporter BtuM. Nat Commun 9 1:3038. PubMed Id: 30072686. doi:10.1038/s41467-018-05441-9.
*Group II energy-coupling factor (ECF) transporter for vitamin B12, apo inward-facing state: Lactobacillus delbrueckii* B Bacteria, 3.40 Å**	6FNP	Data File Jmol Viewer 6FNP	Santos et al. (2018). Santos JA, Rempel S, Mous ST, Pereira CT, Ter Beek J, de Gier JW, Guskov A, & Slotboom DJ (2018). Functional and structural characterization of an ECF-type ABC transporter for vitamin B12. Elife 7 :e35828. PubMed Id: 29809140. doi:10.7554/eLife.35828.
ATP Binding Cassette (ABC) Transporters Reviewed by Hou et al. (2022)
*BtuCD Vitamin B₁₂ Transporter: Escherichia coli* B Bacteria, 3.2 Å**	1L7V	Data File Jmol Viewer 1L7V BtuCD ABC transporter, BtuC subunit	Locher et al. (2002). Locher KP, Lee AT, & Rees DC (2002). The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism. Science 296 :1091-1098. PubMed Id: 12004122.
*BtuCD-F Complex; BtuCD B₁₂ Transporter + BtuF binding protein: Escherichia coli* B Bacteria, 2.6 Å**	2QI9	Data File Jmol Viewer 2QI9	Hvorup et al. (2007). Hvorup RN, Goetz BA, Niederer M, Hollenstein K, Perozo E, & Locher KP (2007). Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF. Science 317 :1387-1390. PubMed Id: 17673622.
*BtuCD-F Vitamin B₁₂ Transporter with bound AMP-PNP: Escherichia coli* B Bacteria, 3.47 Å** Has engineered disulphide cross-linking. Structure suggests a peristaltic transport mechanism.	4FI3	Data File Jmol Viewer 4FI3	Korkhov et al. (2012). Korkhov VM, Mireku SA, & Locher KP (2012). Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F. Nature 490 :367-372. PubMed Id: 23000901. doi:10.1038/nature11442.
*Sav1866 Multidrug Transporter: Staphylococcus aureus* B Bacteria, 3.0 Å**	2HYD	Data File Jmol Viewer 2HYD	Dawson and Locher (2006). Dawson RJP & Locher KP (2006). Structure of a bacterial multidrug ABC transporter. Nature 443 :180-185. PubMed Id: 16943773.
*Sav1866 Multidrug Transporter in complex with AMP-PNP: Staphylococcus aureus* B Bacteria (expressed in E. coli), 3.40 Å**	2ONJ	Data File Jmol Viewer 2ONJ	Dawson & Locher (2007). Dawson RJ, & Locher KP (2007). Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett 581 5:935-938. PubMed Id: 17303126.
*Molybdate Transporter ModB₂C₂ Complexed with ModA: Archaeoglobus fulgidus* A Archaea, 3.1 Å** ModA with bound MoO₄, 1.60 Å 2ONR ModA with bound WO₄, 1.55 Å 2ONS	2ONK	Data File Jmol Viewer 2ONK 2ONS 2ONR	Hollenstein et al. (2007). Hollenstein K, Frei DC, & Locher KP (2007). Structure of an ABC transporter in complex with its binding protein. Nature 446 :213-216. PubMed Id: 17322901.
*ModBC Molybdate ABC Transporter in a trans-inhibited state: Methanosarcina acetivorans* A Archaea, 3.0 Å**	3D31	Data File Jmol Viewer 3D31	Gerber et al. (2008). Gerber S, Comellas-Bigler M, Goetz BA, & Locher KP (2008). Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter. Science 321 :246-250. PubMed Id: 18511655.
*HI1470/1 Putative Metal-Chelate-type ABC Transporter: Haemophilus influenzae* B Bacteria, 2.4 Å** First structure showing an inward-facing conformation of an ABC transporter	2NQ2	Data File Jmol Viewer 2NQ2	Pinkett et al. (2007). Pinkett HW, Lee AT, Lum P, Locher KP & Rees DC (2007). An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science 315 :373-377. PubMed Id: 17158291.
*MsbA Lipid "flippase" with bound AMPPNP: Salmonella typhimurium* B Bacteria (expressed in E. coli), 3.7 Å** MsbA with bound AMPPNP used for initial model: 3B5Y, 4.5 Å ADP + Vanadate-bound conformation: 3B5Z, 4.2 Å Open apo-conformation (E. coli): 3B5W, 5.3 Å Closed apo-conformation (Vibrio cholerae expressed in E. coli): 3B5X, 5.5 Å	3B60	Data File Jmol Viewer 3B60 3B5Z 3B5X 3B5Y 3B5W	Ward et al. (2007). Ward A, Reyes CL, Yu J, Roth CB, & Chang G (2007). Flexibility in the ABC transporter MsbA: Alternating access with a twist. Proc Natl Acad Sci U S A 104 :19005-19010. PubMed Id: 18024585.
*MsbA Lipid "flippase" with bound lipid A: Salmonella typhimurium* B Bacteria (expressed in E. coli), 2.8 Å** apo protein, 4.47 Å: 6O30	6BL6	Data File Jmol Viewer 6BL6 6O30	Padayatti et al. (2019). Padayatti PS, Lee SC, Stanfield RL, Wen PC, Tajkhorshid E, Wilson IA, & Zhang Q (2019). Structural Insights into the Lipid A Transport Pathway in MsbA. Structure 27 7:1114-1123.e3. PubMed Id: 31130486. doi:10.1016/j.str.2019.04.007.
*MsbA Lipid "flippase" in nano-discs with bound LPS: Escherichia coli* B Bacteria, 4.2 Å** cryo-EM structure with bound ADP-vanadate, 4.8 Å: 5TTP	5TV4	Data File Jmol Viewer 5TV4 5TTP	Mi et al. (2017). Mi W, Li Y, Yoon SH, Ernst RK, Walz T, & Liao M (2017). Structural basis of MsbA-mediated lipopolysaccharide transport. Nature 549 :233-237. PubMed Id: 28869968. doi:10.1038/nature23649.
*MsbA Lipid "flippase" in complex with LPS and inhibitor G907: Escherichia coli* B Bacteria, 2.91 Å** in complex with LPS and inhibitor G092, 2.92 Å: 6BPP	6BPL	Data File Jmol Viewer 6BPL 6BPP	Ho et al. (2018). Ho H, Miu A, Alexander MK, Garcia NK, Oh A, Zilberleyb I, Reichelt M, Austin CD, Tam C, Shriver S, Hu H, Labadie SS, Liang J, Wang L, Wang J, Lu Y, Purkey HE, Quinn J, Franke Y, Clark K, Beresini MH, Tan MW, Sellers BD, Maurer T, Koehler MFT, Wecksler AT, Kiefer JR, Verma V, Xu Y, Nishiyama M, Payandeh J, & Koth CM (2018). Structural basis for dual-mode inhibition of the ABC transporter MsbA. Nature 557 7704:196-201. PubMed Id: 29720648. doi:10.1038/s41586-018-0083-5.
*MsbA Lipid "flippase" in peptidiscs, conformation 1: Escherichia coli* B Bacteria, 4.2 Å** conformation 2, 4.4 Å: 6UZL	6UZ2	Data File Jmol Viewer 6UZ2 6UZL	Angiulli et al. (2020). Angiulli G, Dhupar HS, Suzuki H, Wason IS, Duong Van Hoa F, & Walz T (2020). New approach for membrane protein reconstitution into peptidiscs and basis for their adaptability to different proteins. Elife 9 :e53530. PubMed Id: 32125274. doi:10.7554/eLife.53530.
*MsbA Lipid "flippase" in Salipro with ADP vanadate: Escherichia coli* B Bacteria, 3.50 Å** cryo-EM structure	7BCW	Data File Jmol Viewer 7BCW	Kehlenbeck et al. (2021). Kehlenbeck DM, Traore DAK, Josts I, Sander S, Moulin M, Haertlein M, Prevost S, Forsyth VT, & Tidow H (2021). Cryo-EM structure of MsbA in saposin-lipid nanoparticles (Salipro) provides insights into nucleotide coordination. FEBS J . PubMed Id: 34921499. doi:10.1111/febs.16327.
*MsbA Lipid "flippase", open & inward facing state: Escherichia coli* B Bacteria, 3.90 Å** cryo-EM structure vanadate-trapped MsbA bound to KDL, 3.47 Å: 8DMM x-ray: N-terminal fragment of MsbA fused to GFP in complex with copper(II), 2.15 Å: 8DHY	8DMO	Data File Jmol Viewer 8DMO 8DMM 8DHY	Lyu et al. (2022). Lyu J, Liu C, Zhang T, Schrecke S, Elam NP, Packianathan C, Hochberg GKA, Russell D, Zhao M, & Laganowsky A (2022). Structural basis for lipid and copper regulation of the ABC transporter MsbA. Nat Commun 13 1:7291. PubMed Id: 36435815. doi:10.1038/s41467-022-34905-2.
*MsbA Lipid "flippase" in nano-discs, in complex with nanobodies, spin-labeled at position A60C: Escherichia coli* B Bacteria, 3.70 Å** cryo-EM structure AMP-PNP bound MsbA with nanobodies, spin-labeled at position A60C, 2.80 Å: 7PH3 spin-labeled at position T68C, 2.80 Å: 2.80 Å: 7PH4 in complex with nanobodies, spin-labeled at position T68C, 4.10 Å: 7PH7	7PH2	Data File Jmol Viewer 7PH2 7PH3 7PH7 7PH4	Galazzo et al. (2022). Galazzo L, Meier G, Januliene D, Parey K, De Vecchis D, Striednig B, Hilbi H, Schäfer LV, Kuprov I, Moeller A, Bordignon E, & Seeger MA (2022). The ABC transporter MsbA adopts the wide inward-open conformation in E. coli cells. Sci Adv 8 41:eabn6845. PubMed Id: 36223470. doi:10.1126/sciadv.abn6845.
*P-Glycoprotein multi-drug transporter (ABCB1): Mus musculus (mouse)* E Eukaryota (expressed in Pichia pastoris), 3.8 Å** With bound QZ59-RRR: 3G60, 4.40 Å With bound QZ59-SSS: 3G61, 4.35 Å	3G5U	Data File Jmol Viewer 3G5U 3G60 3G61	Aller et al. (2009). Aller SG, Yu J, Ward A, Weng Y, Chittaboina S, Zhuo R, Harrell PM, Trinh YT, Zhang Q, Urbatsch IL, & Chang G. (2009). Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding. Science 323 :1718-1722. PubMed Id: 19325113.
*P-Glycoprotein multi-drug transporter (ABCB1), refined structure: Mus musculus* E Eukaryota (expressed in Komagataella pastoris), 3.80 Å** Corrected Structure of Mouse P-glycoprotein bound to QZ59-RRR, 4.40 Å: 4M2S Corrected Structure of Mouse P-glycoprotein bound to QZ59-RRR, 4.35 Å: 4M2T	4M1M	Data File Jmol Viewer 4M1M 4M2S 4M2T	Li et al. (2014). Li J, Jaimes KF, & Aller SG (2014). Refined structures of mouse P-glycoprotein. Protein Sci. 23 :34-46. PubMed Id: 24155053. doi:10.1002/pro.2387.
*P-Glycoprotein multi-drug transporter (ABCB1): Mus musculus* E Eukaryota (expressed in Pichia pastoris), 3.40 Å** in complex with QZ-Ala, 3.78 Å: 4Q9I in complex with QZ-Val, 3.60 Å: 4Q9J in complex with QZ-Leu, 3.80 Å: 4Q9K in complex with QZ-Phe, 3.80 Å: 4Q9L	4Q9H	Data File Jmol Viewer 4Q9H 4Q9K 4Q9I 4Q9L 4Q9J	Szewczyk et al. (2015). Szewczyk P, Tao H, McGrath AP, Villaluz M, Rees SD, Lee SC, Doshi R, Urbatsch IL, Zhang Q, & Chang G (2015). Snapshots of ligand entry, malleable binding and induced helical movement in P-glycoprotein. Acta Crystallogr D Biol Crystallogr 71 :732-741. PubMed Id: 25760620. doi:10.1107/S1399004715000978.
*P-Glycoprotein multi-drug transporter (ABCB1) co-crystallized with BDE-100: Mus musculus* E Eukaryota (expressed in Komagataella pastoris), 3.50 Å**	4XWK	Data File Jmol Viewer 4XWK	Nicklisch et al. (2016). Nicklisch SC, Rees SD, McGrath AP, Gökirmak T, Bonito LT, Vermeer LM, Cregger C, Loewen G, Sandin S, Chang G, & Hamdoun A (2016). Global marine pollutants inhibit P-glycoprotein: Environmental levels, inhibitory effects, and cocrystal structure. Sci Adv 2 4. PubMed Id: 27152359. doi:10.1126/sciadv.1600001.
*P-Glycoprotein multi-drug transporter (ABCB1), mutant-C952A-with BDE100: Mus musculus* E Eukaryota (expressed in Komagataella pastoris), 3.98 Å** mutant-F979A and C952A-with BDE100, 3.98 Å: 6UJP mutant-F724A and C952A-with BDE100, 4.10 Å: 6UJR mutant-F728A and C952A-with BDE100, 4.17 Å: 6UJS mutant-Y303A and C952A-with BDE100, 4.17 Å: 6UJT mutant-Y306A and C952A-with BDE100, 4.15 Å: 6UJW	6UJN	Data File Jmol Viewer 6UJN 6UJS 6UJR 6UJW 6UJP 6UJT	Le et al. (2020). Le CA, Harvey DS, & Aller SG (2020). Structural definition of polyspecific compensatory ligand recognition by P-glycoprotein. IUCrJ 7 :663-672. PubMed Id: 32695413. doi:10.1107/S2052252520005709.
*P-Glycoprotein multi-drug transporter (ABCB1) in the presence of the CFTR potentiator ivacaftor: Mus musculus* E Eukaryota (expressed in Komagataella pastoris), 5.40 Å** cryo-EM structure P-glycoprotein in apo state, 4.20 Å 7OTI	7OTG	Data File Jmol Viewer 7OTG 7OTI	Barbieri et al. (2021). Barbieri A, Thonghin N, Shafi T, Prince SM, Collins RF, & Ford RC (2021). Structure of ABCB1/P-Glycoprotein in the Presence of the CFTR Potentiator Ivacaftor. Membranes (Basel) 11 12:923. PubMed Id: 34940424. doi:10.3390/membranes11120923.
*P-Glycoprotein multi-drug transporter (ABCB1) chimera, Zosuquidar/UIC2 Fab complex: Mus musculus & Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.58 Å** cryo-EM structure. Chimera: mouse ABCB1 background with human extracellular region. apo form of UIC2 Fab complex, 4.14 Å: 6FN4	6FN1	Data File Jmol Viewer 6FN1 6FN4	Alam et al. (2018). Alam A, Küng R, Kowal J, McLeod RA, Tremp N, Broude EV, Roninson IB, Stahlberg H, & Locher KP (2018). Structure of a zosuquidar and UIC2-bound human-mouse chimeric ABCB1. Proc Natl Acad Sci USA 115 9:E1973-E1982. PubMed Id: 29440498. doi:10.1073/pnas.1717044115.
*P-Glycoprotein multi-drug transporter (ABCB1), ATP-bound outward-facing conformation: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.4 Å** cryo-EM structure	6C0V	Data File Jmol Viewer 6C0V	Kim & Chen (2018). Kim Y, & Chen J (2018). Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation. Science 359 :915-919. PubMed Id: 29371429. doi:10.1126/science.aar7389.
*P-Glycoprotein multi-drug transporter (ABCB1) in nanodiscs, with bound taxol: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.5 Å** cryo-EM structure with bound zosuquidar, 3.86 Å: 6QEE	6QEX	Data File Jmol Viewer 6QEX 6QEE	Alam et al. (2019). Alam A, Kowal J, Broude E, Roninson I, & Locher KP (2019). Structural insight into substrate and inhibitor discrimination by human P-glycoprotein. Science 363 6428:753-756. PubMed Id: 30765569. doi:10.1126/science.aav7102.
*P-Glycoprotein multi-drug transporter (ABCB1) in nanodiscs: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.90 Å** cryo-EM structure in complex with vincristine, 3.20 Å: 7A69 in complex with tariquidar, 3.60 Å: 7A6E in complex with zosuquidar, 3.50 Å: 7A6F in complex with elacridar, 3.60 Å: 7A6C	7A65	Data File Jmol Viewer 7A65 7A69 7A6C 7A6E 7A6F	Nosol et al. (2020). Nosol K, Romane K, Irobalieva RN, Alam A, Kowal J, Fujita N, & Locher KP (2020). Cryo-EM structures reveal distinct mechanisms of inhibition of the human multidrug transporter ABCB1. Proc Natl Acad Sci U S A 117 42:26245-26253. PubMed Id: 33020312. doi:10.1073/pnas.2010264117.
*P-Glycoprotein multi-drug transporter (ABCB1) in complex with UIC2: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure	7O9W	Data File Jmol Viewer 7O9W	Urgaonkar et al. (2022). Urgaonkar S, Nosol K, Said AM, Nasief NN, Bu Y, Locher KP, Lau JYN, & Smolinski MP (2022). Discovery and Characterization of Potent Dual P-Glycoprotein and CYP3A4 Inhibitors: Design, Synthesis, Cryo-EM Analysis, and Biological Evaluations. J Med Chem 65 1:191-216. PubMed Id: 34928144. doi:10.1021/acs.jmedchem.1c01272.
*P-Glycoprotein multi-drug transporter (ABCB1): Caenorhabditis elegans* E Eukaryota (expressed in Pichia pastoris), 3.40 Å**	4F4C	Data File Jmol Viewer 4F4C	Jin et al. (2012). Jin MS, Oldham ML, Zhang Q, & Chen J (2012). Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans. Nature 490 :566-569. PubMed Id: 23000902. doi:10.1038/nature11448.
*P-Glycoprotein multi-drug transporter (ABCB1) homolog, inward facing state: Cyanidioschyzon merolae* E Eukaryota (expressed in Komagataella pastoris), 2.75 Å** G277V/A278V/A279V mutant, 2.60 Å: 3WMF G277V/A278V/A279V mutant in complex with an cyclic peptide inhibitor, aCAP, 2.40 Å: 3WMG	3WME	Data File Jmol Viewer 3WME 3WMG 3WMF	Kodan et al. (2014). Kodan A, Yamaguchi T, Nakatsu T, Sakiyama K, Hipolito CJ, Fujioka A, Hirokane R, Ikeguchi K, Watanabe B, Hiratake J, Kimura Y, Suga H, Ueda K, & Kato H (2014). Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog. Proc Natl Acad Sci USA 111 :4049-4054. PubMed Id: 24591620. doi:10.1073/pnas.1321562111.
*P-Glycoprotein multi-drug transporter (ABCB1) homolog with bound AMP-PNP-Mg²⁺, outward facing state: Cyanidioschyzon merolae* E Eukaryota (expressed in S. cerevisiae), 1.89 Å** apo state, inward facing, 2.70 Å: 6A6N	6A6M	Data File Jmol Viewer 6A6M 6A6N	Kodan et al. (2019). Kodan A, Yamaguchi T, Nakatsu T, Matsuoka K, Kimura Y, Ueda K, & Kato H (2019). Inward- and outward-facing X-ray crystal structures of homodimeric P-glycoprotein CmABCB1. Nat Commun 10 1. PubMed Id: 30622258. doi:10.1038/s41467-018-08007-x.
*MalFGK₂-MBP Maltose uptake transporter complex: Escherichia coli* B Bacteria, 2.8 Å** Complex includes maltose-binding protein (MBP), maltose, and ATP	2R6G	Data File Jmol Viewer 2R6G	Oldham et al. (2007). Oldham ML, Khare D, Quiocho FA, Davidson AL, & Chen J (2007). Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450 :515-521. PubMed Id: 18033289.
*MalFGK₂ uptake transporter: Escherichia coli* B Bacteria, 4.5 Å** Helix TM1 deleted. Shows transporter in the inward conformation in the resting state.	3FH6	Data File Jmol Viewer 3FH6	Khare et al. (2009). Khare D, Oldham ML, Orelle C, Davidson AL, & Chen J (2009). Alternating access in maltose transporter mediated by rigid-body rotations. Mol Cell 27 :528-536. PubMed Id: 19250913.
*MalFGK₂-MBP Maltose uptake transporter complex: Escherichia coli* B Bacteria, 3.10 Å** The structure shows the transporter in the pretranslocation (pre-T) state using a mutant maltose binding protein MBP_G69C/S337C that stabilizes the closed substrate-bound conformation. Complex with MBP_G69C/S337C and AMP-PNP, 2.9 Å: 3PUZ Complex with wt. MBP and AMP-PNP, 3.1 Å: 3PUY	3PV0	Data File Jmol Viewer 3PV0 3PUY 3PUZ	Oldham & Chen (2011). Oldham ML & Chen J (2011). Crystal structure of the maltose transporter in a pretranslocation intermediate State Science 332 :1202-1205. PubMed Id: 21566157. doi:10.1126/science.1200767.
*MalFGK₂-MBP Maltose uptake transporter complex with bound MgAMPPNP: Escherichia coli* B Bacteria, 2.20 Å** The protein is in the outward-facing conformation. With bound ADP-BeF₃, 2.30 Å: 3PUX With bound ADP-VO₄, 2.40 Å: 3PUV With bound ADP-AlF₄, 2.30 Å: 3PUW	3RLF	Data File Jmol Viewer 3RLF 3PUX 3PUV 3PUW	Oldham & Chen (2011). Oldham ML & Chen J (2011). Snapshots of the maltose transporter during ATP hydrolysis. Proc Natl Acad Sci USA 108 :15152-15156. PubMed Id: 21825153. doi:10.1073/pnas.1108858108.
*MalFGK₂ in complex with glucose-specific enzyme IIA: Escherichia coli* B Bacteria, 3.91 Å** The structure provides a structural framework for understanding carbon catabolite represion.	4JBW	Data File Jmol Viewer 4JBW	Chen et al. (2013). Chen S, Oldham ML, Davidson AL, & Chen J (2013). Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography. Nature 499 7458:364-368. PubMed Id: 23770568. doi:10.1038/nature12232.
*MalFGK₂-MBP Maltose uptake transporter complex; pre-translocation conformation bound to maltoheptaose : Escherichia coli* B Bacteria, 2.90 Å** Outward-facing conformation bound to maltohexaose, 2.38 Å: 4KI0	4KHZ	Data File Jmol Viewer 4KHZ 4KI0	Oldham et al. (2013). Oldham ML, Chen S, & Chen J (2013). Structural basis for substrate specificity in the Escherichia coli maltose transport system. Proc Natl Acad Sci USA 110 :18132-18137. PubMed Id: 24145421. doi:10.1073/pnas.1311407110.
*MetNI Methionine uptake transporter complex: Escherichia coli* B Bacteria, 3.7 Å** MetN-C2 domain 3DHX, 2.1 Å	3DHW	Data File Jmol Viewer 3DHW 3DHX	Kadaba et al. (2008). Kadaba NS, Kaiser JT, Johnson E, Lee A, & Rees DC (2008). The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation. Science 321 :250-253. PubMed Id: 18621668.
*MetNI methionine ABC transporter, inward facing conformation: Neisseria meningitidis* B Bacteria (expressed in E. coli), 3.30 Å** cryo-EM structure outward facing conformation in complex with lipo-MetQ, 6.40 Å: 7MBZ	7MC0	Data File Jmol Viewer 7MC0 7MBZ	Sharaf et al. (2021). Sharaf NG, Shahgholi M, Kim E, Lai JY, VanderVelde DG, Lee AT, & Rees DC (2021). Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction. Elife 10 :e69742. PubMed Id: 34409939. doi:10.7554/eLife.69742.
*FbpC ferric iron-uptake transporter nucleotide-binding domain: Neisseria gonorrhoeae* B Bacteria, 1.9 Å** A domain-swapped neucleotide-binding domain dimer	3FVQ	Data File Jmol Viewer 3FVQ	Newstead et al. (2009). Newstead S, Fowler PW, Bilton P, Carpenter EP, Sadler PJ, Campopiano DJ, Sansom MS, & Iwata S (2009). Insights into how nucleotide-binding domains power ABC transport. Structure 17 :1213-1222. PubMed Id: 19748342.
*Heterodimeric ABC exporter TM287-TM288: Thermotoga maritima* B Bacteria (expressed in E. coli), 2.90 Å** Protein is in the inward-facing conformation.	3QF4	Data File Jmol Viewer 3QF4	Hohl et al. (2012). Hohl M, Briand C, Grütter MG, & Seeger MA (2012). Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation. Nature Struc Mol Biol 19 :395-402. PubMed Id: 22447242. doi:10.1038/nsmb.2267.
*Heterodimeric ABC exporter TM287-TM288, apo form: Thermotoga maritima* B Bacteria (expressed in E. coli), 2.53 Å** with bound AMP-PNP, 2.60 Å: 4Q4A with cross-linked D-loops, 3.20 Å: 4Q4J	4Q4H	Data File Jmol Viewer 4Q4H 4Q4A 4Q4J	Hohl et al. (2014). Hohl M, Hürlimann LM, Böhm S, Schöppe J, Grütter MG, Bordignon E, & Seeger MA (2014). Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter. Proc Natl Acad Sci USA 111 :11025-11030. PubMed Id: 25030449. doi:10.1073/pnas.1400485111.
*Heterodimeric ABC exporter TM287-TM288, NBD287 domain: Thermotoga maritima* B Bacteria (expressed in E. coli), 1.80 Å** NBD288 domain, 2.35 Å: 4Q7L NBD288-Avi, 2.30 Å: 4Q7M	4Q7K	Data File Jmol Viewer 4Q7K 4Q7M 4Q7L	Bukowska et al. (2015). Bukowska MA, Hohl M, Geertsma ER, Hürlimann LM, Grütter MG, & Seeger MA (2015). A Transporter Motor Taken Apart: Flexibility in the Nucleotide Binding Domains of a Heterodimeric ABC Exporter. Biochemistry 54 :3086-3099. PubMed Id: 25947941. doi:10.1021/acs.biochem.5b00188.
*Heterodimeric ABC exporter TM287-TM288 (EtoA mutant) with bound ATPγS-Mg: Thermotoga maritima* B Bacteria (expressed in E. coli), 3.20 Å** 2xDtoA/EtoA mutant with bound ATP-Mg, 3.11 Å: 6QV0 2xDtoA/EtoA mutant with bound ATPγS-Mg, 3.48 Å: 6QV1 2xDtoA/EtoA mutant with bound ATPγS-Mg, 4.22 Å: 6QV2	6QUZ	Data File Jmol Viewer 6QUZ 6QV0 6QV2 6QV1	Hutter et al. (2019). Hutter CAJ, Timachi MH, Hürlimann LM, Zimmermann I, Egloff P, Göddeke H, Kucher S, Štefanić S, Karttunen M, Schäfer LV, Bordignon E, & Seeger MA (2019). The extracellular gate shapes the energy profile of an ABC exporter. Nat Commun 10 1:2260. PubMed Id: 31113958. doi:10.1038/s41467-019-09892-6.
*HmuUV heme transporter: Yersinia pestis* B Bacteria (expressed in E. coli), 3.00 Å**	4G1U	Data File Jmol Viewer 4G1U	Woo et al. (2012). Woo JS, Zeltina A, Goetz BA, & Locher KP (2012). X-ray structure of the Yersinia pestis heme transporter HmuUV Nature Struc Mol Biol 19 :1310-1314. PubMed Id: 23142986. doi:10.1038/nsmb.2417.
*ABCB6 Mitochondrial ABC transporter core domain: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.00 Å** cryo-EM structure complete structure with TMD0 domains, 5.20 Å: 7D7N	7D7R	Data File Jmol Viewer 7D7R 7D7N	Wang et al. (2020). Wang C, Cao C, Wang N, Wang X, Wang X, & Zhang XC (2020). Cryo-electron microscopy structure of human ABCB6 transporter. Protein Sci 29 12:2363-2374. PubMed Id: 33007128. doi:10.1002/pro.3960.
*ABCB6 Mitochondrial ABC transporter in a nanodisc, ATP-bound state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure apo state, 3.60 Å 7EKM	7EKL	Data File Jmol Viewer 7EKL 7EKM	Song et al. (2021). Song G, Zhang S, Tian M, Zhang L, Guo R, Zhuo W, & Yang M (2021). Molecular insights into the human ABCB6 transporter. Cell Discov 7 1:55. PubMed Id: 34312373. doi:10.1038/s41421-021-00284-z.
*ABCB6 Mitochondrial ABC transporter, coproporphyrin III-bound state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.40 Å** cryo-EM structure Hemin and GSH-bound state, 3.60 Å: 7DNZ	7DNY	Data File Jmol Viewer 7DNY 7DNZ	Kim et al. (2022). Kim S, Lee SS, Park JG, Kim JW, Ju S, Choi SH, Kim S, Kim NJ, Hong S, Kang JY, & Jin MS (2022). Structural Insights into Porphyrin Recognition by the Human ATP-Binding Cassette Transporter ABCB6. Mol Cells 45 8:575-587. PubMed Id: 35950458. doi:10.14348/molcells.2022.0040.
*ABCB7 Mitochondrial ABC transporter with bound AMP-PNP: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.30 Å** cryo-EM structure	7VGF	Data File Jmol Viewer 7VGF	Yan et al. (2022). Yan Q, Shen Y, & Yang X (2022). Cryo-EM structure of AMP-PNP-bound human mitochondrial ATP-binding cassette transporter ABCB7. J Struct Biol 214 1:107832. PubMed Id: 35041979. doi:10.1016/j.jsb.2022.107832.
*ABCB8 Mitochondrial ABC transporter in nucleotide binding state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 4.1 Å** cryo-EM structure	7EHL	Data File Jmol Viewer 7EHL	Li et al. (2021). Li S, Ren Y, Lu X, Shen Y, & Yang X (2021). Cryo-EM structure of human ABCB8 transporter in nucleotide binding state. Biochem Biophys Res Commun 557 :187-191. PubMed Id: 33872987. doi:10.1016/j.bbrc.2021.04.007.
*ABCB10 Mitochondrial ABC transporter with bound AMPPC: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.85 Å** Supersedes 2YL4. This is the first human ABC transporter and also the first mitochondrial ABC transporter. The protein conformation is open-inward (residues 152-738). Rod form B, 2.90 Å: 4AYX Plate form, 3.30 Å: 4AYW Nucleotide-free rod form, 2.85 Å: 3ZDQ	4AYT	Data File Jmol Viewer 4AYT 3ZDQ 4AYX 4AYW	Shintre et al. (2013). Shintre CA, Pike AC, Li Q, Kim JI, Barr AJ, Goubin S, Shrestha L, Yang J, Berridge G, Ross J, Stansfeld PJ, Sansom MS, Edwards AM, Bountra C, Marsden BD, von Delft F, Bullock AN, Gileadi O, Burgess-Brown NA, & Carpenter EP (2013). Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states. Proc Natl Acad Sci USA 110 :9710–9715. PubMed Id: 23716676. doi:10.1073/pnas.1217042110.
*ABCB10 Mitochondrial ABC transporter with bound biliverdin: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.58 Å** cryo-EM structure apo form, 3.67 Å: 7Y49	7Y48	Data File Jmol Viewer 7Y48 7Y49	Cao et al. (2023). Cao S, Yang Y, He L, Hang Y, Yan X, Shi H, Wu J, & Ouyang Z (2023). Cryo-EM structures of mitochondrial ABC transporter ABCB10 in apo and biliverdin-bound form. Nat Commun 14 1:2030. PubMed Id: 37041204. doi:10.1038/s41467-023-37851-9.
*Bile salt exporter ABCB11, apo form, inward-open conformation: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure	6LR0	Data File Jmol Viewer 6LR0	Wang et al. (2020). Wang L, Hou WT, Chen L, Jiang YL, Xu D, Sun L, Zhou CZ, & Chen Y (2020). Cryo-EM structure of human bile salts exporter ABCB11. Cell Res 30 7:623-625. PubMed Id: 32203132. doi:10.1038/s41422-020-0302-0.
*Bile salt exporter ABCB11 with two taurocholates bound: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.70 Å** cryo-EM structure with one taurocholate bound, 3.66 Å 7E1A	7DV5	Data File Jmol Viewer 7DV5 7E1A	Wang et al. (2022). Wang L, Hou WT, Wang J, Xu D, Guo C, Sun L, Ruan K, Zhou CZ, & Chen Y (2022). Structures of human bile acid exporter ABCB11 reveal a transport mechanism facilitated by two tandem substrate-binding pockets. Cell Res 32 5:501-504. PubMed Id: 35043010. doi:10.1038/s41422-021-00611-9.
*Bile salt exporter ABCB11 with bound inhibitor GBM in nanodiscs: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.22 Å** cryo-EM structure with bound vanadate, 2.81 Å: 8PMJ mutant E1244Q, with bound nucleotide, 2.95 Å: 8PMD	8PM6	Data File Jmol Viewer 8PM6 8PMD 8PMJ	Liu et al. (2023). Liu H, Irobalieva RN, Kowal J, Ni D, Nosol K, Bang-Sørensen R, Lancien L, Stahlberg H, Stieger B, & Locher KP (2023). Structural basis of bile salt extrusion and small-molecule inhibition in human BSEP. Nat Commun 14 1:7296. PubMed Id: 37949847. doi:10.1038/s41467-023-43109-1.
*Atm1-type ABC exporter, apo protein: Novosphingobium aromaticivorans* B Bacteria (expressed in E. coli), 2.50 Å** in complex with GSH, 2.50 Å: 4MRP in complex with selenomethionine, 2.97 Å: 4MRR in complex with GSSG, 2.34 Å: 4MRS in complex with GS-Hg, 2.50 Å: 4MRV	4MRN	Data File Jmol Viewer 4MRN 4MRR 4MRS 4MRV 4MRP	Lee et al. (2014). Lee JY, Yang JG, Zhitnitsky D, Lewinson O, & Rees DC (2014). Structural basis for heavy metal detoxification by an Atm1-type ABC exporter. Science 343 :1133-1136. PubMed Id: 24604198. doi:10.1126/science.1246489.
*Atm1-type ABC exporter with MgADP bound: Novosphingobium aromaticivorans* B Bacteria (expressed in E. coli), 3.70 Å** with ATP bound, 3.40 Å: 6PAN with ATP bound, 3.65 Å: 6PAO with ATP bound, 3.30 Å: 6PAQ with MgAMPPNP bound, 3.35 Å: 6PAR cryo-EM structure in nanodiscs with MgADPVO4 bound, 3.03 Å: 6VQT cryo-EM structure in nanodiscs, 3.88 Å: 6VQU	6PAM	Data File Jmol Viewer 6PAM 6PAQ 6VQU 6PAO 6PAN 6PAR 6VQT	Fan et al. (2020). Fan C, Kaiser JT, & Rees DC (2020). A structural framework for unidirectional transport by a bacterial ABC exporter. Proc Natl Acad Sci USA 117 32:19228-19236. PubMed Id: 32703810. doi:10.1073/pnas.2006526117.
*Atm1 mitochondrial ABC transporter, apo form: Saccharomyces cerevisiae* E Eukaryota (expressed in E. coli), 3.06 Å** in complex with GSH, 3.38 Å: 4MYH	4MYC	Data File Jmol Viewer 4MYC 4MYH	Srinivasan et al. (2014). Srinivasan V, Pierik AJ, & Lill R (2014). Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1. Science 343 :1137-1140. PubMed Id: 24604199. doi:10.1126/science.1246729.
*Atm1 mitochondrial ABC transporter in MSP1D1 nanodiscs, nucleotide-free state: Saccharomyces cerevisiae* E Eukaryota (expressed in E. coli), 3.30 Å** cryo-EM structure with bound AMP-PNP and Mg²⁺, 3.40 Å 7PSM in MSP1E3D1 nanodiscs with bound AMP-PNP and Mg²⁺, 2.90 Å 7PSN	7PSL	Data File Jmol Viewer 7PSL 7PSM 7PSN	Ellinghaus et al. (2021). Ellinghaus TL, Marcellino T, Srinivasan V, Lill R, & Kühlbrandt W (2021). Conformational changes in the yeast mitochondrial ABC transporter Atm1 during the transport cycle. Sci Adv 7 52:eabk2392. PubMed Id: 34936443. doi:10.1126/sciadv.abk2392.
*Atm3 mitochondrial ABC transporter, inward-facing conformation: Arabidopsis thaliana* E Eukaryota (expressed in E. coli), 3.40 Å** cryo-EM structure inward-facing conformation with bound GSSG, 3.60 Å 7N59 closed conformation, 3.95 Å 7N5A outward-facing conformation, 3.80 Å 7N5B	7N58	Data File Jmol Viewer 7N58 7N59 7N5A 7N5B	Fan & Rees (2022). Fan C, & Rees DC (2022). Glutathione binding to the plant AtAtm3 transporter and implications for the conformational coupling of ABC transporters. Elife 11 :e76140. PubMed Id: 35333177. doi:10.7554/eLife.76140.
*McjD antimicrobial peptide transporter: Escherichia coli* B Bacteria, 2.70 Å** Structure shows transporter in a novel outward occluded state	4PL0	Data File Jmol Viewer 4PL0	Choudhury et al. (2014). Choudhury HG, Tong Z, Mathavan I, Li Y, Iwata S, Zirah S, Rebuffat S, van Veen HW, & Beis K (2014). Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state. Proc Natl Acad Sci USA 111 :9145-9150. PubMed Id: 24920594. doi:10.1073/pnas.1320506111.
*McjD antimicrobial peptide transporter, high energy outward occluded intermediate state: Escherichia coli* B Bacteria, 3.4 Å** apo inward occluded conformation, 4.71 Å: 5OFP	5OFR	Data File Jmol Viewer 5OFR 5OFP	Bountra et al. (2017). Bountra K, Hagelueken G, Choudhury HG, Corradi V, El Omari K, Wagner A, Mathavan I, Zirah S, Yuan Wahlgren W, Tieleman DP, Schiemann O, Rebuffat S, & Beis K (2017). Structural basis for antibacterial peptide self-immunity by the bacterial ABC transporter McjD. EMBO J 36 :3062-3079. PubMed Id: 28864543. doi:10.15252/embj.201797278.
*McjD antimicrobial peptide transporter, native-SAD structure determined at wavelength 2.75 Å: Escherichia coli* B Bacteria, 2.80 Å** X-ray Structure	8PX9	Data File Jmol Viewer 8PX9	El Omari et al. (2023). El Omari K, Duman R, Mykhaylyk V, Orr CM, Latimer-Smith M, Winter G, Grama V, Qu F, Bountra K, Kwong HS, Romano M, Reis RI, Vogeley L, Vecchia L, Owen CD, Wittmann S, Renner M, Senda M, Matsugaki N, Kawano Y, Bowden TA, Moraes I, Grimes JM, Mancini EJ, Walsh MA, Guzzo CR, Owens RJ, Jones EY, Brown DG, Stuart DI, Beis K, & Wagner A (2023). Experimental phasing opportunities for macromolecular crystallography at very long wavelengths. Commun Chem 6 1:219. PubMed Id: 37828292. doi:10.1038/s42004-023-01014-0.
*Art(QN)₂ amino acid importer: Caldanaerobacter tengcongensis* B Bacteria (expressed in E. coli), 2.80 Å** in complex with Arg, 2.60 Å: 4YMT in complex with Arg & ATP, 2.50 Å: 4YMU in complex with ATP, 3.00 Å: 4YMV in complex with His, 2.80 Å: 4YMW ArtI binding protein in complex with Arg, 1.48 Å: 4YMX	4YMS	Data File Jmol Viewer 4YMS 4YMU 4YMX 4YMW 4YMT 4YMV	Yu et al. (2015). Yu J, Ge J, Heuveling J, Schneider E, & Yang M (2015). Structural basis for substrate specificity of an amino acid ABC transporter. Proc Natl Acad Sci USA 112 :5243-5248. PubMed Id: 25848002. doi:10.1073/pnas.1415037112.
*Peptidase-containing ABC transporter (PCAT1): Ruminiclostridium thermocellum* B Bacteria (expressed in E. coli), 3.61 Å** E648Q mutant with bound ATPγS, 5.51 Å: 4S0F	4RY2	Data File Jmol Viewer 4RY2 4S0F	Lin et al. (2015). Lin DY, Huang S, & Chen J (2015). Crystal structures of a polypeptide processing and secretion transporter. Nature 523 :425-430. PubMed Id: 26201595. doi:10.1038/nature14623.
*Peptidase-containing ABC transporter (PCAT1) bound to CtA peptide substrate: Hungateiclostridium thermocellum* B Bacteria (expressed in E. coli), 3.35 Å** cryo-EM structure	6V9Z	Data File Jmol Viewer 6V9Z	Kieuvongngam et al. (2020). Kieuvongngam V, Olinares PDB, Palillo A, Oldham ML, Chait BT, & Chen J (2020). Structural basis of substrate recognition by a polypeptide processing and secretion transporter. Elife 9 :e51492. PubMed Id: 31934861. doi:10.7554/eLife.51492.
*peptidase-containing ABC transporter PCAT1, outward facing conformation: Acetivibrio thermocellus* B Bacteria (expressed in E. coli), 4.50 Å** cryo-EM structure inward-facing wide conformation under ATP turnover, 4.10 Å 7T55 inward-facing intermediate conformation under ATP turnover, 3.70 Å 7T56 inward-facing narrow conformation under ATP turnover, 3.70 Å 7T57	7T54	Data File Jmol Viewer 7T54 7T55 7T56 7T57	Kieuvongngam & Chen (2022). Kieuvongngam V, & Chen J (2022). Structures of the peptidase-containing ABC transporter PCAT1 under equilibrium and nonequilibrium conditions. Proc Natl Acad Sci U S A 119 4:e2120534119. PubMed Id: 35074919. doi:10.1073/pnas.2120534119.
*Alginate transporter AlgM1M2SS with bound periplasmic protein AlgQ2: Sphingomonas sp.* B Bacteria (expressed in E. coli), 3.20 Å** AlgQ2-free structure, 4.50 Å: 4TQV	4TQU	Data File Jmol Viewer 4TQU 4TQV	Maruyama et al. (2015). Maruyama Y, Itoh T, Kaneko A, Nishitani Y, Mikami B, Hashimoto W, & Murata K (2015). Structure of a Bacterial ABC Transporter Involved in the Import of an Acidic Polysaccharide Alginate. Structure 23 9:1643-1654. PubMed Id: 26235029. doi:10.1016/j.str.2015.06.021.
*PglK lipid-linked oligosaccharide flippase, apo-inward structure 1: Campylobacter jejuni* B Bacteria (expressed in E. coli), 2.90 Å** apo-inward structure 2, 3.94 Å: 5C76 outward-occluded conformation, 5.90 Å: 5C73	5C78	Data File Jmol Viewer 5C78 5C73 5C76	Perez et al. (2015). Perez C, Gerber S, Boilevin J, Bucher M, Darbre T, Aebi M, Reymond JL, & Locher KP (2015). Structure and mechanism of an active lipid-linked oligosaccharide flippase. Nature 524 :433-438. PubMed Id: 26266984. doi:10.1038/nature14953.
*PglK lipid-linked oligosaccharide flippase, outward facing with bound ATPγS: Campylobacter jejuni* B Bacteria (expressed in E. coli), 3.3 Å**	6HRC	Data File Jmol Viewer 6HRC	Perez et al. (2019). Perez C, Mehdipour AR, Hummer G, & Locher KP (2019). Structure of Outward-Facing PglK and Molecular Dynamics of Lipid-Linked Oligosaccharide Recognition and Translocation. Structure 27 4:669-678.e5. PubMed Id: 30799077. doi:10.1016/j.str.2019.01.013.
*O-antigen polysaccharide ABC-transporter, Wzm-WztN homolog in an open conformation: Aquifex aeolicus* B Bacteria (expressed in E. coli), 3.85 Å** nucleotide binding domain WztN, 2.05 Å: 6AMX nucleotide binding domain dimer, 3.51 Å: 6AN5	6AN7	Data File Jmol Viewer 6AN7 6AN5 6AMX	Bi et al. (2018). Bi Y, Mann E, Whitfield C, & Zimmer J (2018). Architecture of a channel-forming O-antigen polysaccharide ABC transporter. Nature 553 :361-365. PubMed Id: 29320481. doi:10.1038/nature25190.
*O-antigen polysaccharide ABC-transporter, Wzm-WztN homolog, ATP-bound conformation: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.05 Å**	6M96	Data File Jmol Viewer 6M96	Caffalette et al. (2019). Caffalette CA, Corey RA, Sansom MSP, Stansfeld PJ, & Zimmer J (2019). A lipid gating mechanism for the channel-forming O antigen ABC transporter. Nat Commun 10 1. PubMed Id: 30778065. doi:10.1038/s41467-019-08646-8.
*O-antigen polysaccharide ABC-transporter carbohydrate-binding domain: Aquifex aeolicus* B Bacteria (expressed in E. coli), 2.65 Å**	6O14	Data File Jmol Viewer 6O14	Bi & Zimmer (2020). Bi Y, & Zimmer J (2020). Structure and Ligand-Binding Properties of the O Antigen ABC Transporter Carbohydrate-Binding Domain. Structure 28 2:252-258.e2. PubMed Id: 31879128. doi:10.1016/j.str.2019.11.020.
*O-antigen polysaccharide ABC-transporter Wzm-WztN bound to ATP, full length in nanodiscs: Aquifex aeolicus* B Bacteria (expressed in E. coli), 3.60 Å** cryo-EM structure	7K2T	Data File Jmol Viewer 7K2T	Caffalette & Zimmer (2021). Caffalette CA, & Zimmer J (2021). Cryo-EM structure of the full-length WzmWzt ABC transporter required for lipid-linked O antigen transport. Proc Natl Acad Sci U S A 118 1. PubMed Id: 33443152. doi:10.1073/pnas.2016144118.
*O-antigen polysaccharide Wzm-Wzt ABC-transporter, bound to the native O antigen: Aquifex aeolicus* B Bacteria (expressed in E. coli), 3.20 Å** cryo-EM structure ADP-bound, 3.54 Å: 8DOU bound to 3-O-methyl-D-mannose, 3.70 Å: 8DN8 bound to the native O antigen and ADP, 3.30 Å: 8DNC bound to ATP, 3.50 Å: 8DNE DDM-solubilized and nucleotide-free, 4.10 Å: 8DL0 x-ray: Carbohydrate Binding Domain bound to 3-O-methyl-D-mannose, 1.61 Å: 8DKY	8DKU	Data File Jmol Viewer 8DKU 8DL0 8DN8 8DNC 8DOU 8DNE 8DKY	Spellmon et al. (2022). Spellmon N, Muszyński A, Górniak I, Vlach J, Hahn D, Azadi P, & Zimmer J (2022). Molecular basis for polysaccharide recognition and modulated ATP hydrolysis by the O antigen ABC transporter. Nat Commun 13 1:5226. PubMed Id: 36064941. doi:10.1038/s41467-022-32597-2.
*ABCB4 phosphatidylcholine transporter: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.2 Å** cryo-EM structure	6SP7	Data File Jmol Viewer 6SP7	Olsen et al. (2020). Olsen JA, Alam A, Kowal J, Stieger B, & Locher KP (2020). Structure of the human lipid exporter ABCB4 in a lipid environment. Nat Struct Mol Biol 27 1:62-70. PubMed Id: 31873305. doi:10.1038/s41594-019-0354-3.
*ABCB4 (MDR3) phospholipid transporter, apo-inward-open conformation: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.20 Å** cryo-EM structure phosphatidylcholine-bound, occluded conformation, 3.60 Å 7NIV posaconazole-bound, inward-open conformation, 3.80 Å 7NIW	7NIU	Data File Jmol Viewer 7NIU 7NIV 7NIW	Nosol et al. (2021). Nosol K, Bang-Sørensen R, Irobalieva RN, Erramilli SK, Stieger B, Kossiakoff AA, & Locher KP (2021). Structures of ABCB4 provide insight into phosphatidylcholine translocation. Proc Natl Acad Sci U S A 118 33:e2106702118. PubMed Id: 34385322. doi:10.1073/pnas.2106702118.
*peroxisomal fatty acid transporter ABCD1, oleoyl-CoA-bound: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure ATP-bound, 3.14 Å 7SHM	7SHN	Data File Jmol Viewer 7SHN 7SHM	Wang et al. (2021). Wang R, Qin Y, & Li X (2021). Structural basis of acyl-CoA transport across the peroxisomal membrane by human ABCD1. Cell Res . PubMed Id: 34754073. doi:10.1038/s41422-021-00585-8.
*peroxisomal fatty acid transporter ABCD1, nucleotide bound, outward open conformation: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure inward open conformation, 4.40 Å: 7RRA	7RR9	Data File Jmol Viewer 7RR9 7RRA	Le et al. (2022). Le LTM, Thompson JR, Dang PX, Bhandari J, & Alam A (2022). Structures of the human peroxisomal fatty acid transporter ABCD1 in a lipid environment. Commun Biol 5 1. PubMed Id: 35013584. doi:10.1038/s42003-021-02970-w.
*peroxisomal fatty acid transporter ABCD1: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.53 Å** cryo-EM structure C22:0-CoA bound, 3.59 Å: 7VZB ATP-bound, 2.80 Å: 7VX8	7VWC	Data File Jmol Viewer 7VWC 7VX8 7VZB	Chen et al. (2022). Chen ZP, Xu D, Wang L, Mao YX, Li Y, Cheng MT, Zhou CZ, Hou WT, & Chen Y (2022). Structural basis of substrate recognition and translocation by human very long-chain fatty acid transporter ABCD1. Nat Commun 13 1:3299. PubMed Id: 35676282. doi:10.1038/s41467-022-30974-5.
*peroxisomal fatty acid transporter ABCD1, also known as adrenoleukodystrophy protein (ALDP), C26:0 bound: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.78 Å** cryo-EM structure E630Q mutant, C26:0-CoA and ATP bound, 3.30 Å: 7X0T E630Q mutant, ATP bound, inward-facing state 2, 3.34 Å: 7XEC E630Q mutant, ATP and Magnesium bound, outward-facing state, 2.96 Å: 7X0Z E630Q mutant, ATP bound, inward-facing state, 3.30 Å: 7X1W	7X07	Data File Jmol Viewer 7X07 7X1W 7X0Z 7X0T 7XEC	Xiong et al. (2023). Xiong C, Jia LN, Xiong WX, Wu XT, Xiong LL, Wang TH, Zhou D, Hong Z, Liu Z, & Tang L (2023). Structural insights into substrate recognition and translocation of human peroxisomal ABC transporter ALDP. Signal Transduct Target Ther 8 1:74. PubMed Id: 36810450. doi:10.1038/s41392-022-01280-9.
*lysosomal cobalamin exporter ABCD4: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure	6JBJ	Data File Jmol Viewer 6JBJ	Xu et al. (2019). Xu D, Feng Z, Hou WT, Jiang YL, Wang L, Sun L, Zhou CZ, & Chen Y (2019). Cryo-EM structure of human lysosomal cobalamin exporter ABCD4. Cell Res 29 12:1039-1041. PubMed Id: 31467407. doi:10.1038/s41422-019-0222-z.
*ABCG1 cholesterol transporter: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.00 Å** cryo-EM structure	7OZ1	Data File Jmol Viewer 7OZ1	Skarda et al. (2021). Skarda L, Kowal J, & Locher KP (2021). Structure of the Human Cholesterol Transporter ABCG1. J Mol Biol 433 21:167218. PubMed Id: 34461069. doi:10.1016/j.jmb.2021.167218.
*ABCG1 cholesterol transporter: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.70 Å** cryo-EM structure E242Q mutant with cholesterol, 3.20 Å 7R8D E242Q mutant complexed with ATP, 3.70 Å 7R8E	7R8C	Data File Jmol Viewer 7R8C 7R8E 7R8D	Sun et al. (2021). Sun Y, Wang J, Long T, Qi X, Donnelly L, Elghobashi-Meinhardt N, Esparza L, Cohen JC, Xie XS, Hobbs HH, & Li X (2021). Molecular basis of cholesterol efflux via ABCG subfamily transporters. Proc Natl Acad Sci U S A 118 34:e2110483118. PubMed Id: 34404721. doi:10.1073/pnas.2110483118.
*ABCG1 cholesterol transporter in complex with cholesterol: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.26 Å** cryo-EM structure	7FDV	Data File Jmol Viewer 7FDV	Xu et al. (2022). Xu D, Li Y, Yang F, Sun CR, Pan J, Wang L, Chen ZP, Fang SC, Yao X, Hou WT, Zhou CZ, & Chen Y (2022). Structure and transport mechanism of the human cholesterol transporter ABCG1. Cell Rep 38 4. PubMed Id: 35081353. doi:10.1016/j.celrep.2022.110298.
*ABCG5/ABCG8 sterol transporter: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 3.93 Å**	5DO7	Data File Jmol Viewer 5DO7	Lee et al. (2016). Lee JY, Kinch LN, Borek DM, Wang J, Wang J, Urbatsch IL, Xie XS, Grishin NV, Cohen JC, Otwinowski Z, Hobbs HH, & Rosenbaum DM (2016). Crystal structure of the human sterol transporter ABCG5/ABCG8. Nature 533 :561-564. PubMed Id: 27144356. doi:10.1038/nature17666.
*ABCG5/ABCG8 sterol transporter purified from mammalian cells: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure ABCG5-I529W/ABCG8-WT, 3.50 Å 7R88 ABCG5-WT/ABCG8-I419E, 3.40 Å 7R87 Purified from Komagataella pastoris: ABCG5/ABCG8 wild type, 2.60 Å 7R89 ABCG5/ABCG8 supplemented with cholesterol, 3.10 Å 7R8B	7R8A	Data File Jmol Viewer 7R8A 7R87 7R88 7R8B 7R89	Sun et al. (2021). Sun Y, Wang J, Long T, Qi X, Donnelly L, Elghobashi-Meinhardt N, Esparza L, Cohen JC, Xie XS, Hobbs HH, & Li X (2021). Molecular basis of cholesterol efflux via ABCG subfamily transporters. Proc Natl Acad Sci U S A 118 34:e2110483118. PubMed Id: 34404721. doi:10.1073/pnas.2110483118.
*ABCG5/ABCG8 sterol transporter in complex with cholesterol: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 4.05 Å**	8CUB	Data File Jmol Viewer 8CUB	Farhat et al. (2022). Farhat D, Rezaei F, Ristovski M, Yang Y, Stancescu A, Dzimkova L, Samnani S, Couture JF, & Lee JY (2022). Structural Analysis of Cholesterol Binding and Sterol Selectivity by ABCG5/G8. J Mol Biol 434 20:167795. PubMed Id: 35988751. doi:10.1016/j.jmb.2022.167795.
*BhuU/BhuV haem importer, inward facing: Burkholderia cenocepacia* B Bacteria (expressed in E. coli), 2.8 Å** in complex with periplasmic heme binding protein BhuT, 3.21 Å: 5B58	5B57	Data File Jmol Viewer 5B57 5B58	Naoe et al. (2016). Naoe Y, Nakamura N, Doi A, Sawabe M, Nakamura H, Shiro Y, & Sugimoto H (2016). Crystal structure of bacterial haem importer complex in the inward-facing conformation. Nat Commun 7 :13411. PubMed Id: 27830695. doi:10.1038/ncomms13411.
*Cystic Fibrosis Transmembrane Conductance Regulator (CFTR): Danio rerio* E Eukaryota (expressed in Sf9 cells), 3.73 Å** Cryo-EM structure	5TSI	Data File Jmol Viewer 5TSI	Zhang & Chen (2016). Zhang Z, & Chen J (2016). Atomic Structure of the Cystic Fibrosis Transmembrane Conductance Regulator. Cell 167 :1586-1597.e9. PubMed Id: 27912062. doi:10.1016/j.cell.2016.11.014.
*Cystic Fibrosis Transmembrane Conductance Regulator (CFTR), phosphorylated, ATP-bound state: Danio rerio* E Eukaryota (expressed in HEK293S), 3.37 Å** cryo-EM structure	5W81	Data File Jmol Viewer 5W81	Zhang et al. (2017). Zhang Z, Liu F, & Chen J (2017). Conformational Changes of CFTR upon Phosphorylation and ATP Binding. Cell 170 :483-491.e8. PubMed Id: 28735752. doi:10.1016/j.cell.2017.06.041.
*Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) in dephosphorylated, ATP-free state: Homo sapiens* E Eukaryota (expressed in HEK293S cells), 3.87 Å** cryo-EM structure	5UAK	Data File Jmol Viewer 5UAK	Liu et al. (2017). Liu F, Zhang Z, Csanády L, Gadsby DC, & Chen J (2017). Molecular Structure of the Human CFTR Ion Channel. Cell 169 1:85-95.e8. PubMed Id: 28340353. doi:10.1016/j.cell.2017.02.024.
*Cystic Fibrosis Transmembrane Conductance Regulator (CFTR), ATP-bound and phosphorylated: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.2 Å** cryo-EM structure	6MSM	Data File Jmol Viewer 6MSM	Zhang et al. (2018). Zhang Z, Liu F, & Chen J (2018). Molecular structure of the ATP-bound, phosphorylated human CFTR. Proc Natl Acad Sci USA 115 50:12757-12762. PubMed Id: 30459277. doi:10.1073/pnas.1815287115.
*Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) with bound ivacaftor: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.3 Å** cryo-EM structure in complex with GLPG1837, 3.2 Å: 6O1V	6O2P	Data File Jmol Viewer 6O2P 6O1V	Liu et al. (2019). Liu F, Zhang Z, Levit A, Levring J, Touhara KK, Shoichet BK, & Chen J (2019). Structural identification of a hotspot on CFTR for potentiation. Science 364 6446:1184-1188. PubMed Id: 31221859. doi:10.1126/science.aaw7611.
*Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) phosphorylated & with ATP/Mg and Lumacaftor (VX-809): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.70 Å** cryo-EM structure with ATP/Mg and Tezacaftor (VX-661), 3.80 Å 7SV7 dephosphorylated & Lumacaftor (VX-809), 7SVR	7SVD	Data File Jmol Viewer 7SVD 7SV7 7SVR	Fiedorczuk & Chen (2022). Fiedorczuk K, & Chen J (2022). Mechanism of CFTR correction by type I folding correctors. Cell 185 1:158-168.e11. PubMed Id: 34995514. doi:10.1016/j.cell.2021.12.009.
*ΔF508 cystic fibrosis transmembrane conductance regulator (CFTR), dephosphorylated: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 6.90 Å** cryo-EM structure phosphorylated with elexacaftor (VX-445) and ATP/Mg, 3.60 Å: 8EIG phosphorylated with elexacaftor (VX-445), lumacaftor (VX-809), and ATP/Mg, 2.80 Å: 8EIO phosphorylated with Trikafta [elexacaftor (VX-445), tezacaftor (VX-661), ivacaftor (VX-770)], and ATP/Mg, 3.00 Å: 8EIQ	8EJ1	Data File Jmol Viewer 8EJ1 8EIO 8EIQ 8EIG	Fiedorczuk & Chen (2022). Fiedorczuk K, & Chen J (2022). Molecular structures reveal synergistic rescue of Δ508 CFTR by Trikafta modulators. Science 378 6617:284-290. PubMed Id: 36264792. doi:10.1126/science.ade2216.
*Cystic Fibrosis Transmembrane Conductance Regulator (CFTR), dephosphorylated, ATP-bound state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.30 Å** cryo-EM structure	8FZQ	Data File Jmol Viewer 8FZQ	Levring et al. (2023). Levring J, Terry DS, Kilic Z, Fitzgerald G, Blanchard S, & Chen J (2023). CFTR function, pathology and pharmacology at single-molecule resolution. Nature 616 7957:606-614. PubMed Id: 36949202. doi:10.1038/s41586-023-05854-7.
*Cystic Fibrosis Transmembrane Conductance Regulator (CFTR), dephosphorylated form: Gallus gallus* E Eukaryota (expressed in BHK cells), 4.3 Å** cryo-EM structure phosphorylated form, 6.6 Å: 6D3S	6D3R	Data File Jmol Viewer 6D3R 6D3S	Fay et al. (2018). Fay JF, Aleksandrov LA, Jensen TJ, Cui LL, Kousouros JN, He L, Aleksandrov AA, Gingerich DS, Riordan JR, & Chen JZ (2018). Cryo-EM Visualization of an Active High Open Probability CFTR Anion Channel. Biochemistry 57 43:6234-6246. PubMed Id: 30281975. doi:10.1021/acs.biochem.8b00763.
*Transporter associated with antigen processing (TAP) bound to ICP47: Homo sapiens* E Eukaryota (expressed in Pichia pastoris), 4.0 Å** cryo-EM structure	5U1D	Data File Jmol Viewer 5U1D	Oldham et al. (2016). Oldham ML, Grigorieff N, & Chen J (2016). Structure of the transporter associated with antigen processing trapped by herpes simplex virus. Elife 5 :e21829. PubMed Id: 27935481. doi:10.7554/eLife.21829.
*Transporter associated with antigen processing (TAP-like or ABCB9), PG bound: Mus musculus* E Eukaryota (expressed in Trichoplusia ni), 3.40 Å** cryo-EM structure with bound 9mer-peptide, 3.98 Å: 7VFI with bound ADP.BeF3, 3.20 Å: 7V5C	7V5D	Data File Jmol Viewer 7V5D 7VFI 7V5C	Park et al. (2022). Park JG, Kim S, Jang E, Choi SH, Han H, Ju S, Kim JW, Min DS, & Jin MS (2022). The lysosomal transporter TAPL has a dual role as peptide translocator and phosphatidylserine floppase. Nat Commun 13 1:5851. PubMed Id: 36195619. doi:10.1038/s41467-022-33593-2.
*TmrAB antigen transporter homolog: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.7 Å**	5MKK	Data File Jmol Viewer 5MKK	Nöll et al. (2017). Nöll A, Thomas C, Herbring V, Zollmann T, Barth K, Mehdipour AR, Tomasiak TM, Büchert S, Joseph B, Abele R, Oliéric V, Wang M, Diederichs K, Hummer G, Stroud RM, Pos KM, & Tampé R (2017). Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP. Proc Natl Aca. Sci USA 114 :E438-E447. PubMed Id: 28069938. doi:10.1073/pnas.1620009114.
*TmrAB antigen transporter homolog under turnover conditions, inward-facing narrow conformation: Thermus thermophilus* B Bacteria (expressed in E. coli), 3.8 Å** cryo-EM structure Download video of conformational transitions: Nature Magazine inward-facing wide conformation, 4.2 Å: 6RAG ATP-bound outward-facing open conformation, 2.8 Å: 6RAH ATP-bound outward-facing occluded conformation, 2.9 Å: 6RAI in vanadate trapped outward-facing open conformation, 3.5 Å: 6RAJ in vanadate trapped outward-facing occluded conformation, 3.3 Å: 6RAK in asymmetric unlocked return conformation, 3.5 Å: 6RAL in asymmetric unlocked return conformation with wider opened intracellular gate, 3.8 Å: 6RAM in inward-facing wide conformation, 4.2 Å: 6RAN	6RAF	Data File Jmol Viewer 6RAF 6RAL 6RAN 6RAM 6RAK 6RAH 6RAJ 6RAI 6RAG	Hofmann et al. (2019). Hofmann S, Januliene D, Mehdipour AR, Thomas C, Stefan E, Brüchert S, Kuhn BT, Geertsma ER, Hummer G, Tampé R, & Moeller A (2019). Conformation space of a heterodimeric ABC exporter under turnover conditions. Nature 571 7766:580-583. PubMed Id: 31316210. doi:10.1038/s41586-019-1391-0.
*PrtD Type-1 secretion system ABC transporter: Aquifex aeolicus* B Bacteria (expressed in E. coli), 3.15 Å**	5L22	Data File Jmol Viewer 5L22	Morgan et al. (2017). Morgan JL, Acheson JF, & Zimmer J (2017). Structure of a Type-1 Secretion System ABC Transporter. Structure 25 :522-529. PubMed Id: 28216041. doi:10.1016/j.str.2017.01.010.
*MRP1 Multidrug resistance protein 1: Bos taurus* E Eukaryota (expressed in S. frugiperda), 3.49 Å** cryo-EM structure with bound LTC₄, 3.34 Å: 5UJA	5UJ9	Data File Jmol Viewer 5UJ9 5UJA	Johnson & Chen (2017). Johnson ZL, & Chen J (2017). Structural Basis of Substrate Recognition by the Multidrug Resistance Protein MRP1. Cell 168 :1075-1085. PubMed Id: 28238471. doi:10.1016/j.cell.2017.01.041.
*MRP1 Multidrug resistance protein 1, ATP-bound form: Bos taurus* E Eukaryota (expressed in HEK293S cells), 3.14 Å** cryo-EM structure	6BHU	Data File Jmol Viewer 6BHU	Johnson & Chen (2018). Johnson ZL, & Chen J (2018). ATP Binding Enables Substrate Release from Multidrug Resistance Protein 1. Cell 172 :81-89.e10. PubMed Id: 29290467. doi:10.1016/j.cell.2017.12.005.
*MRP1 Multidrug resistance protein 1 under active turnover conditions: Bos taurus* E Eukaryota (expressed in HEK293 cells), 3.23 Å** cryo-EM structure	6UY0	Data File Jmol Viewer 6UY0	Wang et al. (2020). Wang L, Johnson ZL, Wasserman MR, Levring J, Chen J, & Liu S (2020). Characterization of the kinetic cycle of an ABC transporter by single-molecule and cryo-EM analyses. Elife 9 :e56451. PubMed Id: 32458799. doi:10.7554/eLife.56451.
*MRP1 Multidrug resistance protein 1 with bound cyclic peptide inhibitor 1 (CPI1): Bos taurus* E Eukaryota (expressed in HEK293 cells), 3.27 Å** cryo-EM structure	8F4B	Data File Jmol Viewer 8F4B	Pietz et al. (2023). Pietz HL, Abbas A, Johnson ZL, Oldham ML, Suga H, & Chen J (2023). A macrocyclic peptide inhibitor traps MRP1 in a catalytically incompetent conformation. Proc Natl Acad Sci U S A 120 11:e2220012120. PubMed Id: 36893260. doi:10.1073/pnas.2220012120.
*cadmium factor 1 protein (cf1p) homolog of multidrug resistance protein 1 (MRP1): Saccharomyces cerevisiae* E Eukaryota, 3.20 Å** cryo-EM structure	7MPE	Data File Jmol Viewer 7MPE	Bickers et al. (2021). Bickers SC, Benlekbir S, Rubinstein JL, & Kanelis V (2021). Structure of Ycf1p reveals the transmembrane domain TMD0 and the regulatory region of ABCC transporters. Proc Natl Acad Sci U S A 118 21:e2025853118. PubMed Id: 34021087. doi:10.1073/pnas.2025853118.
*cadmium factor 1 protein (cf1p) homolog of multidrug resistance protein 1 (MRP1), E1435Q mutant in inward-facing narrow conformation: Saccharomyces cerevisiae* E Eukaryota, 4.04 Å** cryo-EM structure inward-facing wide conformation, 3.42 Å 7M69	7M68	Data File Jmol Viewer 7M68 7M69	Khandelwal et al. (2022). Khandelwal NK, Millan CR, Zangari SI, Avila S, Williams D, Thaker TM, & Tomasiak TM (2022). The structural basis for regulation of the glutathione transporter Ycf1 by regulatory domain phosphorylation. Nat Commun 13 1:1278. PubMed Id: 35277487. doi:10.1038/s41467-022-28811-w.
*Lipopolysaccharide transporter complex LptB₂FG (nucleotide free): Pseudomonas aeruginosa* B Bacteria (expressed in E. coli), 3.46 Å**	5X5Y	Data File Jmol Viewer 5X5Y	Luo et al. (2017). Luo Q, Yang X, Yu S, Shi H, Wang K, Xiao L, Zhu G, Sun C, Li T, Li D, Zhang X, Zhou M, & Huang Y (2017). Structural basis for lipopolysaccharide extraction by ABC transporter LptB2FG. Nat Struct Mol Biol 24 :469-474. PubMed Id: 28394325. doi:10.1038/nsmb.3399.
*Lipopolysaccharide transporter complex LptB₂FGC, nucleotide free: Escherichia coli* B Bacteria, 4.2 Å** cryo-EM structure LptB₂FGC, vanadate trapped, 4.3 Å: 6MI8 LptB₂FG; nucleotide free, 4 Å: 6MHU LptB₂FG; vanadate trapped, 4.1 Å: 6MHZ	6MI7	Data File Jmol Viewer 6MI7 6MI8 6MHZ 6MHU	Li et al. (2019). Li Y, Orlando BJ, & Liao M (2019). Structural basis of lipopolysaccharide extraction by the LptB₂FGC complex. Nature 567 7749:486-490. PubMed Id: 30894744. doi:10.1038/s41586-019-1025-6.
*Lipopolysaccharide transporter complex LptB₂FGC: Enterobacter cloacae* B Bacteria (expressed in E. coli), 3.2 Å**	6MIT	Data File Jmol Viewer 6MIT	Owens et al. (2019). Owens TW, Taylor RJ, Pahil KS, Bertani BR, Ruiz N, Kruse AC, & Kahne D (2019). Structural basis of unidirectional export of lipopolysaccharide to the cell surface. Nature 567 7749:550-553. PubMed Id: 30894747. doi:10.1038/s41586-019-1039-0.
*Lipopolysaccharide transporter complex LptB₂FGC: Vibrio cholerae* B Bacteria (expressed in E.coli), 2.85 Å**	6MJP	Data File Jmol Viewer 6MJP	Owens et al. (2019). Owens TW, Taylor RJ, Pahil KS, Bertani BR, Ruiz N, Kruse AC, & Kahne D (2019). Structural basis of unidirectional export of lipopolysaccharide to the cell surface. Nature 567 7749:550-553. PubMed Id: 30894747. doi:10.1038/s41586-019-1039-0.
*Lipopolysaccharide transporter complex LptB₂FGC in complex with lipopolysaccharide:: Shigella flexneri* B Bacteria (expressed in E. coli), 3.1 Å** cryo-EM structure in complex with LPS, 3.7 Å: 6S8H in complex with AMP-PNP, 3.5 Å: 6S8G	6S8N	Data File Jmol Viewer 6S8N 6S8G 6S8H	Tang et al. (2019). Tang X, Chang S, Luo Q, Zhang Z, Qiao W, Xu C, Zhang C, Niu Y, Yang W, Wang T, Zhang Z, Zhu X, Wei X, Dong C, Zhang X, & Dong H (2019). Cryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism. Nat Commun 10 1. PubMed Id: 31519889. doi:10.1038/s41467-019-11977-1.
*Lipopolysaccharide transporter LptB₂FGC in complex with LPS: Klebsiella pneumoniae* B Bacteria (expressed in E. coli), 3.85 Å** cryo-EM structure	7EFO	Data File Jmol Viewer 7EFO	Luo et al. (2021). Luo Q, Shi H, & Xu X (2021). Cryo-EM structures of LptB₂FG and LptB₂FGC from Klebsiella pneumoniae in complex with lipopolysaccharide. Biochem Biophys Res Commun 571 :20-25. PubMed Id: 34303191. doi:10.1016/j.bbrc.2021.07.049.
*Multidrug transporter ABCG2: Homo sapiens* E Eukaryota (expressed in HEK293), 3.78 Å** cryo-EM structure de novo built TMD in complex with 5D4-fab variable domain, 3.78 Å: 5NJG	5NJ3	Data File Jmol Viewer 5NJ3 5NJG	Taylor et al. (2017). Taylor NMI, Manolaridis I, Jackson SM, Kowal J, Stahlberg H, & Locher KP (2017). Structure of the human multidrug transporter ABCG2. Nature 546 :504-509. PubMed Id: 28554189. doi:10.1038/nature22345.
*Multidrug transporter ABCG2 with bound inhibitor MZ29 and 5D3-Fab variable domain: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.1 Å** cryo-EM structure with bound MZ29 only, 3.56 Å: 6FFC with bound inhibitor MB136 and and 5D3-Fab variable domain, 3.6 Å: 6FEQ	6ETI	Data File Jmol Viewer 6ETI 6FFC 6FEQ	Jackson et al. (2018). Jackson SM, Manolaridis I, Kowal J, Zechner M, Taylor NMI, Bause M, Bauer S, Bartholomaeus R, Bernhardt G, Koenig B, Buschauer A, Stahlberg H, Altmann KH, & Locher KP (2018). Structural basis of small-molecule inhibition of human multidrug transporter ABCG2. Nat Struct Mol Biol 25 4:333-340. PubMed Id: 29610494. doi:10.1038/s41594-018-0049-1.
*Multidrug transporter ABCG2 E211Q mutant with bound substrate estrone 3-sulfate: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.58 Å** cryo-EM structure E211Q mutant bound to ATP and Magnesium, 3.09 Å: 6HBU	6HCO	Data File Jmol Viewer 6HCO 6HBU	Manolaridis et al. (2018). Manolaridis I, Jackson SM, Taylor NMI, Kowal J, Stahlberg H, & Locher KP (2018). Cryo-EM structures of a human ABCG2 mutant trapped in ATP-bound and substrate-bound states. Nature 563 7731:426-430. PubMed Id: 30405239. doi:10.1038/s41586-018-0680-3.
*Multidrug transporter ABCG2 in apo-closed state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure bound to imatinib, 4.00 Å: 6VXH bound to mitoxantrone, 3.70 Å: 6VXI bound to SN38, 4.10 Å: 6VXJ	6VXF	Data File Jmol Viewer 6VXF 6VXH 6VXJ 6VXI	Orlando & Liao (2020). Orlando BJ, & Liao M (2020). ABCG2 transports anticancer drugs via a closed-to-open switch. Nat Commun 11 1:2264. PubMed Id: 32385283. doi:10.1038/s41467-020-16155-2.
*Multidrug transporter ABCG2 with bound topotecan: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.39 Å** cryo-EM structure with bound tariquidar, 3.12 Å: 7NEQ with bound mitoxantrone, 3.51 Å: 7NFD	7NEZ	Data File Jmol Viewer 7NEZ 7NFD 7NEQ	Kowal et al. (2021). Kowal J, Ni D, Jackson SM, Manolaridis I, Stahlberg H, & Locher KP (2021). Structural Basis of Drug Recognition by the Multidrug Transporter ABCG2. J Mol Biol 433 13:166980. PubMed Id: 33838147. doi:10.1016/j.jmb.2021.166980.
*Multidrug transporter ABCG2, E1S turnover-2 state: Homo sapiens* E Eukaryota (expressed in HEK293), 3.40 Å** cryo-EM structure topotecan turnover-1 state, 3.10 Å: 7OJH topotecan turnover-2 state, 3.40 Å: 7JOI	7OJ8	Data File Jmol Viewer 7OJ8 7OJH 7JOI	Yu et al. (2021). Yu Q, Ni D, Kowal J, Manolaridis I, Jackson SM, Stahlberg H, & Locher KP (2021). Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism. Nat Commun 12 1:4376. PubMed Id: 34282134. doi:10.1038/s41467-021-24651-2.
*Multidrug transporter ABCG2, tariquidar turnover-1 state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure tariquidar turnover-2 state, 3.20 Å: 8BI0	8BHT	Data File Jmol Viewer 8BHT 8BI0	Rasouli et al. (2023). Rasouli A, Yu Q, Dehghani-Ghahnaviyeh S, Wen PC, Kowal J, Locher KP, & Tajkhorshid E (2023). Differential dynamics and direct interaction of bound ligands with lipids in multidrug transporter ABCG2. Proc Natl Acad Sci U S A 120 1:e2213437120. PubMed Id: 36580587. doi:10.1073/pnas.2213437120.
*Multidrug transporter ABCG2 with bound 5D3-Fab and nanobody Nb8: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.04 Å** cryo-EM structure with bound 5D3-Fab and nanobody Nb17, 3.20 Å: 8P8A with bound 5D3-Fab and nanobody Nb96, 3.49 Å: 8P8J	8P7W	Data File Jmol Viewer 8P7W 8P8A 8P8J	Irobalieva et al. (2023). Irobalieva RN, Manolaridis I, Jackson SM, Ni D, Pardon E, Stahlberg H, Steyaert J, & Locher KP (2023). Structural Basis of the Allosteric Inhibition of Human ABCG2 by Nanobodies. J Mol Biol 435 19:168234. PubMed Id: 37597690. doi:10.1016/j.jmb.2023.168234.
*MacB ABC transporter: Acinetobacter baumannii* B Bacteria (expressed in E. coli), 3.39 Å** with bound ADPβS, 3.4 Å: 5WS4	5GKO	Data File Jmol Viewer 5GKO 5WS4	Okada et al. (2017). Okada U, Yamashita E, Neuberger A, Morimoto M, van Veen HW, & Murakami S (2017). Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii. Nat Commun 8 1:1336. PubMed Id: 29109439. doi:10.1038/s41467-017-01399-2.
*MacAB-TolC tripartite multidrug efflux pump, MacA-TolC section: Escherichia coli* B Bacteria, 3.3 Å** cryo-EM structure MacB section, 5.3 Å: 5NIL	5NIK	Data File Jmol Viewer 5NIK 5NIL	Fitzpatrick et al. (2017). Fitzpatrick AWP, Llabrés S, Neuberger A, Blaza JN, Bai XC, Okada U, Murakami S, van Veen HW, Zachariae U, Scheres SHW, Luisi BF, & Du D (2017). Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump. Nat Microbiol 2 :17070. PubMed Id: 28504659. doi:10.1038/nmicrobiol.2017.70.
*MacB ABC tranporter with bound ATPγS (P21): Aggregatibacter actinomycetemcomitans* B Bacteria (expressed in E. coli), 3.35 Å** with bound ATPγS (P6522), 3.9 Å: 5LJ6 with bound ATP (P21), 3.25 Å: 5LJ7 E. coli periplasmic domain (P21), 1.9 Å:5LJ8 E. coli MacB ABC domain (C2221), 2.3 Å: 5LJ9 E. coli MacB ABC domain (P6122), 2.4 Å:5LJA E. coli Lipoprotein-releasing system transmembrane protein LolC, 1.88 Å: 5NAA	5LIL	Data File Jmol Viewer 5LIL 5LJ9 5LJ7 5LJA 5NAA 5LJ8 5LJ6	Crow et al. (2017). Crow A, Greene NP, Kaplan E, & Koronakis V (2017). Structure and mechanotransmission mechanism of the MacB ABC transporter superfamily. Proc Natl Acad Sci USA 114 47:12572-12577. PubMed Id: 29109272. doi:10.1073/pnas.1712153114.
*MacAB-like efflux pump, Spr0694-0695 section: Streptococcus pneumoniae R6* B Bacteria (expressed in E. coli), 3.3 Å** Spr0693 section, 2.95 Å: 5UX0	5XU1	Data File Jmol Viewer 5XU1 5UX0	Yang et al. (2018). Yang HB, Hou WT, Cheng MT, Jiang YL, Chen Y, & Zhou CZ (2018). Structure of a MacAB-like efflux pump from Streptococcus pneumoniae. Nat Commun 9 1:196. PubMed Id: 29335499. doi:10.1038/s41467-017-02741-4.
*ABC transporter Rv1819c in AMP-PNP bound state: Mycobacterium tuberculosis* B Bacteria (expressed in E. coli), 3.50 Å** cryo-EM structure Rv1819c without addition of substrate, 4.30 Å: 6TQE	6TQF	Data File Jmol Viewer 6TQF 6TQE	Rempel et al. (2020). Rempel S, Gati C, Nijland M, Thangaratnarajah C, Karyolaimos A, de Gier JW, Guskov A, & Slotboom DJ (2020). A mycobacterial ABC transporter mediates the uptake of hydrophilic compounds. Nature 580 7803:409-412. PubMed Id: 32296172. doi:10.1038/s41586-020-2072-8.
*SbmA proton-dependent antibacterial peptide transporter in a nanodisc: Escherichia coli* B Bacteria, 3.59 Å** cryo-EM structure SbmA is not a true ABC transporter. Its closest relative is ABC transporter Rv1819c.	7P34	Data File Jmol Viewer 7P34	Ghilarov et al. (2021). Ghilarov D, Inaba-Inoue S, Stepien P, Qu F, Michalczyk E, Pakosz Z, Nomura N, Ogasawara S, Walker GC, Rebuffat S, Iwata S, Heddle JG, & Beis K (2021). Molecular mechanism of SbmA, a promiscuous transporter exploited by antimicrobial peptides. Sci Adv 7 37:eabj5363. PubMed Id: 34516884. doi:10.1126/sciadv.abj5363.
*heterodimeric IrtAB ABC transporter, apo form: Mycolicibacterium thermoresistibile* B Bacteria (expressed in E. coli), 2.70 Å** siderophore interaction domain of IrtAB, 1.80 Å: 6TEK	6TEJ	Data File Jmol Viewer 6TEJ 6TEK	Arnold et al. (2020). Arnold FM, Weber MS, Gonda I, Gallenito MJ, Adenau S, Egloff P, Zimmermann I, Hutter CAJ, Hürlimann LM, Peters EE, Piel J, Meloni G, Medalia O, & Seeger MA (2020). The ABC exporter IrtAB imports and reduces mycobacterial siderophores. Nature 580 7803:413-417. PubMed Id: 32296173. doi:10.1038/s41586-020-2136-9.
*YbtPQ ABC importer: Escherichia coli* B Bacteria, 3.67 Å** cryo-EM structure with substrate Ybt-Fe bound, 3.40 Å: 6P6J	6P6I	Data File Jmol Viewer 6P6I 6P6J	Wang et al. (2020). Wang Z, Hu W, & Zheng H (2020). Pathogenic siderophore ABC importer YbtPQ adopts a surprising fold of exporter. Sci Adv 6 6. PubMed Id: 32076651. doi:10.1126/sciadv.aay7997.
*YbtPQ ABC importer in occluded state:: Escherichia coli* B Bacteria, 3.10 Å** cryo-EM structure	8VSI	Data File Jmol Viewer 8VSI	Hu et al. (2024). Hu W, Parkinson C, & Zheng H (2024). Mechanistic Insights Revealed by YbtPQ in the Occluded State. Biomolecules 14 3:322. PubMed Id: 38540742. doi:10.3390/biom14030322.
*FhuCDB ferrichrome importer: Escherichia coli* B Bacteria, 3.40 Å** cryo-EM structure	7LB8	Data File Jmol Viewer 7LB8	Hu & Zheng (2021). Hu W, & Zheng H (2021). Cryo-EM reveals unique structural features of the FhuCDB Escherichia coli ferrichrome importer. Commun Biol 4 1:1383. PubMed Id: 34887516. doi:10.1038/s42003-021-02916-2.
*PmtCD ABC exporter, C1 symmetry: Staphylococcus aureus* B Bacteria, 4.00 Å** cryo-EM structure without the basket domain, C2 symmetry, 3.60 Å: 6XJH x-ray: peptide exporter basket domain, 2.11 Å: 6U2D x-ray: exporter basket domain, 1.40 Å: 6XFU	6XJI	Data File Jmol Viewer 6XJI 6U2D 6XJH 6XFU	Zeytuni et al. (2020). Zeytuni N, Dickey SW, Hu J, Chou HT, Worrall LJ, Alexander JAN, Carlson ML, Nosella M, Duong F, Yu Z, Otto M, & Strynadka NCJ (2020). Structural insight into the Staphylococcus aureus ATP-driven exporter of virulent peptide toxins. Sci Adv 6 40. PubMed Id: 32998902. doi:10.1126/sciadv.abb8219.
*OpuA osmoregulatory ABC transporter, inward facing state: Lactococcus lactis* B Bacteria, 3.30 Å** Cryo-EM structure E190Q mutant (occluded state), 3.40 Å: 7AHD inhibited inward facing state, 4.10 Å: 7AHE inhibited inward-facing, SBD docked, 3.50 Å: 7AHH	7AHC	Data File Jmol Viewer 7AHC 7AHD 7AHE 7AHH	Sikkema et al. (2020). Sikkema HR, van den Noort M, Rheinberger J, de Boer M, Krepel ST, Schuurman-Wolters GK, Paulino C, & Poolman B (2020). Gating by ionic strength and safety check by cyclic-di-AMP in the ABC transporter OpuA. Sci Adv 6 47:eabd7697. PubMed Id: 33208376. doi:10.1126/sciadv.abd7697.
*ABCA1 lipid exporter: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 4.1 Å** cryo-EM structure	5XJY	Data File Jmol Viewer 5XJY	Qian et al. (2017). Qian H, Zhao X, Cao P, Lei J, Yan N, & Gong X (2017). Structure of the Human Lipid Exporter ABCA1. Cell 169 7:1228-1239.e10. PubMed Id: 28602350. doi:10.1016/j.cell.2017.05.020.
*ABCA1 lipid exporter in nanodisc: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.00 Å** cryo-EM structure	7TDT	Data File Jmol Viewer 7TDT	Plummer-Medeiros et al. (2023). Plummer-Medeiros AM, Culbertson AT, Morales-Perez CL, & Liao M (2023). Activity and Structural Dynamics of Human ABCA1 in a Lipid Membrane. J Mol Biol 435 8:168038. PubMed Id: 36889459. doi:10.1016/j.jmb.2023.168038.
*surfactant lipids exporter ABCA3 (nucleotide-free): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure with bound ATP, 3.30 Å: 7W02	7W01	Data File Jmol Viewer 7W01 7W02	Xie et al. (2022). Xie T, Zhang Z, Yue J, Fang Q, & Gong X (2022). Cryo-EM structures of the human surfactant lipid transporter ABCA3. Sci Adv 8 14:eabn3727. PubMed Id: 35394827. doi:10.1126/sciadv.abn3727.
*retinal importer ABCA4 (Rim protein ABCR), ATP-free: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.27 Å** cryo-EM structure with bound ATP, 3.27 Å: 7LKZ	7LKP	Data File Jmol Viewer 7LKP 7LKZ	Liu et al. (2021). Liu F, Lee J, & Chen J (2021). Molecular structures of the eukaryotic retinal importer ABCA4. Elife 10 :e63524. PubMed Id: 33605212. doi:10.7554/eLife.63524.
*retinal importer ABCA4 (Rim protein ABCR), apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure in NRPE-bound state, 3.40 Å: 7E7O in ATP-bound state, 3.30 Å: 7E7Q	7E7I	Data File Jmol Viewer 7E7I 7E7Q 7E7O	Xie et al. (2021). Xie T, Zhang Z, Fang Q, Du B, & Gong X (2021). Structural basis of substrate recognition and translocation by human ABCA4. Nat Commun 12 1:3853. PubMed Id: 34158497. doi:10.1038/s41467-021-24194-6.
*retinal importer ABCA4 (Rim protein ABCR), unbound state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure in complex with N-ret-PE, 2.92 Å 7M1Q	7M1P	Data File Jmol Viewer 7M1P 7M1Q	Scortecci et al. (2021). Scortecci JF, Molday LL, Curtis SB, Garces FA, Panwar P, Van Petegem F, & Molday RS (2021). Cryo-EM structures of the ABCA4 importer reveal mechanisms underlying substrate binding and Stargardt disease. Nat Commun 12 1:5902. PubMed Id: 34625547. doi:10.1038/s41467-021-26161-7.
*ABCA7 lipid exporter in brain polar lipid extract (BPL)/Chol nanodiscs: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure in PE/Chol nanodiscs, 4.00 Å: 8EE6 in digitonin, 3.90 Å: 8EEB E965Q/E1951Q mutant reconstituted in nanodiscs, ATP-bound closed state, 3.70 Å: 8EOP	8EDW	Data File Jmol Viewer 8EDW 8EE6 8EOP 8EEB	Le et al. (2023). Le LTM, Thompson JR, Dehghani-Ghahnaviyeh S, Pant S, Dang PX, French JB, Kanikeyo T, Tajkhorshid E, & Alam A (2023). Cryo-EM structures of human ABCA7 provide insights into its phospholipid translocation mechanisms. EMBO J 42 3:e111065. PubMed Id: 36484366. doi:10.15252/embj.2022111065.
*lipoprotein outer membrane localization (Lol) protein LolCDE in complex with lipoprotein: Escherichia coli* B Bacteria, 3.30 Å** cryo-EM structure in complex with lipoprotein and LolA, 3.60 Å: 7ARM in complex with AMP-PNP in the closed NBD state, 4.10 Å: 7ARK in complex with lipoprotein and AMP-PNP complex, undimerized form, 3.20 Å: 7ARJ in complex with lipoprotein and ADP, 3.20 Å: 7ARL apo structure, 3.40 Å: 7ARI	7ARH	Data File Jmol Viewer 7ARH 7ARI 7ARM 7ARK 7ARL 7ARJ	Tang et al. (2021). Tang X, Chang S, Zhang K, Luo Q, Zhang Z, Wang T, Qiao W, Wang C, Shen C, Zhang Z, Zhu X, Wei X, Dong C, Zhang X, & Dong H (2021). Structural basis for bacterial lipoprotein relocation by the transporter LolCDE. Nat Struct Mol Biol 28 4:347-355. PubMed Id: 33782615. doi:10.1038/s41594-021-00573-x.
*lipoprotein outer membrane localization (Lol) protein LolCDE, nucleotide-free: Escherichia coli* B Bacteria, 3.80 Å** cryo-EM structure nucleotide-bound, 3.50 Å: 7MDY	7MDX	Data File Jmol Viewer 7MDX 7MDY	Sharma et al. (2021). Sharma S, Zhou R, Wan L, Feng S, Song K, Xu C, Li Y, & Liao M (2021). Mechanism of LolCDE as a molecular extruder of bacterial triacylated lipoproteins. Nat Commun 12 1:4687. PubMed Id: 34344901. doi:10.1038/s41467-021-24965-1.
*Pdr5 pleiotropic drug resistance transporter, inward-facing conformation: Saccharomyces cerevisiae* E Eukaryota, 3.45 Å** cryo-EM structure inward-facing conformation with ADP/ATP, 2.85 Å 7P04 inward-facing conformation with ADP/ATP and rhodamine 6G, 3.13 Å 7P05 in outward-facing conformation with ADP-orthovanadate/ATP, 3.77 Å 7P06	7P03	Data File Jmol Viewer 7P03 7P04 7P05 7P06	Harris et al. (2021). Harris A, Wagner M, Du D, Raschka S, Nentwig LM, Gohlke H, Smits SHJ, Luisi BF, & Schmitt L (2021). Structure and efflux mechanism of the yeast pleiotropic drug resistance transporter Pdr5. Nat Commun 12 1:5254. PubMed Id: 34489436. doi:10.1038/s41467-021-25574-8.
*BmrCD heterodimeric multidrug exporter: Bacillus subtilis* B Bacteria (expressed in E. coli), 3.55 Å** cryo-EM structure	7M33	Data File Jmol Viewer 7M33	Thaker et al. (2022). Thaker TM, Mishra S, Zhou W, Mohan M, Tang Q, Faraldo-Goméz JD, Mchaourab HS, & Tomasiak TM (2022). Asymmetric drug binding in an ATP-loaded inward-facing state of an ABC transporter. Nat Chem Biol 18 2:226-235. PubMed Id: 34931066. doi:10.1038/s41589-021-00936-x.
*BmrCD heterodimeric multidrug exporter, inward-facing conformation with bound 2 Hoechst molecules and ATP: Bascillus subtilis* B Bacteria (expressed in E. coli), 3.34 Å** cryo-EM structure inward-facing conformation, with bound 1 Hoechst molecule and ATP, 3.06 Å: 8SZC occluded conformation, with bound ATP, 2.90 Å: 8FHK occluded confirmation, with bound ADPV_i, 2.96 Å: 8T1P	8FMV	Data File Jmol Viewer 8FMV 8T1P 8FHK 8SZC	Tang et al. (2023). Tang Q, Sinclair M, Hasdemir HS, Stein RA, Karakas E, Tajkhorshid E, & Mchaourab HS (2023). Asymmetric conformations and lipid interactions shape the ATP-coupled cycle of a heterodimeric ABC transporter. Nat Commun 14 1:7184. PubMed Id: 37938578. doi:10.1038/s41467-023-42937-5.
*BmrA type IV ABC transporter. E504A mutant with bound ATP and Mg: Bacillus subtilis* B Bacteria (expressed in E. coli), 3.90 Å** cryo-EM structure with bound ATP, Mg, and Rhodamine 6G, 4.20 Å 7BG4 in complex with ATP-Mg, 3.50 Å 7OW8 x-ray: E504A in an outward-facing conformation, 3.95 Å 6R72	6R81	Data File Jmol Viewer 6R81 7OW8 6R72 7BG4	Chaptal et al. (2022). Chaptal V, Zampieri V, Wiseman B, Orelle C, Martin J, Nguyen KA, Gobet A, Di Cesare M, Magnard S, Javed W, Eid J, Kilburg A, Peuchmaur M, Marcoux J, Monticelli L, Hogbom M, Schoehn G, Jault JM, Boumendjel A, & Falson P (2022). Substrate-bound and substrate-free outward-facing structures of a multidrug ABC exporter. Sci Adv 8 4:eabg9215. PubMed Id: 35080979. doi:10.1126/sciadv.abg9215.
*Bce-type ABC transporter, nucleotide-free conformation: Bacillus subtilis* B Bacteria (expressed in E. coli), 3.80 Å** cryo-EM structure E169Q variant, ATP-bound conformation, 3.70 Å 7TCH	7TCG	Data File Jmol Viewer 7TCG 7TCH	George et al. (2022). George NL, Schilmiller AL, & Orlando BJ (2022). Conformational snapshots of the bacitracin sensing and resistance transporter BceAB. Proc Natl Acad Sci U S A 119 14:e2123268119. PubMed Id: 35349335. doi:10.1073/pnas.2123268119.
*NosDFY ABC transporter complexed with nitrous oxide reductase NosZ: Pseudomonas stutzeri* B Bacteria (expressed in E. coli), 3.78 Å** cryo-EM structure NosDFYL in GDN, 3.04 Å: 7ZNQ	7QBA	Data File Jmol Viewer 7QBA 7ZNQ	Müller et al. (2022). Müller C, Zhang L, Zipfel S, Topitsch A, Lutz M, Eckert J, Prasser B, Chami M, Lü W, Du J, & Einsle O (2022). Molecular interplay of an assembly machinery for nitrous oxide reductase. Nature 608 7923:626-631. PubMed Id: 35896743. doi:10.1038/s41586-022-05015-2.
*hemolysin A secretion system HlyB/D complex: Escherichia coli* B Bacteria, 2.90 Å** cryo-EM structure ATP-bound, 3.40 Å: 8DCK	7SGR	Data File Jmol Viewer 7SGR 8DCK	Zhao et al. (2022). Zhao H, Lee J, & Chen J (2022). The hemolysin A secretion system is a multi-engine pump containing three ABC transporters. Cell 185 18:3329-3340.e13. PubMed Id: 36055198. doi:10.1016/j.cell.2022.07.017.
*ABC transporter STE6-2p, apo conformation: Pichia pastoris* E Eukaryota, 3.10 Å** cryo-EM structure with bound Verapamil, 3.20 Å: 7QKR	7QKS	Data File Jmol Viewer 7QKS 7QKR	Schleker et al. (2022). Schleker ESM, Buschmann S, Xie H, Welsch S, Michel H, & Reinhart C (2022). Structural and functional investigation of ABC transporter STE6-2p from Pichia pastoris reveals unexpected interaction with sterol molecules. Proc Natl Acad Sci U S A 119 43:e2202822119. PubMed Id: 36256814. doi:10.1073/pnas.2202822119.
*EfrCD ABC transporter in complex with nanobody: Enterococcus faecalis* B Bacteria (expressed in Lactococcus lactis), 4.25 Å** cryo-EM structure	7OCY	Data File Jmol Viewer 7OCY	Meier et al. (2023). Meier G, Thavarasah S, Ehrenbolger K, Hutter CAJ, Hürlimann LM, Barandun J, & Seeger MA (2023). Deep mutational scan of a drug efflux pump reveals its structure-function landscape. Nat Chem Biol 19 4:440-450. PubMed Id: 36443574. doi:10.1038/s41589-022-01205-1.
*OppABCD oligopeptide permease in pre-translocation state: Mycobacterium tuberculosis* B Bacteria (expressed in M. smegmatis), 3.25 Å** cryo-EM structure in resting state, 3.28 Å: 8J5R in pre-catalytic intermediate state, 3.00 Å: 8J5S in catalytic intermediate state, 2.98 Å: 8J5T X-ray: OppA with bound endogenous oligopeptide, 1.98 Å: 8J5U	8J5Q	Data File Jmol Viewer 8J5Q 8J5R 8J5S 8J5T 8J5U	Yang et al. (2024). Yang X, Hu T, Liang J, Xiong Z, Lin Z, Zhao Y, Zhou X, Gao Y, Sun S, Yang X, Guddat LW, Yang H, Rao Z, & Zhang B (2024). An oligopeptide permease, OppABCD, requires an iron-sulfur cluster domain for functionality. Nat Struct Mol Biol . PubMed Id: 38548954. doi:10.1038/s41594-024-01256-z.
Tripartite ATP-independent periplasmic (TRAP) protein family
*SiaQM TRAP transporter: Haemophilus influenzae* B Bacteria (expressed in E. coli), 4.70 Å** cryo-EM structure	7QE5	Data File Jmol Viewer 7QE5	Peter et al. (2022). Peter MF, Ruland JA, Depping P, Schneberger N, Severi E, Moecking J, Gatterdam K, Tindall S, Durand A, Heinz V, Siebrasse JP, Koenig PA, Geyer M, Ziegler C, Kubitscheck U, Thomas GH, & Hagelueken G (2022). Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter. Nat Commun 13 1:4471. PubMed Id: 35927235. doi:10.1038/s41467-022-31907-y.
*SiaQM TRAP transporter in amphipol: Photobacterium profundum* B Bacteria (expressed in E. coli), 2.97 Å** cryo-EM structure in nanodisc, 3.03 Å: 8B01 x-ray: periplasmic component SiaP, 1.04 Å: 7T3E	7QHA	Data File Jmol Viewer 7QHA 7T3E 8B01	Davies et al. (2023). Davies JS, Currie MJ, North RA, Scalise M, Wright JD, Copping JM, Remus DM, Gulati A, Morado DR, Jamieson SA, Newton-Vesty MC, Abeysekera GS, Ramaswamy S, Friemann R, Wakatsuki S, Allison JR, Indiveri C, Drew D, Mace PD, & Dobson RCJ (2023). Structure and mechanism of a tripartite ATP-independent periplasmic TRAP transporter. Nat Commun 14 1:1120. PubMed Id: 36849793. doi:10.1038/s41467-023-36590-1.
Major Facilitator Superfamily (MFS) Transporters
*LacY Lactose Permease Transporter (C154G mutant): Escherichia coli* B Bacteria, 3.6 Å** 1PV7 is with bound high-affinity lactose homolog, TDG. See 1PV6 for structure without TDG (3.5 Å).	1PV7	Data File Jmol Viewer 1PV7 1PV6 lactose permease, 3D structure	Abramson et al. (2003). Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, & Iwata S (2003). Structure and mechanism of the lactose permease of Escherichia coli. Science 301 :610-615. PubMed Id: 12893935.
*LacY Lactose Permease (C154G mutant) without substrate at 2 pH values: Escherichia coli* B Bacteria, 2.95 Å** 2CFQ structure determined at pH 6.5. 2CFP structure determined at pH 5.6 (3.30 Å).	2CFQ	Data File Jmol Viewer 2CFQ 2CFP	Mirza et al. (2006). Mirza O, Guan L, Verner G, Iwata S & Kaback HR (2006). Structural evidence for induced fit and a mechanism for sugar/H⁺symport in LacY. EMBO J 25 :1177-1183. PubMed Id: 16525509.
*LacY Lactose Permease (wild-type) with TDG: Escherichia coli* B Bacteria, 3.6 Å**	2V8N	Data File Jmol Viewer 2V8N	Guan et al. (2007). Guan L, Mirza O, Verner G, Iwata S, & Kaback HR (2007). Structural determination of wild-type lactose permease. Proc Natl Acad Sci USA 104 :15294-15298. PubMed Id: 17881559.
*LacY Lactose Permease with covalently bound MTS-gal: Escherichia coli* B Bacteria, 3.4 Å** methanethiosulfonyl-galactopyranoside (MTS-gal) is a 'suicide' substrate.	2Y5Y	Data File Jmol Viewer 2Y5Y	Chaptal et al. (2011). Chaptal V, Kwon S, Sawaya MR, Guan L, Kaback HR, & Abramson J (2011). Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition. Proc Natl Acad Sci USA 108 :9361-9366. PubMed Id: 21593407. doi:10.1073/pnas.1105687108.
*LacY Lactose Permease Transporter (G46W/G262W mutant) with bound lactose analog: Escherichia coli* B Bacteria, 3.50 Å** Occluded, partially open to periplasmic side	4OAA	Data File Jmol Viewer 4OAA	Kumar et al. (2014). Kumar H, Kasho V, Smirnova I, Finer-Moore JS, Kaback HR, & Stroud RM (2014). Structure of sugar-bound LacY. Proc Natl Acad Sci USA 111 :1784-1788. PubMed Id: 24453216. doi:10.1073/pnas.1324141111.
*LacY Lactose Permease Transporter (G46W, G262W mutant) with bound α-NPG: Escherichia coli* B Bacteria, 3.31 Å**	4ZYR	Data File Jmol Viewer 4ZYR	Kumar et al. (2015). Kumar H, Finer-Moore JS, Kaback HR, & Stroud RM (2015). Structure of LacY with an ?-substituted galactoside: Connecting the binding site to the protonation site. Proc Natl. Acad Sc. USA 112 :9004-9009. PubMed Id: 26157133. doi:10.1073/pnas.1509854112.
*LacY Lactose Permease Transporter (G46W, G262W mutant) with bound nanobody Nb9039: Escherichia coli* B Bacteria, 3.3 Å**	5GXB	Data File Jmol Viewer 5GXB	Jiang et al. (2016). Jiang X, Smirnova I, Kasho V, Wu J, Hirata K, Ke M, Pardon E, Steyaert J, Yan N, & Kaback HR (2016). Crystal structure of a LacY-nanobody complex in a periplasmic-open conformation. Proc Natl Acad Sci USA 113 :12420-12425. PubMed Id: 27791182. doi:10.1073/pnas.1615414113.
*LacY Lactose Permease Transporter (G46W, G262W mutant) with bound nanobody Nb9047 in complex with NPG: Escherichia coli* B Bacteria, 3.0 Å**	6C9W	Data File Jmol Viewer 6C9W	Kumar et al. (2018). Kumar H, Finer-Moore JS, Jiang X, Smirnova I, Kasho V, Pardon E, Steyaert J, Kaback HR, & Stroud RM (2018). Crystal Structure of a ligand-bound LacY-Nanobody Complex. Proc Natl Acad Sci USA 115 35:8769-8774. PubMed Id: 30108145. doi:10.1073/pnas.1801774115.
*FucP Fucose Transporter in outward-facing conformation: Escherichia coli* B Bacteria, 3.1 Å** N162A mutant, 3.2 Å: 3O7P	3O7Q	Data File Jmol Viewer 3O7Q 3O7P	Dang et al. (2010). Dang S, Sun L, Huang Y, Lu F, Liu Y, Gong H, Wang J, & Yan N (2010). Structure of a fucose transporter in an outward-open conformation. Nature 467 :734-738. PubMed Id: 20877283.
*MelB Na⁺/melibiose symporter: Salmonella typhimurium* B Bacteria (expressed in E. coli), 3.35 Å** MelB catalyzes electrogenic symport of galactosides with Na⁺, Li⁺, or H⁺	4M64	Data File Jmol Viewer 4M64	Ethayathulla et al. (2014). Ethayathulla AS, Yousef MS, Amin A, Leblanc G, Kaback HR, & Guan L (2014). Structure-based mechanism for Na⁺/melibiose symport by MelB. Nat Commun 5 :3009. PubMed Id: 24389923. doi:10.1038/ncomms4009.
*MelB Na⁺/melibiose symporter, D59C mutant with bound DDMB: Salmonella typhimurium* B Bacteria (expressed in E. coli), 3.15 Å** with bound α-NPG, 3.05 Å 7L17	7L16	Data File Jmol Viewer 7L16 7L17	Guan & Hariharan (2021). Guan L, & Hariharan P (2021). X-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB. Commun Biol 4 1:931. PubMed Id: 34341464. doi:10.1038/s42003-021-02462-x.
*XylE proton:xylose symporter with bound D-xylose: Escherichia coli* B Bacteria, 2.81 Å** With bound D-glucose, 2.89 Å: 4GBZ With bound 6-bromo-6-deoxy-D-glucose, 2.60 Å: 4GC0	4GBY	Data File Jmol Viewer 4GBY 4GC0 4GBZ	Sun et al. (2012). Sun L, Zeng X, Yan C, Sun X, Gong X, Rao Y, & Yan N (2012). Crystal structure of a bacterial homologue of glucose transporters GLUT1-4. Nature 490 :361-366. PubMed Id: 23075985. doi:10.1038/nature11524.
*XylE proton:xylose symporter in partially occluded inward-open state: Escherichia coli* B Bacteria, 3.80 Å** inward-open state, 4.20 Å: 4JA4	4JA3	Data File Jmol Viewer 4JA3 4JA4	Quistgaard et al. (2013). Quistgaard EM, Löw C, Moberg P, Trésaugues L, & Nordlund P (2013). Structural basis for substrate transport in the GLUT-homology family of monosaccharide transporters. Nature Struc Mol Biol 20 :766-768. PubMed Id: 23624861. doi:10.1038/nsmb.2569.
*XylE proton:xylose symporter, inward-facing open conformation: Escherichia coli* B Bacteria, 3.51 Å**	4QIQ	Data File Jmol Viewer 4QIQ	Wisedchaisri et al. (2014). Wisedchaisri G, Park MS, Iadanza MG, Zheng H, & Gonen T (2014). Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE. Nat Comms 5 :4521. PubMed Id: 25088546. doi:10.1038/ncomms5521.
*GlcP Glucose/H⁺ symporter: Staphylococcus epidermidis* B Bacteria (expressed in E. coli), 3.20 Å**	4LDS	Data File Jmol Viewer 4LDS	Iancu et al. (2013). Iancu CV, Zamoon J, Woo SB, Aleshin A, & Choe JY (2013). Crystal structure of a glucose/H⁺ symporter and its mechanism of action. Proc Natl Acad Sci USA 110 :17862-17867. PubMed Id: 24127585. doi:10.1073/pnas.1311485110.
*GlpT Glycerol-3-Phosphate Transporter: Escherichia coli* B Bacteria, 3.3 Å**	1PW4	Data File Jmol Viewer 1PW4 glycerol-3-phosphate transporter	Huang et al. (2003). Huang Y, Lemieux MJ, Song J, Auer M, & Wang D-N (2003). Structure and mechanism of the glycerol-3-phosphate transporter from Eschericia coli. Science 301 :616-620. PubMed Id: 12893936.
*EmrD Multidrug Transporter: Escherichia coli* B Bacteria, 3.5 Å**	2GFP	Data File Jmol Viewer 2GFP multidrug resistance protein EmrD	Yin et al. (2006). Yin Y, He X, Szewczyk P, Nguyen T, & Chang G. (2006). Structure of the multidrug transporter EmrD from Escherichia coli. Science 312 :741-744. PubMed Id: 16675700.
*PepT_So Oligopeptide-proton symporter (POT family): Shewanella oneidensis* B Bacteria (expressed in E. coli), 3.6 Å** The conformation appears to be that of an occluded state.	2XUT	Data File Jmol Viewer 2XUT	Newstead et al. (2011). Newstead S, Drew D, Cameron AD, Postis VL, Xia X, Fowler PW, Ingram JC, Carpenter EP, Sansom MS, McPherson MJ, Baldwin SA, & Iwata S (2011). Crystal structure of a prokaryotic homologue of the mammalian oligopeptide-proton symporters, PepT1 and PepT2. EMBO J 30 :417-426. PubMed Id: 21131908.
*PepT_So Oligopeptide-proton symporter (POT family) with bound AlaTyr(Br): Shewanella oneidensis* B Bacteria (expressed in E. coli), 3.15 Å** with bound AlaTyr(Br)Ala, 3.91 Å: 4TPG with bound AlaAlaAla, 3.20 Å: 4TPJ	4TPH	Data File Jmol Viewer 4TPH 4TPJ 4TPG	Guettou et al. (2014). Guettou F, Quistgaard EM, Raba M, Moberg P, Löw C, & Nordlund P (2014). Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2. Nat Struct Mol Biol 21 8:728-731. PubMed Id: 25064511. doi:10.1038/nsmb.2860.
*PepT_So Oligopeptide-proton symporter (POT family), inward-open conformation: Shewanella oneidensi* B Bacteria (expressed in E. coli), 3.00 Å**	4UVM	Data File Jmol Viewer 4UVM	Fowler et al. (2015). Fowler PW, Orwick-Rydmark M, Radestock S, Solcan N, Dijkman PM, Lyons JA, Kwok J, Caffrey M, Watts A, Forrest LR, & Newstead S (2015). Gating topology of the proton-coupled oligopeptide symporters. Structure 23 2:290-301. PubMed Id: 25651061. doi:10.1016/j.str.2014.12.012.
*PepT_So2 Oligopeptide-proton symporter (POT family): Shewanella oneidensis* B Bacteria (expressed in E. coli), 4.13 Å** cryo-EM structure Form A x-ray crystal structure, 3.90 Å: 6JKD Form B x-ray crystal structure, 3.50 Å: 6JKC	6JI1	Data File Jmol Viewer 6JI1 6JKC 6JKD	Nagamura et al. (2019). Nagamura R, Fukuda M, Kawamoto A, Matoba K, Dohmae N, Ishitani R, Takagi J, & Nureki O (2019). Structural basis for oligomerization of the prokaryotic peptide transporter PepT_So2. Acta Crystallogr F Struct Biol Commun 75 :348-358. PubMed Id: 31045564. doi:10.1107/S2053230X19003546.
*PepT_St Oligopeptide-proton symporter (POT family): Streptococcus thermophilus* B Bacteria (expressed in E. coli), 3.30 Å** Conformation appears to be that of an inward-facing state.	4APS	Data File Jmol Viewer 4APS	Solcan et al. (2012). Solcan N, Kwok J, Fowler PW, Cameron AD, Drew D, Iwata S, & Newstead S (2012). Alternating access mechanism in the POT family of oligopeptide transporters. EMBO J 31 :3411-3421. PubMed Id: 22659829. doi:10.1038/emboj.2012.157.
*PepT_St Oligopeptide-proton symporter (POT family) at 100 K: Streptococcus thermophilus* B Bacteria (expressed in E. coli), 2.30 Å** data collected at 293 K, 2.80 Å: 4XNI Data collected by serial x-ray crystallography.	4XNJ	Data File Jmol Viewer 4XNJ 4XNI	Huang et al. (2015). Huang CY, Olieric V, Ma P, Panepucci E, Diederichs K, Wang M, & Caffrey M (2015). In meso in situ serial X-ray crystallography of soluble and membrane proteins. Acta Crystallogr D Biol Crystallogr 71 :1238-1256. PubMed Id: 26057665. doi:10.1107/S1399004715005210.
*PepT_St Oligopeptide-proton symporter (POT family) with bound dipeptide Ala-Leu: Streptococcus thermophilus* B Bacteria (expressed in E. coli), 2.66 Å** with Ala-Gln peptide, 2.38 Å: 5OXK with Asp-Glu peptide, 2.30 Å: 5OXM with Phe-Ala peptide, 2.20 Å: 5OXN in 100 mM HEPES, 2.0 Å: 6EIA in 300 mM HEPES, 2.20 Å: 5OXQ occluded state with bound PO₄, 2.37 Å: 5OXP apo protein, 1.95 Å: 5OXO	5OXL	Data File Jmol Viewer 5OXL 5OXO 5OXP 5OXQ 5OXK 6EIA 5OXM 5OXN	Martinez Molledo et al. (2018). Martinez Molledo M, Quistgaard EM, Flayhan A, Pieprzyk J, & Löw C (2018). Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter. Structure 26 :467-476.e4. PubMed Id: 29429879. doi:10.1016/j.str.2018.01.005.
*PepT_St Oligopeptide-proton symporter (POT family) crystallized in space group P3₁21: Streptococcus thermophilus* B Bacteria (expressed in E. coli), 3.40 Å**	5MMT	Data File Jmol Viewer 5MMT	Quistgaard et al. (2017). Quistgaard EM, Martinez Molledo M, & Löw C (2017). Structure determination of a major facilitator peptide transporter: Inward facing PepT_St from Streptococcus thermophilus crystallized in space group P3₁21. PLoS ONE 12 3. PubMed Id: 28264013. doi:10.1371/journal.pone.0173126.
*Proton-dependent oligopeptide transporter (POT): Geobacillus kaustophilus* B Bacteria (expressed in E. coli), 1.90 Å** In complex with sulfate, 2.00 Å: 4IKW E310Q mutant, 2.30 Å: 4IKX E310Q mutant in complex with sulfate, 2.10 Å: 4IKY E310Q mutant in complex with dipeptide analog alafosfalin, 2.40 Å: 4IKZ	4IKV	Data File Jmol Viewer 4IKV 4IKY 4IKW 4IKZ 4IKX	Doki et al. (2013). Doki S, Kato HE, Solcan N, Iwaki M, Koyama M, Hattori M, Iwase N, Tsukazaki T, Sugita Y, Kandori H, Newstead S, Ishitani R, & Nureki O (2013). Structural basis for dynamic mechanism of proton-coupled symport by the peptide transporter POT. Proc Natl Acad Sci USA 110 28:11343-11348. PubMed Id: 23798427. doi:10.1073/pnas.1301079110.
*YbgH peptide transporter (POT family), inward facing conformation: Escherichia coli* B Bacteria, 3.40 Å**	4Q65	Data File Jmol Viewer 4Q65	Zhao et al. (2014). Zhao Y, Mao G, Liu M, Zhang L, Wang X, & Zhang XC (2014). Crystal Structure of the E. coli Peptide Transporter YbgH. Structure 22 :1152-1160. PubMed Id: 25066136. doi:10.1016/j.str.2014.06.008.
*PepT dipeptide transporter (POT family): Yersinia enterocolitica* B Bacteria (expressed in E. coli), 3.02 Å**	4W6V	Data File Jmol Viewer 4W6V	Boggavarapu et al. (2015). Boggavarapu R, Jeckelmann JM, Harder D, Ucurum Z, & Fotiadis D (2015). Role of electrostatic interactions for ligand recognition and specificity of peptide transporters. BMC Biol 13 1. PubMed Id: 26246134. doi:10.1186/s12915-015-0167-8.
*PepT_Xc mammalian-like peptide transporter (POT family): Xanthomonas campestris* B Bacteria (expressed in E. coli), 2.1 Å**	6EI3	Data File Jmol Viewer 6EI3	Parker et al. (2017). Parker JL, Li C, Brinth A, Wang Z, Vogeley L, Solcan N, Ledderboge-Vucinic G, Swanson JMJ, Caffrey M, Voth GA, & Newstead S (2017). Proton movement and coupling in the POT family of peptide transporters. Proc Natl Acad Sci USA 114 50:13182-13187. PubMed Id: 29180426. doi:10.1073/pnas.1710727114.
*PepT_Sh S-Cys-Gly-3M3SH transporter involved in body odor production: Staphylococcus hominis* B Bacteria (expressed in E. coli), 2.5 Å**	6EXS	Data File Jmol Viewer 6EXS	Minhas et al. (2018). Minhas GS, Bawdon D, Herman R, Rudden M, Stone AP, James AG, Thomas GH, & Newstead S (2018). Structural basis of malodour precursor transport in the human axilla. Elife 7 :e34995. PubMed Id: 29966586. doi:10.7554/eLife.34995.
*PiPT high-affinity phosphate transporter: Piriformospora indica* E Eukaryota (expressed in S. cerevisiae), 2.90 Å**	4J05	Data File Jmol Viewer 4J05	Pedersen et al. (2013). Pedersen BP, Kumar H, Waight AB, Risenmay AJ, Roe-Zurz Z, Chau BH, Schlessinger A, Bonomi M, Harries W, Sali A, Johri AK, & Stroud RM (2013). Crystal structure of a eukaryotic phosphate transporter. Nature 496 :533-536. PubMed Id: 23542591. doi:10.1038/nature12042.
*NarU nitrate transporter: Escherichia coli* B Bacteria, 3.01 Å** First structure of a member of the nitrate/nitrite porter family (NNP) Selenomethionine derivative, 3.11 Å: 4IU8	4IU9	Data File Jmol Viewer 4IU9 4IU8	Yan et al. (2013). Yan H, Huang W, Yan C, Gong X, Jiang S, Zhao Y, Wang J, & Shi Y (2013). Structure and mechanism of a nitrate transporter. Cell Rep 3 :716-723. PubMed Id: 23523348. doi:10.1016/j.celrep.2013.03.007.
*NarK nitrate/nitrite exchanger: Escherichia coli* B Bacteria, 2.60 Å** A member of the nitrate/nitrite porter family (NNP) with bound nitrite, 2.80 Å: 4JRE	4JR9	Data File Jmol Viewer 4JR9 4JRE	Zheng et al. (2013). Zheng H, Wisedchaisri G, & Gonen T (2013). Crystal structure of a nitrate/nitrite exchanger. Nature 497 :647-651. PubMed Id: 23665960. doi:10.1038/nature12139.
*NarK nitrate/nitrite exchanger, apo inward-open: Escherichia coli* B Bacteria, 2.35 Å** Nitrate-bound, inward-open, 2.40 Å: 4U4T Nitrate-bound, occluded, 2.40 Å: 4U4W	4U4V	Data File Jmol Viewer 4U4V 4U4T 4U4W	Fukuda et al. (2015). Fukuda M, Takeda H, Kato HE, Doki S, Ito K, Maturana AD, Ishitani R, & Nureki O (2015). Structural basis for dynamic mechanism of nitrate/nitrite antiport by NarK. Nat Commun 6 :7097. PubMed Id: 25959928. doi:10.1038/ncomms8097.
*NRT1.1 nitrate transporter, apo form: Arabidopsis thaliana* E Eukaryota (expressed in S. cerevisiae), 3.70 Å** Member of the NPF (NRT1/PTR) family. 5A2N supersedes 4CL4. in complex with nitrate, 3.71 Å: 5A2O 5A2O supersedes 4CL5.	5A2N	Data File Jmol Viewer 5A2N 5A2O	Parker et al. (2014). Parker JL, & Newstead S (2014). Molecular basis of nitrate uptake by the plant nitrate transporter NRT1.1. Nature 507 :68-72. PubMed Id: 24572366. doi:10.1038/nature13116.
*NRT1.1 nitrate transporter, homodimer in inward-facing conformation: Arabidopsis thaliana* E Eukaryota (expressed in S. frugiperda), 3.25 Å**	4OH3	Data File Jmol Viewer 4OH3	Sun et al. (2014). Sun J, Bankston JR, Payandeh J, Hinds TR, Zagotta WN, & Zheng N (2014). Crystal structure of the plant dual-affinity nitrate transporter NRT1.1. Nature 507 :73-77. PubMed Id: 24572362. doi:10.1038/nature13074.
*YajR drug efflux transporter: Escherichia coli* B Bacteria, 3.15 Å** Belongs to the 12-TM drug-resistance H⁺-driven antiporter (DHA12) subfamily.	3WDO	Data File Jmol Viewer 3WDO	Jiang et al. (2013). Jiang D, Zhao Y, Wang X, Fan J, Heng J, Liu X, Feng W, Kang X, Huang B, Liu J, & Zhang XC (2013). Structure of the YajR transporter suggests a transport mechanism based on the conserved motif A. Proc Natl Acad Sci USA 110 :14664-14669. PubMed Id: 23950222. doi:10.1073/pnas.1308127110.
*MdfA multidrug resistance transporter in complex with deoxycholate: Escherichia coli* B Bacteria, 2.0 Å** in complex with chloramphenicol, 2.45 Å: 4ZOW in complex with LDAO, 2.20 Å: 4ZP2	4ZP0	Data File Jmol Viewer 4ZP0 4ZP2 4ZOW	Heng et al. (2015). Heng J, Zhao Y, Liu M, Liu Y, Fan J, Wang X, Zhao Y, & Zhang XC (2015). Substrate-bound structure of the E. coli multidrug resistance transporter MdfA. Cell Res 25 9:1060-1073. PubMed Id: 26238402. doi:10.1038/cr.2015.94.
*MdfA multidrug resistance transporter, E26T/D34M/A150E mutant in the presence of chloramphenicol, pH 5: Escherichia coli* B Bacteria, 2.00 Å** pH 8, 2.10 Å: 6VS0 Deoxycholate-bound, 3.00 Å: 6VS1 LDAO-bound, 3.00 Å: 6VS2	6VRZ	Data File Jmol Viewer 6VRZ 6VS2 6VS0 6VS1	Wu et al. (2020). Wu HH, Symersky J, & Lu M (2020). Structure and mechanism of a redesigned multidrug transporter from the Major Facilitator Superfamily. Sci Rep 10 1. PubMed Id: 32127561. doi:10.1038/s41598-020-60332-8.
*MdfA multidrug resistance transporter, I239T/G354E mutant in complex with LDAO: Escherichia coli* B Bacteria, 2.20 Å** in complex with MV, 2.80 Å: 6OOP in complex with DXC, 3.00 Å: 6OOQ	6OOM	Data File Jmol Viewer 6OOM 6OOQ 6OOP	Wu et al. (2019). Wu HH, Symersky J, & Lu M (2019). Structure of an engineered multidrug transporter MdfA reveals the molecular basis for substrate recognition. Commun Biol 2 :210. PubMed Id: 31240248. doi:10.1038/s42003-019-0446-y.
*MdfA multidrug resistance transporter in outward open conformation: Escherichia coli* B Bacteria, 3.40 Å**	6GV1	Data File Jmol Viewer 6GV1	Nagarathinam et al. (2018). Nagarathinam K, Nakada-Nakura Y, Parthier C, Terada T, Juge N, Jaenecke F, Liu K, Hotta Y, Miyaji T, Omote H, Iwata S, Nomura N, Stubbs MT, & Tanabe M (2018). Outward open conformation of a Major Facilitator Superfamily multidrug/H⁺ antiporter provides insights into switching mechanism. Nat Commun 9 1:4005. PubMed Id: 30275448. doi:10.1038/s41467-018-06306-x.
*MdfA multidrug resistance transporter, Q131R/L339E mutant: Escherichia coli* B Bacteria, 2.20 Å**	6EUQ	Data File Jmol Viewer 6EUQ	Zomot et al. (2018). Zomot E, Yardeni EH, Vargiu AV, Tam HK, Malloci G, Ramaswamy VK, Perach M, Ruggerone P, Pos KM, & Bibi E (2018). A New Critical Conformational Determinant of Multidrug Efflux by an MFS Transporter. J Mol Biol 430 9:1368-1385. PubMed Id: 29530612. doi:10.1016/j.jmb.2018.02.026.
*GLUT1 glucose transporter (N45T/E329Q mutant): Homo sapiens* E Eukaryota (expressed in Trichoplusia ni), 3.17 Å** GLUT1 is a uniporter that catalyzes movement of glucose down its concentration gradient	4PYP	Data File Jmol Viewer 4PYP	Deng et al. (2014). Deng D, Xu C, Sun P, Wu J, Yan C, Hu M, & Yan N (2014). Crystal structure of the human glucose transporter GLUT1. Nature 510 :121-125. PubMed Id: 24847886. doi:10.1038/nature13306.
*GLUT1 glucose transporter, Wild-type in complex with cytochalasin: Homo sapiens* E Eukaryota (expressed in S. cerevisiae), 3.0 Å** in complex with GLUT-i1 inhibitor, 2.9 Å: 5EQG in complex with GLUT-i2 inhibitor, 2.99 Å: 5EQH	5EQI	Data File Jmol Viewer 5EQI 5EQG 5EQH	Kapoor et al. (2016). Kapoor K, Finer-Moore JS, Pedersen BP, Caboni L, Waight A, Hillig RC, Bringmann P, Heisler I, Müller T, Siebeneicher H, & Stroud RM (2016). Mechanism of inhibition of human glucose transporter GLUT1 is conserved between cytochalasin B and phenylalanine amides. Proc Natl Acad Sci USA 113 :4711-4716. PubMed Id: 27078104. doi:10.1073/pnas.1603735113.
*GLUT1 glucose transporter (SLC2A1), inward conformation: Homo sapiens* E Eukaryota (expressed in S. cerevisiae), 2.4 Å**	6THA	Data File Jmol Viewer 6THA	Custódio et al. (2021). Custódio TF, Paulsen PA, Frain KM, & Pedersen BP (2021). Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family. Life Sci Alliance 4 4:e202000858. PubMed Id: 33536238. doi:10.26508/lsa.202000858.
*GLUT3 glucose transporter (N45T mutant) with bound D-glucose, outward-occluded conformation: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 1.50 Å** with exofacial inhibitor maltose in outward-occluded conformation, 2.4 Å: 4ZWB with exofacial inhibitor maltose in outward-open conformation, 2.6 Å: 4ZWC	4ZW9	Data File Jmol Viewer 4ZW9 4ZWC 4ZWB	Deng et al. (2015). Deng D, Sun P, Yan C, Ke M, Jiang X, Xiong L, Ren W, Hirata K, Yamamoto M, Fan S, & Yan N (2015). Molecular basis of ligand recognition and transport by glucose transporters. Nature 526 :391-396. PubMed Id: 26176916. doi:10.1038/nature14655.
*GLUT3 glucose transporter in complex with C3361: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.30 Å**	7CRZ	Data File Jmol Viewer 7CRZ	Huang et al. (2021). Huang J, Yuan Y, Zhao N, Pu D, Tang Q, Zhang S, Luo S, Yang X, Wang N, Xiao Y, Zhang T, Liu Z, Sakata-Kato T, Jiang X, Kato N, Yan N, & Yin H (2021). Orthosteric-allosteric dual inhibitors of PfHT1 as selective antimalarial agents. Proc Natl Acad Sci U S A 118 3:e2017749118. PubMed Id: 33402433. doi:10.1073/pnas.2017749118.
*GLUT3 glucose transporter with bound glucose, exofacial state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.10 Å** with bound exofacial inhibitor SA47, 2.30 Å 7SPS	7SPT	Data File Jmol Viewer 7SPT 7SPS	Wang et al. (2022). Wang N, Zhang S, Yuan Y, Xu H, Defossa E, Matter H, Besenius M, Derdau V, Dreyer M, Halland N, He KH, Petry S, Podeschwa M, Tennagels N, Jiang X, & Yan N (2022). Molecular basis for inhibiting human glucose transporters by exofacial inhibitors. Nat Commun 13 1:2632. PubMed Id: 35552392. doi:10.1038/s41467-022-30326-3.
*GLUT4 glucose transporter with bound cytochalasin B in lipid nanodiscs: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.25 Å** cryo-EM structure with bound cytochalasin B in detergent micelles, 3.31 Å 7WSN	7WSM	Data File Jmol Viewer 7WSM 7WSN	Yuan et al. (2022). Yuan Y, Kong F, Xu H, Zhu A, Yan N, & Yan C (2022). Cryo-EM structure of human glucose transporter GLUT4. Nat Commun 13 1:2671. PubMed Id: 35562357. doi:10.1038/s41467-022-30235-5.
*GLUT5 fructose transporter, open-inward conformation: Bos taurus* E Eukaryota, 3.20 Å**	4YB9	Data File Jmol Viewer 4YB9	Nomura et al. (2015). Nomura N, Verdon G, Kang HJ, Shimamura T, Nomura Y, Sonoda Y, Hussien SA, Qureshi AA, Coincon M, Sato Y, Abe H, Nakada-Nakura Y, Hino T, Arakawa T, Kusano-Arai O, Iwanari H, Murata T, Kobayashi T, Hamakubo T, Kasahara M, Iwata S, & Drew D (2015). Structure and mechanism of the mammalian fructose transporter GLUT5. Nature 526 :397-401. PubMed Id: 26416735. doi:10.1038/nature14909.
*GLUT5 fructose transporter, open-outward conformation: Rattus norvegicus* E Eukaryota, 3.27 Å**	4YBQ	Data File Jmol Viewer 4YBQ	Nomura et al. (2015). Nomura N, Verdon G, Kang HJ, Shimamura T, Nomura Y, Sonoda Y, Hussien SA, Qureshi AA, Coincon M, Sato Y, Abe H, Nakada-Nakura Y, Hino T, Arakawa T, Kusano-Arai O, Iwanari H, Murata T, Kobayashi T, Hamakubo T, Kasahara M, Iwata S, & Drew D (2015). Structure and mechanism of the mammalian fructose transporter GLUT5. Nature 526 :397-401. PubMed Id: 26416735. doi:10.1038/nature14909.
*Hexose transporter (HT1): Plasmodium falciparum* E Eukaryota (expressed in S. cerevisiae), 3.65 Å**	6RW3	Data File Jmol Viewer 6RW3	Qureshi et al. (2020). Qureshi AA, Suades A, Matsuoka R, Brock J, McComas SE, Nji E, Orellana L, Claesson M, Delemotte L, & Drew D (2020). The molecular basis for sugar import in malaria parasites. Nature 578 7794:321-325. PubMed Id: 31996846. doi:10.1038/s41586-020-1963-z.
*Ferroportin (FPN) Fe²⁺ transporter (SLC40A1) analog, outward-facing conformation: Bdellovibrio bacteriovarus* B Bacteria (expressed in E. coli), 2.20 Å** outward-facing Fe²⁺ soaked, 3.00 Å: 5AYM inward-facing, 3.00 Å: 5AYO	5AYN	Data File Jmol Viewer 5AYN 5AYO 5AYM	Taniguchi et al. (2015). Taniguchi R, Kato HE, Font J, Deshpande CN, Wada M, Ito K, Ishitani R, Jormakka M, & Nureki O (2015). Outward- and inward-facing structures of a putative bacterial transition-metal transporter with homology to ferroportin. Nat Commun 6 :8545. PubMed Id: 26461048. doi:10.1038/ncomms9545.
*Ferroportin (FPN) Fe²⁺ transporter (SLC40A1), apo protein in nanodisc: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 3.20 Å** cryo-EM structure bound to hepcidin and cobalt, 2.50 Å: 6WBV x-ray: anti-ferroportin Fab45D8, 2.10 Å: 6W4V	6W4S	Data File Jmol Viewer 6W4S 6WBV 6W4V	Billesbølle et al. (2020). Billesbølle CB, Azumaya CM, Kretsch RC, Powers AS, Gonen S, Schneider S, Arvedson T, Dror RO, Cheng Y, & Manglik A (2020). Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms. Nature 586 7831:807-811. PubMed Id: 32814342. doi:10.1038/s41586-020-2668-z.
*Ferroportin (FPN) Fe2+ transporter (SLC40A1), bound to Ca²⁺ in nanodisc: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.00 Å** cryo-EM structure	8DL6	Data File Jmol Viewer 8DL6	Shen et al. (2023). Shen J, Wilbon AS, Zhou M, & Pan Y (2023). Mechanism of Ca2+ transport by ferroportin. Elife 12 :e82947. PubMed Id: 36648329. doi:10.7554/eLife.82947.
*Ferroportin (FPN) Fe²⁺ transporter (SLC40A1) in complex with Fab: Carlito syrichta* E Eukaryota (expressed in Trichoplusia ni), 3.00 Å** cryo-EM structure in the presence of hepcidin, 3.40 Å: 6WIK	6VYH	Data File Jmol Viewer 6VYH 6WIK	Pan et al. (2020). Pan Y, Ren Z, Gao S, Shen J, Wang L, Xu Z, Yu Y, Bachina P, Zhang H, Fan X, Laganowsky A, Yan N, & Zhou M (2020). Structural basis of ion transport and inhibition in ferroportin. Nat Commun 11 1:5686. PubMed Id: 33173040. doi:10.1038/s41467-020-19458-6.
*Sugar Transport Protein 10 in complex with glucose in the outward occluded state: Arabidopsis thaliana* E Eukaryota (expressed in S. cerevisiae), 2.4 Å**	6H7D	Data File Jmol Viewer 6H7D	Paulsen et al. (2019). Paulsen PA, Custódio TF, & Pedersen BP (2019). Crystal structure of the plant symporter STP10 illuminates sugar uptake mechanism in monosaccharide transporter superfamily. Nat Commun 10 1:407. PubMed Id: 30679446. doi:10.1038/s41467-018-08176-9.
*Sugar Transport Protein 10, outward occluded conformation: Arabidopsis thaliana* E Eukaryota (expressed in S. cerevisiae), 1.81 Å** inward open conformation, 2.64 Å 7AAR	7AAQ	Data File Jmol Viewer 7AAQ 7AAR	Bavnhøj et al. (2021). Bavnhøj L, Paulsen PA, Flores-Canales JC, Schiøtt B, & Pedersen BP (2021). Molecular mechanism of sugar transport in plants unveiled by structures of glucose/H⁺ symporter STP10. Nat Plants 7 10:1409-1419. PubMed Id: 34556835. doi:10.1038/s41477-021-00992-0.
*LtaA Lipoteichoic acids flippase: Staphylococcus aureus* B Bacteria (expressed in E. coli), 3.30 Å**	6S7V	Data File Jmol Viewer 6S7V	Zhang et al. (2020). Zhang B, Liu X, Lambert E, Mas G, Hiller S, Veening JW, & Perez C (2020). Structure of a proton-dependent lipid transporter involved in lipoteichoic acids biosynthesis. Nat Struct Mol Biol 27 6:561-569. PubMed Id: 32367070. doi:10.1038/s41594-020-0425-5.
*LmrP multidrug transporter, ligand bound outward-open state: Lactococcus lactis* B Bacteria, 2.90 Å**	6T1Z	Data File Jmol Viewer 6T1Z	Debruycker et al. (2020). Debruycker V, Hutchin A, Masureel M, Ficici E, Martens C, Legrand P, Stein RA, Mchaourab HS, Faraldo-Gómez JD, Remaut H, & Govaerts C (2020). An embedded lipid in the multidrug transporter LmrP suggests a mechanism for polyspecificity. Nat Struct Mol Biol 27 9:829-835. PubMed Id: 32719456. doi:10.1038/s41594-020-0464-y.
*NupG nucleoside proton symporter: Escherichia coli* B Bacteria, 3.00 Å** D323A mutant, 3.00 Å: 7DLA	7DL9	Data File Jmol Viewer 7DL9 7DLA	Wang et al. (2021). Wang C, Xiao Q, Duan H, Li J, Zhang J, Wang Q, Guo L, Hu J, Sun B, & Deng D (2021). Molecular basis for substrate recognition by the bacterial nucleoside transporter NupG. J Biol Chem 296 :100479. PubMed Id: 33640454. doi:10.1016/j.jbc.2021.100479.
*SotB Drug:Proton Antiporter-1 (DHA1), in the inward-occluded conformation: Escherichia coli* B Bacteria, 3.06 Å** inward open conformation, 3.38 Å: 6KKJ inward open conformation (H115A mutant), 3.50 Å: 6KKK inward conformation (H115N mutant), 2.65 Å: 6KKL	6KKI	Data File Jmol Viewer 6KKI 6KKK 6KKL 6KKJ	Xiao et al. (2021). Xiao Q, Sun B, Zhou Y, Wang C, Guo L, He J, & Deng D (2021). Visualizing the nonlinear changes of a drug-proton antiporter from inward-open to occluded state. Biochem Biophys Res Commun 534 :272-278. PubMed Id: 33280821. doi:10.1016/j.bbrc.2020.11.096.
*MFSD2A lysolipid transporter in complex with LPC-18:3: Gallus gallus* E Eukaryota (expressed in Spodoptera frugiperda), 3.03 Å** cryo-EM structure	7MJS	Data File Jmol Viewer 7MJS	Cater et al. (2021). Cater RJ, Chua GL, Erramilli SK, Keener JE, Choy BC, Tokarz P, Chin CF, Quek DQY, Kloss B, Pepe JG, Parisi G, Wong BH, Clarke OB, Marty MT, Kossiakoff AA, Khelashvili G, Silver DL, & Mancia F (2021). Structural basis of omega-3 fatty acid transport across the blood-brain barrier. Nature 595 7866:315-319. PubMed Id: 34135507. doi:10.1038/s41586-021-03650-9.
*MFSD2A lysolipid transporter: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure	7N98	Data File Jmol Viewer 7N98	Wood et al. (2021). Wood CAP, Zhang J, Aydin D, Xu Y, Andreone BJ, Langen UH, Dror RO, Gu C, & Feng L (2021). Structure and mechanism of blood-brain-barrier lipid transporter MFSD2A. Nature 596 7872:444-448. PubMed Id: 34349262. doi:10.1038/s41586-021-03782-y.
*MFSD2A lysolipid transporter in complex with syncytin-2 (SYNC2): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure	7OIX	Data File Jmol Viewer 7OIX	Martinez-Molledo et al. (2022). Martinez-Molledo M, Nji E, & Reyes N (2022). Structural insights into the lysophospholipid brain uptake mechanism and its inhibition by syncytin-2. Nat Struct Mol Biol 29 6:604-612. PubMed Id: 35710838. doi:10.1038/s41594-022-00786-8.
*MFSD2A lysolipid transporter, isoform B, inward open state, with bound lysolipid 1A,2B,3C merged conformation: Danio rerio* E Eukaryota (expressed in S. frugiperda), 2.90 Å** cryo-EM structure lysolipid 1A conformation, 3.30 Å: 8D2U lysolipid 1B conformation, 4.10 Å: 8D2V lysolipid 2B conformation, 3.40 Å: 8D2W lysolipid 3C conformation, 3.40 Å: 8D2X ligand-free conformation, 3.40 Å: 8D2T	8D2S	Data File Jmol Viewer 8D2S 8D2V 8D2X 8D2W 8D2U 8D2T	Nguyen et al. (2023). Nguyen C, Lei HT, Lai LTF, Gallenito MJ, Mu X, Matthies D, & Gonen T (2023). Lipid flipping in the omega-3 fatty-acid transporter. Nat Commun 14 1:2571. PubMed Id: 37156797. doi:10.1038/s41467-023-37702-7.
*OxlT oxalate:formate antiporter (OFA) in complex with fab, oxalate-bound occluded form: Oxalobacter formigenes* B Bacteria (expressed in E. coli), 3.00 Å** in complex with Fv, ligand-free outward-facing form, 3.30 Å, 8HPJ	8HPK	Data File Jmol Viewer 8HPK 8HPJ	Jaunet-Lahary et al. (2023). Jaunet-Lahary T, Shimamura T, Hayashi M, Nomura N, Hirasawa K, Shimizu T, Yamashita M, Tsutsumi N, Suehiro Y, Kojima K, Sudo Y, Tamura T, Iwanari H, Hamakubo T, Iwata S, Okazaki KI, Hirai T, & Yamashita A (2023). Structure and mechanism of oxalate transporter OxlT in an oxalate-degrading bacterium in the gut microbiota. Nat Commun 14 1:1730. PubMed Id: 37012268. doi:10.1038/s41467-023-36883-5.
*SUC1 sucrose transporter: Arabidopsis thaliana* E Eukaryota (expressed in S. cerevisiae), 2.68 Å** x-ray structure	8BB6	Data File Jmol Viewer 8BB6	Bavnhøj et al. (2023). Bavnhøj L, Driller JH, Zuzic L, Stange AD, Schiøtt B, & Pedersen BP (2023). Structure and sucrose binding mechanism of the plant SUC1 sucrose transporter. Nat Plants 9 6:938-950. PubMed Id: 37188854. doi:10.1038/s41477-023-01421-0.
Solute Sodium Symporter (SSS) Family
*SGLT Sodium-Galactose Transporter: Vibrio parahaemolyticus* B Bacteria (expressed in E. coli), 2.70 Å** Galactose-bound inward-occuluded conformation	3DH4	Data File Jmol Viewer 3DH4	Faham et al. (2008). Faham S, Watanabe A, Besserer GM, Cascio D, Specht A, Hirayama BA, Wright EM, & Abramson J (2008). The crystal structure of a sodium galactose transporter reveals mechanistic insights into Na+/sugar symport. Science 321 :810-814. PubMed Id: 18599740.
*SGLT Sodium Galactose Transporter, K294A mutant: Vibrio parahaemolyticus* B Bacteria (expressed in E. coli), 2.70 Å** inward-open conformation	2XQ2	Data File Jmol Viewer 2XQ2	Watanabe et al. (2010). Watanabe A, Choe S, Chaptal V, Rosenberg JM, Wright EM, Grabe M, & Abramson J (2010). The mechanism of sodium and substrate release from the binding pocket of vSGLT. Nature 468 :988-991. PubMed Id: 21131949.
*SGLT1 Sodium-Glucose Transporter: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure	7SL8	Data File Jmol Viewer 7SL8	Han et al. (2022). Han L, Qu Q, Aydin D, Panova O, Robertson MJ, Xu Y, Dror RO, Skiniotis G, & Feng L (2022). Structure and mechanism of the SGLT family of glucose transporters. Nature 601 7892:274-279. PubMed Id: 34880492. doi:10.1038/s41586-021-04211-w.
*SGLT1-MAP17 complex bound with LX2761: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure	7WMV	Data File Jmol Viewer 7WMV	Niu et al. (2022). Niu Y, Cui W, Liu R, Wang S, Ke H, Lei X, & Chen L (2022). Structural mechanism of SGLT1 inhibitors. Nat Commun 13 1:6440. PubMed Id: 36307403. doi:10.1038/s41467-022-33421-7.
*SGLT1-MAP17 complex bound with 4D4FDG, occluded conformation: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.26 Å** cryo-EM structure complex in the apo state in the inward-facing conformation, 3.48 Å: 7YNK complex in occluded conformation with bound substrate AMG, 3.33 Å: 7YNJ	7YNI	Data File Jmol Viewer 7YNI 7YNK 7YNJ	Cui et al. (2023). Cui W, Niu Y, Sun Z, Liu R, & Chen L (2023). Structures of human SGLT in the occluded state reveal conformational changes during sugar transport. Nat Commun 14 1:2920. PubMed Id: 37217492. doi:10.1038/s41467-023-38720-1.
*SMCT1 Sodium-monocarboxylate Transporter: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure	7SL9	Data File Jmol Viewer 7SL9	Han et al. (2022). Han L, Qu Q, Aydin D, Panova O, Robertson MJ, Xu Y, Dror RO, Skiniotis G, & Feng L (2022). Structure and mechanism of the SGLT family of glucose transporters. Nature 601 7892:274-279. PubMed Id: 34880492. doi:10.1038/s41586-021-04211-w.
*SGLT2 Sodium-Glucose Transporter in complex with MAP17: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.95 Å** cryo-EM structure	7VSI	Data File Jmol Viewer 7VSI	Niu et al. (2022). Niu Y, Liu R, Guan C, Zhang Y, Chen Z, Hoerer S, Nar H, & Chen L (2022). Structural basis of inhibition of the human SGLT2-MAP17 glucose transporter. Nature 601 7892:280-284. PubMed Id: 34880493. doi:10.1038/s41586-021-04212-9.
*SiaT sialic acid transporter (SeMet): Proteus mirabilis* B Bacteria (expressed in E. coli), 1.95 Å** native, 2.26 Å: 5NVA	5NV9	Data File Jmol Viewer 5NV9 5NVA	Wahlgren et al. (2018). Wahlgren WY, Dunevall E, North RA, Paz A, Scalise M, Bisignano P, Bengtsson-Palme J, Goyal P, Claesson E, Caing-Carlsson R, Andersson R, Beis K, Nilsson UJ, Farewell A, Pochini L, Indiveri C, Grabe M, Dobson RCJ, Abramson J, Ramaswamy S, & Friemann R (2018). Substrate-bound outward-open structure of a Na⁺-coupled sialic acid symporter reveals a new Na⁺ site. Nat Commun 9 1. PubMed Id: 29717135. doi:10.1038/s41467-018-04045-7.
*SbtA-SbtB Na⁺ dependent bicarbonate transporter complex bound to HCO₃^-: Synechocystis sp. PCC 6803 substr. Kazusa* B Bacteria, 3.20 Å** bound to AMP, 2.70 Å: 7EGK	7EGL	Data File Jmol Viewer 7EGL 7EGK	Fang et al. (2021). Fang S, Huang X, Zhang X, Zhang M, Hao Y, Guo H, Liu LN, Yu F, & Zhang P (2021). Molecular mechanism underlying transport and allosteric inhibition of bicarbonate transporter SbtA. Proc Natl Acad Sci U S A 118 22:e2101632118. PubMed Id: 34031249. doi:10.1073/pnas.2101632118.
PIN-FORMED (PIN) Auxin Efflux Carriers and Related Proteins PIN-FORMED refers to the phenotype of the pin1 mutant. Plants with this mutation fail to flower properly.
*PIN1 auxin exporter, apo state: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure IAA-bound state, 3.20 Å: 7Y9V NPA-bound state, 3.30 Å: 7Y9U	7Y9T	Data File Jmol Viewer 7Y9T 7Y9V 7Y9U	Yang et al. (2022). Yang Z, Xia J, Hong J, Zhang C, Wei H, Ying W, Sun C, Sun L, Mao Y, Gao Y, Tan S, Friml J, Li D, Liu X, & Sun L (2022). Structural insights into auxin recognition and efflux by Arabidopsis PIN1. Nature 609 7927:611-615. PubMed Id: 35917925. doi:10.1038/s41586-022-05143-9.
*Auxin transporter PIN3, apo state: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure NPA bound state, 2.62 Å: 7WKW IAA bound state, 2.93 Å: 7XXB	7WKS	Data File Jmol Viewer 7WKS 7WKW 7XXB	Su et al. (2022). Su N, Zhu A, Tao X, Ding ZJ, Chang S, Ye F, Zhang Y, Zhao C, Chen Q, Wang J, Zhou CY, Guo Y, Jiao S, Zhang S, Wen H, Ma L, Ye S, Zheng SJ, Yang F, Wu S, & Guo J (2022). Structures and mechanisms of the Arabidopsis auxin transporter PIN3. Nature 609 7927:616-621. PubMed Id: 35917926. doi:10.1038/s41586-022-05142-w.
*Auxin transporter PIN8, apo form: Arabidopsis thaliana* E Eukaryota (expressed in Saccharomyces cerevisiae), 2.89 Å** cryo-EM structure Outward-facing auxin-bound form, 3.18 Å: 7QPA Inward-facing NPA bound form, 3.44 Å: 7QPC	7QP9	Data File Jmol Viewer 7QP9 7QPA 7QPC	Ung et al. (2022). Ung KL, Winkler M, Schulz L, Kolb M, Janacek DP, Dedic E, Stokes DL, Hammes UZ, & Pedersen BP (2022). Structures and mechanism of the plant PIN-FORMED auxin transporter. Nature 609 7927:605-610. PubMed Id: 35768502. doi:10.1038/s41586-022-04883-y.
CDP-Alcohol Phosphotransferases These enzymes facilitate the conjugation of polar headgroups to diacylglycerol lipid tails
*AF2299 CDP-alcohol phosphotransferase w. bound CMP: Archaeoglobus fulgidus* A Archaea (expressed in E. coli), 1.90 Å** with bound CDP, 2.10 Å: 4O6N with CDP-glycerol, 3.10 Å: 4Q7C	4O6M	Data File Jmol Viewer 4O6M 4Q7C 4O6N	Sciara et al. (2014). Sciara G, Clarke OB, Tomasek D, Kloss B, Tabuso S, Byfield R, Cohn R, Banerjee S, Rajashankar KR, Slavkovic V, Graziano JH, Shapiro L, & Mancia F (2014). Structural basis for catalysis in a CDP-alcohol phosphotransferase. Nat Commun 5 :4068. PubMed Id: 24923293. doi:10.1038/ncomms5068.
*CDP-alcohol phosphotransferase domain (DIPPS) with fused nucleotidyltransferase domain: Archaeoglobus fulgidus* B Bacteria (expressed in E. coli), 2.66 Å**	4MND	Data File Jmol Viewer 4MND	Nogly et al. (2014). Nogly P, Gushchin I, Remeeva A, Esteves AM, Borges N, Ma P, Ishchenko A, Grudinin S, Round E, Moraes I, Borshchevskiy V, Santos H, Gordeliy V, & Archer M (2014). X-ray structure of a CDP-alcohol phosphatidyltransferase membrane enzyme and insights into its catalytic mechanism. Nat Commun 5 4169. PubMed Id: 24942835. doi:10.1038/ncomms5169.
*Phosphatidylinositol-phosphate synthase with bound CDP-diacylglycerol: Renibacterium salmoninarum* B Bacteria (expressed in E. coli), 3.6 Å** without bound CDP-diacylglycerol, 2.5 Å: 5D92	5D91	Data File Jmol Viewer 5D91 5D92	Clarke et al. (2015). Clarke OB, Tomasek D, Jorge CD, Dufrisne MB, Kim M, Banerjee S, Rajashankar KR, Shapiro L, Hendrickson WA, Santos H, & Mancia F (2015). Structural basis for phosphatidylinositol-phosphate biosynthesis. Nat Commun 6 :8505. PubMed Id: 26510127. doi:10.1038/ncomms9505.
Insulin-Induced Gene Products: Insig Proteins These are components of the sterol regulatory element-binding protein (SREBP) pathway
*MvINS Insig homolog: Mycobacterium vanbaalenii PYR-1* B Bacteria (expressed in E. coli), 1.90 Å** bound to a bromine-derived 14C Diacylglycerol (DAG), 2.10 Å: 4XU5 cross-linked R77C trimer, 1.90 Å: 4XU6	4XU4	Data File Jmol Viewer 4XU4 4XU5 4XU6	Ren et al. (2015). Ren R, Zhou X, He Y, Ke M, Wu J, Liu X, Yan C, Wu Y, Gong X, Lei X, Yan SF, Radhakrishnan A, & Yan N (2015). PROTEIN STRUCTURE: Crystal structure of a mycobacterial Insig homolog provides insight into how these sensors monitor sterol levels. Science 349 6244:187-191. PubMed Id: 26160948. doi:10.1126/science.aab1091.
*Scap/Insig complex in the presence of 25-hydroxyl cholesterol: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.70 Å** cryo-EM structure	6M49	Data File Jmol Viewer 6M49	Yan et al. (2021). Yan R, Cao P, Song W, Qian H, Du X, Coates HW, Zhao X, Li Y, Gao S, Gong X, Liu X, Sui J, Lei J, Yang H, Brown AJ, Zhou Q, Yan C, & Yan N (2021). A structure of human Scap bound to Insig-2 suggests how their interaction is regulated by sterols. Science 371 6533:eabb2224. PubMed Id: 33446483. doi:10.1126/science.abb2224.
Sterol Reductases
*Δ¹⁴ Sterol reductase: Methylomicrobium alcaliphilum* B Bacteria (expressed in E. coli), 2.74 Å**	4QUV	Data File Jmol Viewer 4QUV	Li et al. (2015). Li X, Roberti R, & Blobel G (2015). Structure of an integral membrane sterol reductase from Methylomicrobium alcaliphilum. Nature 517 :104-107. PubMed Id: 25307054. doi:10.1038/nature13797.
*Steroid 5-alpha-reductase SRD5A: Proteobacteria bacterium* B Bacteria (expressed in Spodoptera frugiperda), 2.00 Å**	7C83	Data File Jmol Viewer 7C83	Han et al. (2021). Han Y, Zhuang Q, Sun B, Lv W, Wang S, Xiao Q, Pang B, Zhou Y, Wang F, Chi P, Wang Q, Li Z, Zhu L, Li F, Deng D, Chiang YC, Li Z, & Ren R (2021). Crystal structure of steroid reductase SRD5A reveals conserved steroid reduction mechanism. Nat Commun 12 1:449. PubMed Id: 33469028. doi:10.1038/s41467-020-20675-2.
HMG CoA Reductase 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR)
*HMG CoA Reductase (HMG CoA) in complex with UBIAD1, state 1: Cricetulus griseus* E Eukaryota (expressed in HEK293 cells), 3.23 Å** cryo-EM structure HMGCR-UBIAD1 Complex State 2, 3.33 Å: 8DJK	8DJM	Data File Jmol Viewer 8DJM 8DJK	Chen et al. (2022). Chen H, Qi X, Faulkner RA, Schumacher MM, Donnelly LM, DeBose-Boyd RA, & Li X (2022). Regulated degradation of HMG CoA reductase requires conformational changes in sterol-sensing domain. Nat Commun 13 1:4273. PubMed Id: 35879350. doi:10.1038/s41467-022-32025-5.
Sterol Isomerases
*Emopamil-Binding Protein (EBP) in complex with U18666A: Homo sapiens* E Eukaryota (expressed in HEK293s cells), 3.2 Å** in complex with tamoxifen, 3.53 Å: 6OHU	6OHT	Data File Jmol Viewer 6OHT 6OHU	Long et al. (2019). Long T, Hassan A, Thompson BM, McDonald JG, Wang J, & Li X (2019). Structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition. Nat Commun 10 1. PubMed Id: 31165728. doi:10.1038/s41467-019-10279-w.
Sterol-Sensing Domain (SSD) Proteins These proteins are involved in cholesterol trafficking in the cholesterol-uptake pathway
*Niemann-Pick C1 protein (NPC1): Homo sapiens E Eukaryota (expressed in 293 GnTI^- cells), 3.35 Å** NPC1* protein consists of NPC1 residues 314-1278. 5U73 supersedes 5I31	5U73	Data File Jmol Viewer 5U73	Li et al. (2016). Li X, Wang J, Coutavas E, Shi H, Hao Q, & Blobel G (2016). Structure of human Niemann-Pick C1 protein. Proc Natl Acad Sci USA 113 :8212-8217. PubMed Id: 27307437. doi:10.1073/pnas.1607795113.
*Niemann-Pick C1 protein, full-length: Homo sapiens* E Eukaryota (expressed in HEK 293F cells), 4.43 Å** cryo-EM structure in complex with the cleaved glycoprotein of Ebola virus, 6.56 Å: 5JNX	3JD8	Data File Jmol Viewer 3JD8 5JNX	Gong et al. (2016). Gong X, Qian H, Zhou X, Wu J, Wan T, Cao P, Huang W, Zhao X, Wang X, Wang P, Shi Y, Gao GF, Zhou Q, & Yan N (2016). Structural Insights into the Niemann-Pick C1 (NPC1)-Mediated Cholesterol Transfer and Ebola Infection. Cell 165 :1467-1478. PubMed Id: 27238017. doi:10.1016/j.cell.2016.05.022.
*Niemann-Pick C1 protein (NPC1): Homo sapiens E Eukaryota (expressed in 293 GnTI^- cells), 3.3 Å** NPC1* is residues 314-1278. This structure features well-resolved structure of the entire C-terminal luminal domain (CTD)	5U74	Data File Jmol Viewer 5U74	Li et al. (2017). Li X, Lu F, Trinh MN, Schmiege P, Seemann J, Wang J, & Blobel G (2017). 3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport. Proc Nat Acad Sci USA 114 :9116-9121. PubMed Id: 28784760. doi:10.1073/pnas.1711716114.
*Niemann-Pick C1 protein (NPC1) with bound itraconazole: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.02 Å** cryo-EM structure	6UOX	Data File Jmol Viewer 6UOX	Long et al. (2020). Long T, Qi X, Hassan A, Liang Q, De Brabander JK, & Li X (2020). Structural basis for itraconazole-mediated NPC1 inhibition. Nat Commun 11 1. PubMed Id: 31919352. doi:10.1038/s41467-019-13917-5.
*Niemann-Pick C1 protein (NPC1) in nanodiscs: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure in GDN micelles at pH 8.0, 3.00 Å: 6W5S in GDN micelles at pH 5.5, 3.70 Å: 6W5T in GDN micelles at pH 5.5, conformation b, 3.90 Å: 6W5U NPC1-NPC2 complex structure at pH 5.5, 4.00 Å: 6W5V	6W5R	Data File Jmol Viewer 6W5R 6W5V 6W5T 6W5S 6W5U	Qian et al. (2020). Qian H, Wu X, Du X, Yao X, Zhao X, Lee J, Yang H, & Yan N (2020). Structural Basis of Low-pH-Dependent Lysosomal Cholesterol Egress by NPC1 and NPC2. Cell 182 1:98-111.e18. PubMed Id: 32544384. doi:10.1016/j.cell.2020.05.020.
*Niemann-Pick C1 protein (NPC1), luminal domain C: Homo sapiens* B Bacteria (expressed in E. coli), 2.30 Å**	8EUS	Data File Jmol Viewer 8EUS	Odongo et al. (2023). Odongo L, Zadrozny KK, Diehl WE, Luban J, White JM, Ganser-Pornillos BK, Tamm LK, & Pornillos O (2023). Purification and structure of luminal domain C of human Niemann-Pick C1 protein. Acta Crystallogr F Struct Biol Commun 79 2:45-50. PubMed Id: 36748341. doi:10.1107/S2053230X23000705.
*Niemann-Pick type C protein NCR1: Saccharomyces cerevisiae* E Eukaryota, 3.5 Å** NPC2 sterol free, 2.8 Å: 6R4M NPC2 with bound sterol, 2.9 Å: 6R4N	6R4L	Data File Jmol Viewer 6R4L 6R4M 6R4N	Winkler et al. (2019). Winkler MBL, Kidmose RT, Szomek M, Thaysen K, Rawson S, Muench SP, Wüstner D, & Pedersen BP (2019). Structural Insight into Eukaryotic Sterol Transport through Niemann-Pick Type C Proteins. Cell 179 2:485-497.e18. PubMed Id: 31543266. doi:10.1016/j.cell.2019.08.038.
*Niemann-Pick C1-Like 1 (NPC1L1) cholesterol intracellular transporter protein: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.70 Å** cryo-EM structure in complex with an ezetimibe analog, 3.50 Å: 6V3H	6V3F	Data File Jmol Viewer 6V3F 6V3H	Huang et al. (2020). Huang CS, Yu X, Fordstrom P, Choi K, Chung BC, Roh SH, Chiu W, Zhou M, Min X, & Wang Z (2020). Cryo-EM structures of NPC1L1 reveal mechanisms of cholesterol transport and ezetimibe inhibition. Sci Adv 6 25:eabb1989. PubMed Id: 32596471. doi:10.1126/sciadv.abb1989.
*Niemann-Pick C1-Like 1 (NPC1L1) cholesterol intracellular transporter, apo form: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.03 Å** cryo-EM structure ΔN-NPC1L1-EZE, 3.58 Å 7DFZ ΔN-NPC1L1-CLR, 2.69 Å 7DFW	7DF8	Data File Jmol Viewer 7DF8 7DFZ 7DFW	Hu et al. (2021). Hu M, Yang F, Huang Y, You X, Liu D, Sun S, & Sui SF (2021). Structural insights into the mechanism of human NPC1L1-mediated cholesterol uptake. Sci Adv 7 29:eabg3188. PubMed Id: 34272236. doi:10.1126/sciadv.abg3188.
*Niemann-Pick C1-Like 1 (NPC1L1) cholesterol intracellular transporter: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.34 Å** cryo-EM structure with bound cholesterol, 3.58 Å, 7N4V W347R mutant, 3.33 Å, 7N4X	7N4U	Data File Jmol Viewer 7N4U 7N4V 7N4X	Long et al. (2021). Long T, Liu Y, Qin Y, DeBose-Boyd RA, & Li X (2021). Structures of dimeric human NPC1L1 provide insight into mechanisms for cholesterol absorption. Sci Adv 7 34:abh3997. PubMed Id: 34407950. doi:10.1126/sciadv.abh3997.
Fatty Acid Desaturases These enzymes maintain the cellular balance of saturated and monounsaturated lipids
*Stearoyl-coenzyme A desaturase (SCD1) in complex with substrate: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 3.25 Å**	4ZYO	Data File Jmol Viewer 4ZYO	Wang et al. (2015). Wang H, Klein MG, Zou H, Lane W, Snell G, Levin I, Li K, & Sang BC (2015). Crystal structure of human stearoyl-coenzyme A desaturase in complex with substrate. Nat Struct Mol Biol 22 :581-585. PubMed Id: 26098317. doi:10.1038/nsmb.3049.
*Stearoyl-coenzyme A desaturase (SCD1) in complex with substrate: Mus musculus* E Eukaryota (expressed in Trichoplusia ni), 2.61 Å**	4YMK	Data File Jmol Viewer 4YMK	Bai et al. (2015). Bai Y, McCoy JG, Levin EJ, Sobrado P, Rajashankar KR, Fox BG, & Zhou M (2015). X-ray structure of a mammalian stearoyl-CoA desaturase. Nature 252 :252-256. PubMed Id: 26098370. doi:10.1038/nature14549.
*Stearoyl-coenzyme A desaturase (SCD1) with diiron center: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.51 Å**	6WF2	Data File Jmol Viewer 6WF2	Shen et al. (2020). Shen J, Wu G, Tsai AL, & Zhou M (2020). Structure and Mechanism of a Unique Diiron Center in Mammalian Stearoyl-CoA Desaturase. J Mol Biol 432 18:5152-5161. PubMed Id: 32470559. doi:10.1016/j.jmb.2020.05.017.
Superfamily of K⁺ Transporters (SKT proteins)
*TrkH potassium ion transporter: Vibrio parahaemolyticus* B Bacteria (expressed in E. coli), 3.51 Å** Lacking a Na⁺/K⁺-ATPase, non-animal cells require two different systems for K⁺ uptake, one of which is the SKT family of proteins.	3PJZ	Data File Jmol Viewer 3PJZ	Cao et al. (2011). Cao Y, Jin X, Huang H, Derebe MG, Levin EJ, Kabaleeswaran V, Pan Y, Punta M, Love J, Weng J, Quick M, Ye S, Kloss B, Bruni R, Martinez-Hackert E, Hendrickson WA, Rost B, Javitch JA, Rajashankar KR, Jiang Y, & Zhou M (2011). Crystal structure of a potassium ion transporter, TrkH. Nature 471 :336-340. PubMed Id: 21317882.
*TrkH potassium ion transporter in complex with TrkA: Vibrio parahaemolyticus* B Bacteria (expressed in E. coli), 3.80 Å** TrkA Gating ring bound to ATP-gamma-S, 3.05 Å: 4J9V	4J9U	Data File Jmol Viewer 4J9U 4J9V	Cao et al. (2013). Cao Y, Pan Y, Huang H, Jin X, Levin EJ, Kloss B, & Zhou M (2013). Gating of the TrkH ion channel by its associated RCK protein TrkA. Nature 496 :317-322. PubMed Id: 23598339. doi:10.1038/nature12056.
*TrkH potassium ion transporter in complex with TrkA in complex with ATP: Vibrio parahaemolyticus* B Bacteria (expressed in E. coli), 2.97 Å** cryo-EM structure in complex with ADP, 3.53 Å: 6V4K with ATPγS, 3.80 Å: 6V4L	6V4J	Data File Jmol Viewer 6V4J 6V4L 6V4K	Zhang et al. (2020). Zhang H, Pan Y, Hu L, Hudson MA, Hofstetter KS, Xu Z, Rong M, Wang Z, Prasad BVV, Lockless SW, Chiu W, & Zhou M (2020). TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential. Nat Commun 11 1:547. PubMed Id: 31992706. doi:10.1038/s41467-019-14240-9.
*KtrAB potassium ion transporter: Bacillus subtilis* B Bacteria (expressed in E. coli), 3.50 Å** Square-shaped octameric structure of KtrA with ATP bound, 3.24 Å: 4J90 Diamond-shaped octameric structure of KtrA with ADP bound, 2.93 Å: 4J91	4J7C	Data File Jmol Viewer 4J7C 4J91 4J90	Vieira-Pires et al. (2013). Vieira-Pires RS, Szollosi A, & Morais-Cabral JH (2013). The structure of the KtrAB potassium transporter. Nature 496 :323-328. PubMed Id: 23598340. doi:10.1038/nature12055.
*Potassium-importing KdpFABC membrane complex: Escherichia coli* B Bacteria, 2.9 Å** The complex has a channel-like subunit (KdpA) and a pump-like P-type ATPase (KdpB).	5MRW	Data File Jmol Viewer 5MRW	Huang et al. (2017). Huang CS, Pedersen BP, & Stokes DL (2017). Crystal structure of the potassium-importing KdpFABC membrane complex. Nature 546 :681-685. PubMed Id: 28636601. doi:10.1038/nature22970.
*Potassium-importing KdpFABC membrane complex, E1 state w K⁺: Escherichia coli* B Bacteria, 3.38 Å** cryo-EM structure E1-ATP state, 3.23 Å: 7LC3 E2-P state with BeF₃, 3.70 Å: 7LC6 E2P_i state with BeF₃ and K⁺, 3.00 Å: 7BH2 E2P_i state with MgF₄, 2.90 Å: 7BGY	7BH1	Data File Jmol Viewer 7BH1 7LC6 7BH2 7BGY 7LC3	Sweet et al. (2021). Sweet ME, Larsen C, Zhang X, Schlame M, Pedersen BP, & Stokes DL (2021). Structural basis for potassium transport in prokaryotes by KdpFABC. Proc Natl Acad Sci U S A 118 29:e2105195118. PubMed Id: 34272288. doi:10.1073/pnas.2105195118.
*Potassium-importing KdpFABC membrane complex, E1-ATP conformation loaded with K⁺: Escherichia coli* B Bacteria, 3.10 Å** cryo-EM structure Rb-loaded structure, 3.20 Å 7NNP	7NNL	Data File Jmol Viewer 7NNL 7NNP	Silberberg et al. (2021). Silberberg JM, Corey RA, Hielkema L, Stock C, Stansfeld PJ, Paulino C, & Hänelt I (2021). Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC. Nat Commun 12 1:5098. PubMed Id: 34429416. doi:10.1038/s41467-021-25242-x.
*Potassium-importing KdpFABC membrane complex in the E1-ATP early state under turnover conditions: Escherichia coli* B Bacteria, 3.50 Å** cryo-EM structure E1P tight state, 3.40 Å: 7ZRE E1P-ADP state, 3.10 Å: 7ZRK E2P state, 4.00 Å: 7ZRL E1P-ADP state, 3.70 Å: 7ZRM E1P tight state with bound inhibitor orthovanadate, 3.30 Å: 7ZRD E1 apo tight state, 3.40 Å: 7ZRH E1 apo open 1 state, 3.50 Å: 7ZRI E1 apo open 2 state, 3.70 Å: 7ZRJ	7ZRG	Data File Jmol Viewer 7ZRG 7ZRM 7ZRD 7ZRL 7ZRH 7ZRJ 7ZRI 7ZRE 7ZRK	Silberberg et al. (2022). Silberberg JM, Stock C, Hielkema L, Corey RA, Rheinberger J, Wunnicke D, Dubach VRA, Stansfeld PJ, Hänelt I, & Paulino C (2022). Inhibited KdpFABC transitions into an E1 off-cycle state. Elife 11 :80988. PubMed Id: 36255052. doi:10.7554/eLife.80988.
Membrane-Integral Pyrophosphatases (M-PPases) Ion-Translocating Pyrophosphatases Link Pyrophosphate (PP_i) Hydrolysis to Sodium or Proton Pumping V-ATPases and H⁺-PPases coexist on plant vacuolar membranes
*H⁺-translocating M-PPase: Vigna radiata* E Eukaryota (expressed in S. cerevisiae), 2.35 Å** Structure shows protein in complex with the non-hydrolysable substrate analog imidodiphosphate (IDP). The protein has 16 TM helices.	4A01	Data File Jmol Viewer 4A01	Lin et al. (2012). Lin SM, Tsai JY, Hsiao CD, Huang YT, Chiu CL, Liu MH, Tung JY, Liu TH, Pan RL, & Sun YJ (2012). Crystal structure of a membrane-embedded H⁺-translocating pyrophosphatase. Nature 484 :399-403. PubMed Id: 22456709. doi:10.1038/nature10963.
*H⁺-translocating M-PPase: Vigna radiata* E Eukaryota (expressed in S. crevisiae), 3.5 Å**	5GPJ	Data File Jmol Viewer 5GPJ	Li et al. (2016). Li KM, Wilkinson C, Kellosalo J, Tsai JY, Kajander T, Jeuken LJ, Sun YJ, & Goldman A (2016). Membrane pyrophosphatases from Thermotoga maritima and Vigna radiata suggest a conserved coupling mechanism. Nat Commun 7 :13596. PubMed Id: 27922000. doi:10.1038/ncomms13596.
*H⁺-translocating M-PPase with two bound phosphates: Vigna radiata* E Eukaryota (expressed in S. cerevisiae), 2.30 Å** E301Q mutant, 2.49 Å: 6AFT L555M mutant, 2.80 Å: 6AFU L555K mutant, 2.70 Å: 6AFV T228D mutant, 2.18 Å: 6AFW E225A mutant, 2.30 Å: 6AFX E225S mutant, 2.40 Å: 6AFY E225H mutant, 2.48 Å: 6AFZ	6AFS	Data File Jmol Viewer 6AFS 6AFU 6AFZ 6AFV 6AFY 6AFW 6AFX 6AFT	Tsai et al. (2019). Tsai JY, Tang KZ, Li KM, Hsu BL, Chiang YW, Goldman A, & Sun YJ (2019). Roles of the Hydrophobic Gate and Exit Channel in Vigna radiata Pyrophosphatase Ion Translocation. J Mol Biol 431 8:1619-1632. PubMed Id: 30878480. doi:10.1016/j.jmb.2019.03.009.
*Na⁺-translocating M-PPase with metal ions in active site: Thermotoga maritima* B Bacteria (expressed in S. cerevisiae), 2.60 Å** In complex with phosphate and magnesium, 4.00 Å: 4AV6	4AV3	Data File Jmol Viewer 4AV3 4AV6	Kellosalo et al. (2012). Kellosalo J, Kajander T, Kogan K, Pokharel K, & Goldman A (2012). The structure and catalytic cycle of a sodium-pumping pyrophosphatase. Science 337 :473-476. PubMed Id: 22837527. doi:10.1126/science.1222505.
*Na⁺-translocating M-PPase in complex with imidodiphosphate and magnesium, and with bound sodium ion: Thermotoga maritima* E Eukaryota (expressed in S. cerevisiae), 3.49 Å** in complex with tungstate and magnesium, 4.0 Å: 5LZR	5LZQ	Data File Jmol Viewer 5LZQ 5LZR	Li et al. (2016). Li KM, Wilkinson C, Kellosalo J, Tsai JY, Kajander T, Jeuken LJ, Sun YJ, & Goldman A (2016). Membrane pyrophosphatases from Thermotoga maritima and Vigna radiata suggest a conserved coupling mechanism. Nat Commun 7 :13596. PubMed Id: 27922000. doi:10.1038/ncomms13596.
Vacuolar Iron Transporter (VIT) Family These proteins transport cytoplasmic ferrous ions into vacuoles
*iron transporter VIT1 with zinc ions: Eucalyptus grandis* E Eukaryota (expressed in Saccharomyces cerevisiae), 2.70 Å** with cobalt ion, 3.50 Å 6IU4 cytoplasmic metal binding domain with zinc ions, 2.25 Å 6IU5 cytoplasmic metal binding domain with nickel ions, 2.90 Å 6IU6 cytoplasmic metal binding domain with cobalt ions, 2.70 Å 6IU8 cytoplasmic metal binding domain with iron ions, 3.00 Å6IU9	6IU3	Data File Jmol Viewer 6IU3 6IU4 6IU9 6IU5 6IU6 6IU8	Kato et al. (2019). Kato T, Kumazaki K, Wada M, Taniguchi R, Nakane T, Yamashita K, Hirata K, Ishitani R, Ito K, Nishizawa T, & Nureki O (2019). Crystal structure of plant vacuolar iron transporter VIT1. Nat Plants 5 3:308-315. PubMed Id: 30742036. doi:10.1038/s41477-019-0367-2.
Bacterial V-type ATPase Also called A-type ATPase
*Rotor of V-type Na⁺-ATPase: Enterococcus hirae* B Bacteria, 2.1 Å**	2BL2	Data File Jmol Viewer 2BL2	Murata et al. (2005). Murata T, Yamato I, Kakinuma Y, Leslie AG, & Walker JE (2005). Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae. Science 308 :654-659. PubMed Id: 15802565.
*V-ATPase central-axis DF complex: Enterococcus hirae* B Bacteria (expressed in Cell-free synthesis), 2.00 Å**	3AON	Data File Jmol Viewer 3AON	Saijo et al. (2011). Saijo S, Arai S, Hossain KM, Yamato I, Suzuki K, Kakinuma Y, Ishizuka-Katsura Y, Ohsawa N, Terada T, Shirouzu M, Yokoyama S, Iwata S, & Murata T (2011). Crystal structure of the central axis DF complex of the prokaryotic V-ATPase. Proc Natl Acad Sci USA 108 :19955-19960. PubMed Id: 22114184. doi:10.1073/pnas.1108810108.
*A₃B₃ Assembly of V-type Na⁺-ATPase (nucleotide-free): Enterococcus hirae* B Bacteria (expressed in Cell-free synthesis), 2.80 Å** Nucleotide-bound, 3.40 Å: 3VR3 Nucleotide-free, 2.17 Å: 3VR4 Nucleotide-free, 3.90 Å: 3VR5 Nucleotide-bound, 2.68 Å: 3VR6	3VR2	Data File Jmol Viewer 3VR2 3VR4 3VR3 3VR5 3VR6	Arai et al. (2013). Arai S, Saijo S, Suzuki K, Mizutani K, Kakinuma Y, Ishizuka-Katsura Y, Ohsawa N, Terada T, Shirouzu M, Yokoyama S, Iwata S, Yamato I, & Murata T (2013). Rotation mechanism of Enterococcus hirae V₁-ATPase based on asymmetric crystal structures. Nature 493 :703-707. PubMed Id: 23334411. doi:10.1038/nature11778.
*V₁ rotary motor, 2 ADP-bound state: Enterococcus hirae* B Bacteria (expressed in E. coli), 3.25 Å** 3 ADP-bound state, 3.02 Å: 5KNC P_i-bound state, 2.89 Å: 5KND	5KNB	Data File Jmol Viewer 5KNB 5KND 5KNC	Suzuki et al. (2016). Suzuki K, Mizutani K, Maruyama S, Shimono K, Imai FL, Muneyuki E, Kakinuma Y, Ishizuka-Katsura Y, Shirouzu M, Yokoyama S, Yamato I, & Murata T (2016). Crystal structures of the ATP-binding and ADP-release dwells of the V₁ rotary motor. Nat Commun 7 :13235. PubMed Id: 27807367. doi:10.1038/ncomms13235.
*V₁-ATPase atomic model derived from Cryo-EM reconstructions.: Thermus thermophilus* B Bacteria, 9.7 Å**	3J0J	Data File Jmol Viewer 3J0J	Lau & Rubinstein (2012). Lau WC & Rubinstein JL (2012). Subnanometre-resolution structure of the intact Thermus thermophilus H⁺-driven ATP synthase. Nature 481 :214-218. PubMed Id: 22178924. doi:10.1038/nature10699.
*V₁-ATPase Complex (V-ATPase soluble domain) with bound nucleotide: Thermus thermophilus* B Bacteria, 4.51 Å** Without nucleotide, 4.80 Å: 3A5D	3A5C	Data File Jmol Viewer 3A5C 3A5D	Numoto et al. (2009). Numoto N, Hasegawa Y, Takeda K, & Miki K (2009). Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V₁-ATPase. EMBO Rep 10 :1228-1234. PubMed Id: 19779483.
*A₃B₃ complex of V₁-ATPase: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.8 Å**	3GQB	Data File Jmol Viewer 3GQB	Maher et al. (2009). Maher MJ, Akimoto S, Iwata M, Nagata K, Hori Y, Yoshida M, Yokoyama S, Iwata S, & Yokoyama K (2009). Crystal structure of A₃B₃complex of V-ATPase from Thermus thermophilus. EMBO J 28 :3771-3779. PubMed Id: 19893485.
*Peripheral stalk of H⁺-dependent V-ATP Synthase: Thermus thermophilus* B Bacteria (expressed in E. coli), 3.10 Å** So-called PS1 structure.	3K5B	Data File Jmol Viewer 3K5B	Lee et al. (2010). Lee LK, Stewart AG, Donohoe M, Bernal RA, & Stock D (2010). The structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase. Nat Struct Mol Biol 17 :373-378. PubMed Id: 20173764.
*Peripheral stalk of H⁺-dependent V-ATP Synthase: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.25 Å** So-called PS2 structure.	3V6I	Data File Jmol Viewer 3V6I	Stewart et al. (2012). Stewart AG, Lee LK, Donohoe M, Chaston JJ, & Stock D (2012). The dynamic stator stalk of rotary ATPases. Nature Commun 3 :687. PubMed Id: 22353718. doi:10.1038/ncomms1693.
*A₃B₃DF complex of V₁-ATPase: Thermus thermophilus* B Bacteria, 3.90 Å**	3W3A	Data File Jmol Viewer 3W3A	Nagamatsu et al. (2013). Nagamatsu Y, Takeda K, Kuranaga T, Numoto N, & Miki K (2013). Origin of Asymmetry at the Intersubunit Interfaces of V₁-ATPase from Thermus thermophilus. J Mol Biol 425 15:2699-2708. PubMed Id: 23639357. doi:10.1016/j.jmb.2013.04.022.
*Complete V-type ATPase, rotation state 1: Thermus thermophilus* B Bacteria, 5 Å** cryo-EM structure peripheral domain (rotational state 1) 4.7 Å: 5Y5Y rotational state 2, 6.7 Å: 5Y5Z rotational state 3, 7.5 Å: 5Y60	5Y5X	Data File Jmol Viewer 5Y5X 5Y5Y 5Y5Z 5Y60	Nakanishi et al. (2018). Nakanishi A, Kishikawa JI, Tamakoshi M, Mitsuoka K, & Yokoyama K (2018). Cryo EM structure of intact rotary H⁺-ATPase/synthase from Thermus thermophilus. Nat Commun 9 1:89. PubMed Id: 29311594. doi:10.1038/s41467-017-02553-6.
*V/A—type ATPase in nanodiscs, rotational state 1: Thermus thermophilus* B Bacteria, 3.25 Å** cryo-EM structure in state 1L, 3.8 Å: 6ROZ in state 1R, 4.29 Å: 6R10 in state 2, 3.61 Å: 6R0W in state 3, 3.91 Å: 6R0Y	6QUM	Data File Jmol Viewer 6QUM 6R0W 6ROZ 6R0Y 6R10	Zhou & Sazanov (2019). Zhou L, & Sazanov LA (2019). Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. Science 365 6455. PubMed Id: 31439765. doi:10.1126/science.aaw9144.
*V/A—type ATPase in nanodiscs, soluble domain: Thermus thermophilus* B Bacteria, 3.50 Å** cryo-EM structure membrane-embedded V_o domain, 3.93 Å: 6YL9	6LY8	Data File Jmol Viewer 6LY8 6YL9	Kishikawa et al. (2020). Kishikawa JI, Nakanishi A, Furuta A, Kato T, Namba K, Tamakoshi M, Mitsuoka K, & Yokoyama K (2020). Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductance. Elife 9 . PubMed Id: 32639230. doi:10.7554/eLife.56862.
*V₁EG of V/A-ATPase, state 1-1: Thermus thermophilus* B Bacteria, 3.10 Å** cryo-EM structure Nucleotide-free V₁EG domain, state 1-2, 3.10 Å: 7VAJ Nucleotide-free V₁EG domain, state 2, 4.70 Å: 7VAK V₁EG, high ATP state 1-1, 3.10 Å: 7VAL V₁EG, high ATP, state 1-2, 3.20 Å: 7VAM V₁EG, high ATP, state 2-1, 3.00 Å: 7VAN V₁EG, high ATP, state 2-2, 3.40 Å: 7VAO V₁EG, high ATP, state 2-2, 3.00 Å: 7VAP V₁EG, high ATP, state 3-2, 3.60 Å: 7VAQ V₁EG, low ATP, state 1-1, 2.90 Å: 7VAR V₁EG, low ATP, state 1-2, 3.00 Å: 7VAS V₁EG, low ATP, state 2-1, 3.20 Å: 7VAT V₁EG, low ATP, state 2-2, 3.30 Å: 7VAU V₁EG, low ATP, state 3, 2.80 Å: 7VAV V₁EG, saturated ATP-γ-S condition, state1-1, 2.70 Å : 7VAW V₁EG, saturated ATP-γ-S condition, state1-2, 2.90 Å : 7VAX V₁EG, saturated ATP-γ-S condition, state 2, 3.30 Å: 7VAY V₁EG, saturated ATP-γ-S condition, state 3, 3.60 Å: 7VB0	7VAI	Data File Jmol Viewer 7VAI 7VAK 7VAW 7VAT 7VAY 7VAO 7VAL 7VAM 7VAJ 7VAN 7VAV 7VAX 7VAS 7VAQ 7VAP 7VAU 7VB0 7VAR	Kishikawa et al. (2022). Kishikawa J, Nakanishi A, Nakano A, Saeki S, Furuta A, Kato T, Mistuoka K, & Yokoyama K (2022). Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases. Nat Commun 13 1:1213. PubMed Id: 35260556. doi:10.1038/s41467-022-28832-5.
*Peripheral stalk of H⁺-dependent V-ATP Synthase: Pyrococcus horikoshii* A Archaea (expressed in E. coli), 3.65 Å**	4DT0	Data File Jmol Viewer 4DT0	Balakrishna et al. (2012). Balakrishna AM, Hunke C, & Grüber G (2012). The structure of subunit E of the Pyrococcus horikoshii OT3 A-ATP synthase gives insight into the elasticity of the peripheral stalk. J Mol Biol 420 :155-183. PubMed Id: 22516614. doi:10.1016/j.jmb.2012.04.012.
Vacuolar ATPase (V-ATPase) Eukaryotic V-ATPases
*Heterotrimeric EGChead Peripheral Stalk Complex: Saccharomyces cerevisiae* E Eukaryota, 2.90 Å** Second conformation, 2.82 Å: 4EFA	4DL0	Data File Jmol Viewer 4DL0 4EFA	Oot et al. (2012). Oot RA, Huang LS, Berry EA, & Wilkens S (2012). Crystal Structure of the Yeast Vacuolar ATPase Heterotrimeric EGC(head) Peripheral Stalk Complex. Structure 20 :1881-1892. PubMed Id: 23000382. doi:10.1016/j.str.2012.08.020.
*Subunits DF complex: Saccharomyces cerevisiae* E Eukaryota (expressed in E. coli), 3.18 Å**	4RND	Data File Jmol Viewer 4RND	Balakrishna et al. (2015). Balakrishna AM, Basak S, Manimekalai MS, & Grüber G (2015). Crystal structure of subunits D and F in complex gives insight into energy transmission of the eukaryotic V-ATPase from Saccharomyces cerevisiae. J Biol Chem 290 :3183-3196. PubMed Id: 25505269. doi:10.1074/jbc.M114.622688.
*Complete V-ATPase by cryo-EM, state 1: Saccharomyces cerevisiae* E Eukaryota, 6.9 Å** state 2, 7.6 Å: 3J9U state 3, 8.3 Å: 3J9V Cryo-EM maps in EM Data Bank: EMD-6284, EMD-6285, & EMD-6286	3J9T	Data File Jmol Viewer 3J9T 3J9U 3J9V	Zhao et al. (2015). Zhao J, Benlekbir S, & Rubinstein JL (2015). Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase. Nature 521 :241-245. PubMed Id: 25971514. doi:10.1038/nature14365.
*Complete V-ATPase by cryo-EM, state 1: Saccharomyces cerevisiae* E Eukaryota (expressed in E. coli), 4.20 Å** cryo-EM structure state 2, 4.80 Å 7FDB state 3, 6.60 Å 7FDC Oxr1 bound, 3.80 Å 7FDE	7FDA	Data File Jmol Viewer 7FDA 7FDB 7FDE 7FDC	Khan et al. (2022). Khan MM, Lee S, Couoh-Cardel S, Oot RA, Kim H, Wilkens S, & Roh SH (2022). Oxidative stress protein Oxr1 promotes V-ATPase holoenzyme disassembly in catalytic activity-independent manner. EMBO J 41 3:e109360. PubMed Id: 34918374. doi:10.15252/embj.2021109360.
*Complete V₁-ATPase in auto-inhibited state by cryo-EM: Saccharomyces cerevisiae* E Eukaryota, 6.2 Å** 7 Å structure, 5BW9	5D80	Data File Jmol Viewer 5D80 5BW9	Oot et al. (2016). Oot RA, Kane PM, Berry EA, & Wilkens S (2016). Crystal structure of yeast V₁-ATPase in the auto-inhibited state. EMBO J 35 :1694-1706. PubMed Id: 27295975. doi:10.15252/embj.201593447.
*membrane-embedded V_O motor of V-ATPase: Saccharomyces cerevisiae* E Eukaryota, 3.9 Å** cryo-EM structure	5TJ5	Data File Jmol Viewer 5TJ5	Mazhab-Jafari et al. (2016). Mazhab-Jafari MT, Rohou A, Schmidt C, Bueler SA, Benlekbir S, Robinson CV, & Rubinstein JL (2016). Atomic model for the membrane-embedded V_O motor of a eukaryotic V-ATPase. Nature 539 :118-122. PubMed Id: 27776355. doi:10.1038/nature19828.
*ATPase V_o proton channel reconstituted in nano-discs: Saccharomyces cerevisiae* E Eukaryota, 3.5 Å** cryo-EM structure	6C6L	Data File Jmol Viewer 6C6L	Roh et al. (2018). Roh SH, Stam NJ, Hryc CF, Couoh-Cardel S, Pintilie G, Chiu W, & Wilkens S (2018). The 3.5-Å CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase V_o Proton Channel. Mol Cell 69 6:993-1004.e3. PubMed Id: 29526695. doi:10.1016/j.molcel.2018.02.006.
*V-ATPase, Vph1-V_O isoform: Saccharomyces cerevisiae* E Eukaryota, 3.2 Å** cryo-EM structure Stv1-V_O isoform, 3.1 Å: 6O7U Stv1-V₁V_O, State 1, 6.6 Å: 6O7V Stv1-V_O, 3.1 Å: 6O7U Stv1-V₁V_O State 1, 6.6 Å: 6O7V Stv1-V₁V_O State 2, 7 Å: 6O7W Stv1-V₁V_O State 3, 8.7 Å: 6O7X	6O7T	Data File Jmol Viewer 6O7T 6O7V 6O7X 6O7U 6O7W	Vasanthakumar et al. (2019). Vasanthakumar T, Bueler SA, Wu D, Beilsten-Edmands V, Robinson CV, & Rubinstein JL (2019). Structural comparison of the vacuolar and Golgi V-ATPases from Saccharomyces cerevisiae. Proc Natl Acad Sci USA 116 15:7272-7277. PubMed Id: 30910982. doi:10.1073/pnas.1814818116.
*V_O motor of V-ATPase in complex with 1 VopQ toxin: Saccharomyces cerevisiae & Vibrio parahaemolyticus (VopQ)* E Eukaryota (expressed in E. coli), 3.10 Å** cryo-EM structure complex with 2 VopQ toxins, 3.20 Å: 6PE5	6PE4	Data File Jmol Viewer 6PE4 6PE5	Peng et al. (2020). Peng W, Casey AK, Fernandez J, Carpinone EM, Servage KA, Chen Z, Li Y, Tomchick DR, Starai VJ, & Orth K (2020). A distinct inhibitory mechanism of the V-ATPase by Vibrio VopQ revealed by cryo-EM. Nat. Struct. Mol. Biol. 27 6:589-597. PubMed Id: 32424347. doi:10.1038/s41594-020-0429-1.
*V-ATPase V_o complex in state 3: Saccharomyces cerevisiae* E Eukaryota, 2.70 Å** cryo-EM structure state3 prime, 3.60 Å: 6M0S	6M0R	Data File Jmol Viewer 6M0R 6M0S	Roh et al. (2020). Roh SH, Shekhar M, Pintilie G, Chipot C, Wilkens S, Singharoy A, & Chiu W (2020). Cryo-EM and MD infer water-mediated proton transport and autoinhibition mechanisms of Vo complex. Sci Adv 6 41. PubMed Id: 33028525. doi:10.1126/sciadv.abb9605.
*V-ATPase V_o complex with bound bafilomycin A1: Saccharomyces cerevisiae* E Eukaryota, 3.20 Å** cryo-EM structure with bound archazolid A, 2.80 Å 7TAP	7TAO	Data File Jmol Viewer 7TAO 7TAP	Keon et al. (2022). Keon KA, Benlekbir S, Kirsch SH, Müller R, & Rubinstein JL (2022). Cryo-EM of the Yeast V_O Complex Reveals Distinct Binding Sites for Macrolide V-ATPase Inhibitors. ACS Chem Biol 17 3:619-628. PubMed Id: 35148071. doi:10.1021/acschembio.1c00894.
*V-ATPase, composite model rotational state 1 bound to ADP & SidK: Rattus norvegicus & Legionella pneumophila (SidK)* E Eukaryota, 3.9 Å** cryo-EM structure rotational state 2 bound to ADP and SidK, 4 Å: 6VQ7 rotational state 3 bound to ADP and SidK, 3.9 Å: 6VQ8 Focused refinement models' PDB codes are listed in Table S6 of the paper.	6VQ6	Data File Jmol Viewer 6VQ6 6VQ8 6VQ7	Abbas et al. (2020). Abbas YM, Wu D, Bueler SA, Robinson CV, & Rubinstein JL (2020). Structure of V-ATPase from the mammalian brain. Science 367 6483:1240-1246. PubMed Id: 32165585. doi:10.1126/science.aaz2924.
*V-ATPase, intact, state 1: Bos taurus* E Eukaryota, 3.37 Å** cryo-EM structure state 2, 3.79 Å: 6XBY	6XBW	Data File Jmol Viewer 6XBW 6XBY	Wang et al. (2020). Wang R, Long T, Hassan A, Wang J, Sun Y, Xie XS, & Li X (2020). Cryo-EM structures of intact V-ATPase from bovine brain. Nat Commun 11 1:3921. PubMed Id: 32764564. doi:10.1038/s41467-020-17762-9.
*V-ATPase with bound bafilomycin A1: Bos taurus* E Eukaryota, 3.62 Å** cryo-EM structure	7KHR	Data File Jmol Viewer 7KHR	Wang et al. (2021). Wang R, Wang J, Hassan A, Lee CH, Xie XS, & Li X (2021). Molecular basis of V-ATPase inhibition by bafilomycin A1. Nat Commun 12 1:1782. PubMed Id: 33741963. doi:10.1038/s41467-021-22111-5.
*V-ATPase complete structure, state 1 with SidK and ADP: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure in state 2 with SidK and ADP, 3.40 Å: 6WM3 in state 3 with SidK and ADP, 3.60 Å: 6WM4 V1 region in state 1 (focused refinement), 2.90 Å: 6WLZ Vo region in state 1 (focused refinement), 3.00 Å: 6WLW	6WM2	Data File Jmol Viewer 6WM2 6WLZ 6WM4 6WM3 6WLW	Wang et al. (2020). Wang L, Wu D, Robinson CV, Wu H, & Fu TM (2020). Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly. Mol Cell 80 3:501-511.e3. PubMed Id: 33065002. doi:10.1016/j.molcel.2020.09.029.
*V-ATPase complex,with mEAK7: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.08 Å** cryo-EM structure V1 region of bovine V-ATPase in complex with human mEAK7 (focused refinement), 3.73 Å: 7UNE	7UNF	Data File Jmol Viewer 7UNF 7UNE	Wang et al. (2022). Wang R, Qin Y, Xie XS, & Li X (2022). Molecular basis of mEAK7-mediated human V-ATPase regulation. Nat Commun 13 1:3272. PubMed Id: 35672408. doi:10.1038/s41467-022-30899-z.
*V-ATPase with SidK, Rotary State 1: Sus scrofa* E Eukaryota, 3.70 Å** cryo-EM structure with mEAK7 and SidK, Rotary state 2, 3.50 Å: 7U8O with SidK, Rotary State 2, 4.10 Å: 7U8Q with SidK, Rotary State 3, 3.80 Å: 7U8R	7U8P	Data File Jmol Viewer 7U8P 7U8Q 7U8R 7U8O	Tan et al. (2022). Tan YZ, Abbas YM, Wu JZ, Wu D, Keon KA, Hesketh GG, Bueler SA, Gingras AC, Robinson CV, Grinstein S, & Rubinstein JL (2022). CryoEM of endogenous mammalian V-ATPase interacting with the TLDc protein mEAK-7. Life Sci Alliance 5 11:e202201527. PubMed Id: 35794005. doi:10.26508/lsa.202201527.
Flagellar Motor Proteins
*MotAB stator units: Campylobacter jejuni* B Bacteria (expressed in E. coli), 3.10 Å** cryo-EM structure unplugged MotAB, 2.98 Å: 6YKP protonation mimic of unplugged MotAB, 3.00 Å: 6YKR	6YKM	Data File Jmol Viewer 6YKM 6YKR 6YKP	Santiveri et al. (2020). Santiveri M, Roa-Eguiara A, Kühne C, Wadhwa N, Hu H, Berg HC, Erhardt M, & Taylor NMI (2020). Structure and Function of Stator Units of the Bacterial Flagellar Motor. Cell 183 1:244-257.e16. PubMed Id: 32931735. doi:10.1016/j.cell.2020.08.016.
*MotAB stator units: Clostridium sporogenes* B Bacteria (expressed in E. coli), 3.40 Å** cryo-EM structure	6YSF	Data File Jmol Viewer 6YSF	Deme et al. (2020). Deme JC, Johnson S, Vickery O, Aron A, Monkhouse H, Griffiths T, James RH, Berks BC, Coulton JW, Stansfeld PJ, & Lea SM (2020). Structures of the stator complex that drives rotation of the bacterial flagellum. Nat Microbiol 5 12:1553-1564. PubMed Id: 32929189. doi:10.1038/s41564-020-0788-8.
*MotAB stator units: Bacillus subtilis* B Bacteria (expressed in E. coli), 3.50 Å** cryo-EM structure	6YSL	Data File Jmol Viewer 6YSL	Deme et al. (2020). Deme JC, Johnson S, Vickery O, Aron A, Monkhouse H, Griffiths T, James RH, Berks BC, Coulton JW, Stansfeld PJ, & Lea SM (2020). Structures of the stator complex that drives rotation of the bacterial flagellum. Nat Microbiol 5 12:1553-1564. PubMed Id: 32929189. doi:10.1038/s41564-020-0788-8.
*flagellar LP ring: Salmonella enterica* B Bacteria, 3.50 Å** cryo-EM structure	7CLR	Data File Jmol Viewer 7CLR	Yamaguchi et al. (2021). Yamaguchi T, Makino F, Miyata T, Minamino T, Kato T, & Namba K (2021). Structure of the molecular bushing of the bacterial flagellar motor. Nat Commun 12 1:4469. PubMed Id: 34294704. doi:10.1038/s41467-021-24715-3.
*MotA stator unit: Aquifex aeolicus* B Bacteria (expressed in E. coli), 3.40 Å** cryo-EM structure	8GQY	Data File Jmol Viewer 8GQY	Nishikino et al. (2022). Nishikino T, Takekawa N, Tran DP, Kishikawa JI, Hirose M, Onoe S, Kojima S, Homma M, Kitao A, Kato T, & Imada K (2022). Structure of MotA, a flagellar stator protein, from hyperthermophile. Biochem Biophys Res Commun 631 :78-85. PubMed Id: 36179499. doi:10.1016/j.bbrc.2022.09.072.
F-type ATPase
*F₁-ATPase from bovine heart mitochondria: Bos taurus* E Eukaryota, 2.8 Å**	1BMF	Data File Jmol Viewer 1BMF	Abrahams et al. (1994). Abrahams JP, Leslie AG, Lutter R, & Walker JE (1994). Structure at 2.8 Å resolution of F₁-ATPase from bovine heart mitochondria. Nature 370 :621-628. PubMed Id: 8065448.
*F₁-ATPase complexed with antibiotic inhibitor aurovertin B: Bos taurus* E Eukaryota, 3.10 Å**	1COW	Data File Jmol Viewer 1COW	van Raaij et al. (1996). van Raaij MJ, Abrahams JP, Leslie AG, & Walker JE (1996). The structure of bovine F₁-ATPase complexed with the antibiotic inhibitor aurovertin B. Proc Natl Acad Sci USA 93 :6913-6917. PubMed Id: 8692918.
*F₁-ATPase complexed with peptide antibiotic efrapeptin: Bos taurus* E Eukaryota, 3.10 Å**	1EFR	Data File Jmol Viewer 1EFR	Abrahams et al. (1996). Abrahams JP, Buchanan SK, Van Raaij MJ, Fearnley IM, Leslie AG, & Walker JE (1996). The structure of bovine F₁-ATPase complexed with the peptide antibiotic efrapeptin. Proc Natl Acad Sci USA 93 :9420-9424. PubMed Id: 8790345.
*F₁-ATPase complexed with azide: Bos taurus* E Eukaryota, 1.95 Å**	2CK3	Data File Jmol Viewer 2CK3	Bowler et al. (2006). Bowler MW, Montgomery MG, Leslie AG, & Walker JE (2006). How azide inhibits ATP hydrolysis by the F-ATPases. Proc Natl Acad Sci USA 103 :8646-8649. PubMed Id: 16728506.
*F₁-ATPase, Ground State Structure: Bos taurus* E Eukaryota, 1.90 Å**	2JDI	Data File Jmol Viewer 2JDI	Bowler et al. (2007). Bowler MW, Montgomery MG, Leslie AG, & Walker JE (2007). Ground state structure of F₁-ATPase from bovine heart mitochondria at 1.9 Å resolution. J Biol Chem 282 :14238-14242. PubMed Id: 17350959.
*ATP Synthase Extrinsic Region: Bos taurus* E Eukaryota, 3.2 Å**	2WSS	Data File Jmol Viewer 2WSS	Rees et al. (2009). Rees DM, Leslie AG, Walker JE (2009). The structure of the membrane extrinsic region of bovine ATP synthase. Proc Natl Acad Sci USA 106 :21597-21601. PubMed Id: 19995987.
*F₁-ATPase inhibited by AMP-PNP and ADP in the presence of thiophosphate: Bos taurus* E Eukaryota, 3.10 Å** inhibited by three copies of the inhibitor protein IF₁ crystallised in the presence of thiophosphate, 3.30 Å: 4Z1M	4YXW	Data File Jmol Viewer 4YXW 4Z1M	Bason et al. (2015). Bason JV, Montgomery MG, Leslie AG, & Walker JE (2015). How release of phosphate from mammalian F₁-ATPase generates a rotary substep. Proc Natl Acad Sci USA 112 :6009-6014. PubMed Id: 25918412. doi:10.1073/pnas.1506465112.
*F₁F_o ATP synthase, F₁-peripheral stalk domain, state 1: Bos taurus* E Eukaryota (expressed in E. coli), 3.23 Å** cryo-EM structure F_o domain, 3.61 Å: 6ZBB rotor domain, state 3, 3.66 Å: 6ZIK stator domain, state 3, 6.02 Å: 6ZIU F₁-peripheral stalk domain, state 2, 3.29 Å: 6Z1R rotor domain, state 1, 3.49 Å: 6ZG7 stator domain, state 1, 4.33 Å: 6ZIQ ATP synthase monomer state 1 (combined), 4.00 Å: 6ZPO F₁c₈-peripheral stalk domain, state 3, 3.47 Å: 6Z1U rotor domain state 2, 3.49 Å: 6ZG8 stator domain, state 2, 3.49 Å: 6ZIT monomer state 2 (combined), 3.29 Å: 6ZQM monomer state 3 (combined), 4.00 Å: 6ZQN Sus scrofa F_o domain, 3.94 Å: 6ZMR Sus scrofa F_o domain, 6.20 Å: 6ZNA	6YY0	Data File Jmol Viewer 6YY0 6ZMR 6ZIU 6Z1U 6ZQM 6ZIK 6ZG7 6ZIT 6ZIQ 6ZG8 6ZPO 6ZBB 6ZNA 6ZQN 6Z1R	Spikes et al. (2020). Spikes TE, Montgomery MG, & Walker JE (2020). Structure of the dimeric ATP synthase from bovine mitochondria. Proc Natl Acad Sci U S A 117 38:23519-23526. PubMed Id: 32900941. doi:10.1073/pnas.2013998117.
*F₁F_o-ATPase dimer, state1:state1: Bos taurus* E Eukaryota (expressed in E. coli), 9.20 Å** cryo-EM structure state1:state2, 11.9 Å 7AJC state1:state3, 9.00 Å 7AJD state1:state3, 9.40 Å 7AJE state2:state2, 8.45 Å 7AJF state2:state3, 10.7 Å 7AJG state3:state1, 9.70 Å 7AJH state3:state2, 11.4 Å 7AJI state3:state3, 13.1 Å 7AJJ	7AJB	Data File Jmol Viewer 7AJB 7AJD 7AJH 7AJF 7AJC 7AJJ 7AJI 7AJE 7AJG	Spikes et al. (2021). Spikes TE, Montgomery MG, & Walker JE (2021). Interface mobility between monomers in dimeric bovine ATP synthase participates in the ultrastructure of inner mitochondrial membranes. Proc Natl Acad Sci U S A 118 8:e2021012118. PubMed Id: 33542155. doi:10.1073/pnas.2021012118.
*F₁-c-ring (c₈) complex: Bos taurus* E Eukaryota, 3.50 Å**	2XND	Data File Jmol Viewer 2XND	Watt et al. (2010). Watt IN, Montgomery MG, Runswick MJ, Leslie AG, & Walker JE (2010). Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria. Proc Natl Acad Sci USA 107 :16823-16827. PubMed Id: 20847295. doi:10.1073/pnas.1011099107.
*F₁F_o ATP synthase, subunit C: Escherichia coli* B Bacteria, NMR Structure**	1A91	Data File Jmol Viewer 1A91 F1F0 ATPsynthase Subunit C	Girvin et al. (1998). Girvin ME, Rastogi VK, Abildgaard F, Markley JL, & Fillingame RH (1998). Solution structure of the transmembrane H⁺-transporting subunit c of the F₁F₀ ATP synthase. Biochemistry 37 :8817-8824. PubMed Id: 9636021. doi:10.1021/bi980511m.
*F₁F_o ATP synthase, cryo-EM structure, state 1: Escherichia coli* B Bacteria, 6.9 Å** state 2, 7.77 Å: 5T4P state 3, 8.53 Å: 5T4Q	5T4O	Data File Jmol Viewer 5T4O 5T4P 5T4Q	Sobti et al. (2016). Sobti M, Smits C, Wong AS, Ishmukhametov R, Stock D, Sandin S, & Stewart AG (2016). Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states. Elife 5 :e21598. PubMed Id: 28001127. doi:10.7554/eLife.21598.
*F₁F_o synthase, ADP state 1A: Escherichia coli* B Bacteria, 3.10 Å** cryo-EM structure state 1B, 3.30 Å: 6OQS state 1C, 3.10 Å: 6OQT state 1D, 3.20 Å: 6OQU state 1E, 3.30 Å: 6PQV state 2A, 3.40 Å: 6WNQ state 2B, 3.30 Å: 6OQV state 3A, 3.10 Å: 6OQW state 3B, 3.30 Å: 6WNR ADP, substate 3A F_ofocussed, 3.30 Å: 6VWK	6OQR	Data File Jmol Viewer 6OQR 6WNR 6OQU 6OQT 6OQW 6OQS 6WNQ 6OQV 6VWK 6PQV	Sobti et al. (2020). Sobti M, Walshe JL, Wu D, Ishmukhametov R, Zeng YC, Robinson CV, Berry RM, & Stewart AG (2020). Cryo-EM structures provide insight into how E. coli F₁F_o ATP synthase accommodates symmetry mismatch. Nat Commun 11 1. PubMed Id: 32457314. doi:10.1038/s41467-020-16387-2.
*ATP synthase (F-ATPase), State 1: Ogataea angusta* E Eukaryota, 7.0 Å** cryo-EM structure State 2, 7.8 Å: 5LQY State 3, 7.9 Å: 5LQX	5LQZ	Data File Jmol Viewer 5LQZ 5LQY 5LQX	Vinothkumar et al. (2016). Vinothkumar KR, Montgomery MG, Liu S, & Walker JE (2016). Structure of the mitochondrial ATP synthase from Pichia angusta determined by electron cryo-microscopy. Proc Natl Acad Sci USA 113 :12709-12714. PubMed Id: 27791192. doi:10.1073/pnas.1615902113.
*ATP synthase (F₁c₁₀): Saccharomyces cerevisiae* E Eukaryota, 3.9 Å** NOTE: X-ray structure is a C-alpha model derived from composite of 1BMF, 1A91, & 1AQT	1QO1	Data File Jmol Viewer 1QO1 1AQT 1BMF 1A91 F1F0 ATPsynthase Subunit C	Stock et al. (1999). Stock S, Leslie AGW, & Walker JE (1999). Molecular architecture of rotary motor in ATP synthase. Science 286 :1700-1705. PubMed Id: 10576729.
*ATP synthase (F₁c₁₀), pH 8.3: Saccharomyces cerevisiae* E Eukaryota, 2.00 Å** The structure reveals the open conformation. pH 5.5, 2.00 Å: 3UD0 pH 5.5 reacted with DCCD, 2.00 Å: 3U32 pH 6.1, 2.50 Å: 3U2Y	3U2F	Data File Jmol Viewer 3U2F 3U2Y 3UD0 3U32	Symersky et al. (2012). Symersky J, Pagadala V, Osowski D, Krah A, Meier T, Faraldo-Gómez JD, & Mueller DM (2012). Structure of the c₁₀ ring of the yeast mitochondrial ATP synthase in the open conformation. Nature Struc Mol Biol 19 :485-491. PubMed Id: 22504883. doi:10.1038/nsmb.2284.
*ATP Synthase c₁₀ ring with bound oligomycin: Saccharomyces cerevisiae* E Eukaryota, 1.90 Å**	4F4S	Data File Jmol Viewer 4F4S	Symersky et al. (2012). Symersky J, Osowski D, Walters DE, & Mueller DM (2012). Oligomycin frames a common drug-binding site in the ATP synthase. Proc Natl Acad Sci USA 109 :13961-13965. PubMed Id: 22869738. doi:10.1073/pnas.1207912109.
*F₁-c-ring (c₁₀) complex: Saccharomyces cerevisiae* E Eukaryota, 3.43 Å**	2WPD	Data File Jmol Viewer 2WPD	Dautant et al. (2010). Dautant A, Velours J, & Giraud MF (2010). Crystal structure of the Mg·ADP-inhibited state of the yeast F₁c₁₀-ATP synthase. J Biol Chem 285 :29502-29510. PubMed Id: 20610387. doi:10.1074/jbc.M110.124529.
*dimeric F_O of ATP synthase: Saccharomyces cerevisiae* E Eukaryota, 3.6 Å** cryo-EM structure F₁F_O dimer model 6B2Z	6B2Z	Data File Jmol Viewer 6B2Z 6B2Z	Guo et al. (2017). Guo H, Bueler SA, & Rubinstein JL (2017). Atomic model for the dimeric F_O region of mitochondrial ATP synthase. Science 358 :936-940. PubMed Id: 29074581. doi:10.1126/science.aao4815.
*F₁F_o ATP synthase, complete structure in lipid nanodiscs: Saccharomyces cerevisiae* E Eukaryota, 3.6 Å** cryo-EM structure F_o subunit (masked refinement), 4.1 Å: 6CP7 F₁F_o with oligomycin, 3.8 Å: 6CP3 F_o with oligomycin (focused refinement), 4.2 Å: 6CP5	6CP6	Data File Jmol Viewer 6CP6 6CP7 6CP5 6CP3	Srivastava et al. (2018). Srivastava AP, Luo M, Zhou W, Symersky J, Bai D, Chambers MG, Faraldo-Gómez JD, Liao M, & Mueller DM (2018). High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane. Science 360 6389:619. PubMed Id: 29650704. doi:10.1126/science.aas9699.
*ATP synthase (F_o) in nanodisc with inhibitor Bedaquiline: Saccharomyces cerevisiae* E Eukaryota, 4.20 Å** cryo-EM structure	6WTD	Data File Jmol Viewer 6WTD	Luo et al. (2020). Luo M, Zhou W, Patel H, Srivastava AP, Symersky J, Bonar MM, Faraldo-Gómez JD, Liao M, & Mueller DM (2020). Bedaquiline inhibits the yeast and human mitochondrial ATP synthases. Commun Biol 3 1. PubMed Id: 32814813. doi:10.1038/s42003-020-01173-z.
*F₁F_o ATP synthase in multiple states, State 1 catalytic (a) without exogenous ATP, backbone model: Saccharomyces cerevisiae* E Eukaryota, 3.80 Å** cryo-EM structure Backbone models, without exogenous ATP: State 1 catalytic (b), 4.40 Å 7TJZ State 1 catalytic (c), 4.40 Å 7TK0 State 1catalytic (d), 7.10 Å 7TK1 Backbone models, with 10 mM ATP: State 1 binding (a), 6.50 Å 7TK2 State 1 binding (b), 6.30 Å 7TK3 State 1 binding (c), 7.00 Å 7TK4 State 1 binding (d), 7.80 Å 7TK5 State 1 catalytic (a), 6.50 Å 7TK6 State 1 catalytic (b), 6.70 Å 7TK7 State 1 catalytic (c), 4.70 Å 7TK8 State 1 catalytic (d), 6.00 Å 7TK9 State 1 catalytic (e), 7.10 Å 7TKA State 1 catalytic (f), 6.30 Å 7TKB State 1 catalytic (g), 5.80 Å 7TKC State 1 catalytic (h), 7.70 Å 7TKD State 2 binding (a), 7.10 Å 7TKE State 2 binding (b), 7.10 Å 7TKF State 2 catalytic (a), 4.50 Å 7TKG State 2 catalytic (b), 4.40 Å 7TKH State 2 catalytic (c), 7.10 Å 7TKI State 2 catalytic (d), 7.50 Å 7TKJ State 2 catalytic (e), 7.30 Å 7TKK State 3 binding (a), 6.40 Å 7TKL State 3 binding (b), 4.50 Å 7TKM State 3 binding (c), 7.10 Å 7TKN State 3 catalytic (a), 4.80 Å 7TKO State 3 catalytic (b), 4.60 Å 7TKP State 3 catalytic (c), 4.50 Å 7TKQ State 3 catalytic (d), 6.50 Å 7TKR State 3 catalytic (e), 7.50 Å 7TKS	7TJY	Data File Jmol Viewer 7TJY 7TK9 7TKL 7TKQ 7TJZ 7TKP 7TKR 7TKS 7TKJ 7TK0 7TKM 7TKE 7TKG 7TKC 7TKN 7TK1 7TKD 7TK2 7TKK 7TKH 7TK3 7TKA 7TK6 7TK5 7TK8 7TKB 7TK7 7TKO 7TK4 7TKF 7TKI	Guo & Rubinstein (2022). Guo H, & Rubinstein JL (2022). Structure of ATP synthase under strain during catalysis. Nat Commun 13 1:2232. PubMed Id: 35468906. doi:10.1038/s41467-022-29893-2.
*Rotor (c₁₁) of Na⁺-dependent F-ATP Synthase: Ilyobacter tartaricus* B Bacteria, 2.4 Å**	1YCE	Data File Jmol Viewer 1YCE F-type Na+-ATPase Subunit C	Meier et al. (2005). Meier T, Polzer P, Diederichs K, Welte W, & Dimroth P (2005). Structure of the rotor ring of F-type Na-ATPase from Ilyobacter tartaricus. Science 308 :659-662. PubMed Id: 15860619.
*Rotor (c₁₁) of Na⁺-dependent F-ATP Synthase with complete ion-coördination structure: Ilyobacter tartaricus* B Bacteria, 2.35 Å**	2WGM	Data File Jmol Viewer 2WGM	Meier et al. (2009). Meier T, Krah A, Bond PJ, Pogoryelov D, Diederichs K, & Faraldo-Gómez JD (2009). Complete Ion-Coordination Structure in the Rotor Ring of Na⁺-Dependent F-ATP Synthases. J Mol Biol 391 :498-507. PubMed Id: 19500592.
*Rotor (c₁₄) of H⁺-dependent F-ATP Synthase of spinach chloroplasts: Spinacia oleracea* E Eukaryota, 3.80 Å**	2W5J	Data File Jmol Viewer 2W5J	Vollmar et al. (2009). Vollmar M, Schlieper D, Winn M, Büchner C, & Groth G (2009). Structure of the c₁₄Rotor Ring of the Proton Translocating Chloroplast ATP Synthase. J Biol Chem 284 :18228-18235. PubMed Id: 19423706.
*F₁F_o ATP synthase complete structure, conformation 1: Spinacia oleracea* E Eukaryota, 3.15 Å** cryo-EM structure conformation 2, 4.2 Å: 6FKH conformation 3, 4.3 Å: 6KFI	6FKF	Data File Jmol Viewer 6FKF 6KFI 6FKH	Hahn et al. (2018). Hahn A, Vonck J, Mills DJ, Meier T, & Kühlbrandt W (2018). Structure, mechanism, and regulation of the chloroplast ATP synthase. Science 360 6389:620. PubMed Id: 29748256. doi:10.1126/science.aat4318.
*Rotor (c₁₄) of H⁺-dependent F-ATP Synthase of spinach chloroplasts: Spinacia oleracea* E Eukaryota, 2.3 Å**	6TQJ	Data File Jmol Viewer 6TQJ	Vlasov et al. (2019). Vlasov AV, Kovalev KV, Marx SH, Round ES, Gushchin IY, Polovinkin VA, Tsoy NM, Okhrimenko IS, Borshchevskiy VI, Büldt GD, Ryzhykau YL, Rogachev AV, Chupin VV, Kuklin AI, Dencher NA, & Gordeliy VI (2019). Unusual features of the c-ring of F1FO ATP synthases. Sci Rep 9 1. PubMed Id: 31811229. doi:10.1038/s41598-019-55092-z.
*F₁F_o ATP synthase, R1, CF1FO: Spinacia oleracea* E Eukaryota, 3.35 Å** cryo-EM structure R1, CF1; 3.05 Å: 6VOO R2, CF1FO; 4.06 Å: 6VOL R2, CF1; 3.60 Å: 6VOM R3, CF1FO; 4.34 Å: 6VOJ R3, CF1; 3.85 Å: 6VOK O1, CF1FO; 4.16 Å: 6VOH O1, CF1; 4.03 Å: 6VOI O2, CF1FO; 4.51 Å: 6VOF O2, CF1; 4.35 Å: 6VOG O3, CF1FO; 6.46 Å: 6VMG C1, CF1FO; 5.23 Å: 6VMB C1, CF1; 4.53 Å: 6VMD C2, CF1FO; 7.08 Å: 6VM4	6VON	Data File Jmol Viewer 6VON 6VM4 6VOI 6VOH 6VOG 6VMB 6VOL 6VOM 6VMG 6VOK 6VMD 6VOJ 6VOO 6VOF	Yang et al. (2020). Yang JH, Williams D, Kandiah E, Fromme P, & Chiu PL (2020). Structural basis of redox modulation on chloroplast ATP synthase. Commun Biol 3 1:482. PubMed Id: 32879423. doi:10.1038/s42003-020-01221-8.
*Rotor (c₁₄) of H⁺-dependent F-ATP Synthase of green pea chloroplasts: Pisum sativum* E Eukaryota, 3.40 Å**	3V3C	Data File Jmol Viewer 3V3C	Saroussi et al. (2012). Saroussi S, Schushan M, Ben-Tal N, Junge W, & Nelson N (2012). Structure and flexibility of the C-ring in the electromotor of rotary F₀F₁-ATPase of pea chloroplasts. PLoS ONE 7 . PubMed Id: 23049735. doi:10.1371/journal.pone.0043045.
*Rotor (c₁₅) of H⁺-dependent F-ATP Synthase of an alkaliphilic cyanobacterium: Spirulina platensis* B Bacteria, 2.1 Å**	2WIE	Data File Jmol Viewer 2WIE	Pogoryelov et al. (2009). Pogoryelov D, Yildiz O, Faraldo-Gómez JD, & Meier T (2009). High-resolution structure of the rotor ring of a proton-dependent ATP synthase. Nat Struct Mol Biol 16 :1068-1073. PubMed Id: 19783985.
*Rotor (c₁₃) of H⁺-dependent F-ATP Synthase: Bacillus pseudofirmus OF4* B Bacteria, 2.5 Å**	2X2V	Data File Jmol Viewer 2X2V	Preiss et al. (2010). Preiss L, Yildiz O, Hicks DB, Krulwich TA, & Meier T (2010). A New Type of Proton Coordination in an F₁F₀-ATP Synthase Rotor Ring. PLoS Biol 8 :e1000443. PubMed Id: 20689804. doi:10.1371/journal.pbio.1000443.
*Rotor (c12) of H⁺-dependent F-ATP Synthase mutant: Bacillus pseudofirmus OF4* B Bacteria, 4.10 Å** In this mutant, the GxGxGxG motif has been replaced by AxAxAxA.	3ZO6	Data File Jmol Viewer 3ZO6	Preiss et al. (2013). Preiss L, Klyszejko AL, Hicks DB, Liu J, Fackelmayer OJ, Yildiz Ö, Krulwich TA, & Meier T (2013). The c-ring stoichiometry of ATP synthase is adapted to cell physiological requirements of alkaliphilic Bacillus pseudofirmus OF4. Proc Natl Acad Sci USA 110 19:7874-7879. PubMed Id: 23613590. doi:10.1073/pnas.1303333110.
*F₁-ATPase, wild-type: Caldalkalibacillus thermarum* B Bacteria (expressed in E. coli), 3.0 Å** epsilon mutant, 2.6 Å: 5IK2	5HKK	Data File Jmol Viewer 5HKK 5IK2	Ferguson et al. (2016). Ferguson SA, Cook GM, Montgomery MG, Leslie AG, & Walker JE (2016). Regulation of the thermoalkaliphilic F₁-ATPase from Caldalkalibacillus thermarum. Proc Natl Acad Sci USA 113 :10860-10865. PubMed Id: 27621435. doi:10.1073/pnas.1612035113.
*F₁-ATPase: Trypanosoma brucei* E Eukaryota, 3.2 Å**	6F5D	Data File Jmol Viewer 6F5D	Montgomery et al. (2018). Montgomery MG, Gahura O, Leslie AGW, Zíková A, & Walker JE (2018). ATP synthase from Trypanosoma brucei has an elaborated canonical F1-domain and conventional catalytic sites. Proc Natl Acad Sci USA 115 9:2102-2107. PubMed Id: 29440423. doi:10.1073/pnas.1720940115.
*F_o subunit of F₁F_o synthase: Polytomells sp.* E Eukaryota, 3.7 Å** cryo-EM structure	6F36	Data File Jmol Viewer 6F36	Klusch et al. (2017). Klusch N, Murphy BJ, Mills DJ, Yildiz Ö, & Kühlbrandt W (2017). Structural basis of proton translocation and force generation in mitochondrial ATP synthase. Elife 6 :e33274. PubMed Id: 29210357. doi:10.7554/eLife.33274.
*F₁-ATPase in an autoinhibited conformation: Escherichia coli* B Bacteria, 3.26 Å**	3OAA	Data File Jmol Viewer 3OAA	Cingolani & Duncan (2011). Cingolani G & Duncan TM (2011). Structure of the ATP synthase catalytic complex (F₁) from Escherichia coli in an autoinhibited conformation. Nat Struct Mol Biol 18 :701-707. PubMed Id: 21602818. doi:10.1038/nsmb.2058.
*F₁-ATPase: Saccharomyces cerevisiae* E Eukaryota, 2.80 Å**	2HLD	Data File Jmol Viewer 2HLD	Kabaleeswaran et al. (2006). Kabaleeswaran V, Puri N, Walker JE, Leslie AG, & Mueller DM (2006). Novel features of the rotary catalytic mechanism revealed in the structure of yeast F₁ATPase. EMBO J 25 :5433-5442. PubMed Id: 17082766.
*F1-ATPase inhibited by its regulatory protein IF1: Saccharomyces cerevisiae* E Eukaryota, 2.50 Å**	3ZIA	Data File Jmol Viewer 3ZIA	Robinson et al. (2013). Robinson GC, Bason JV, Montgomery MG, Fearnley IM, Mueller DM, Leslie AG, & Walker JE (2013). The structure of F₁-ATPase from Saccharomyces cerevisiae inhibited by its regulatory protein IF1. Open Biol 3 :120164. PubMed Id: 23407639. doi:10.1098/rsob.120164.
*F₁-ATPase: Fusobacterium nucleatum* B Bacteria (expressed in E. coli), 3.6 Å**	6Q45	Data File Jmol Viewer 6Q45	Petri et al. (2019). Petri J, Nakatani Y, Montgomery MG, Ferguson SA, Aragão D, Leslie AGW, Heikal A, Walker JE, & Cook GM (2019). Structure of F₁-ATPase from the obligate anaerobe Fusobacterium nucleatum. Open Biol 9 6. PubMed Id: 31238823. doi:10.1098/rsob.190066.
*F₁F_o synthase, class 1: Bacillus sp. (strain PS3)* B Bacteria (expressed in E. coli), 3 Å** cryo-EM structure class 2, 3 Å: 6N2Z class 3, 3.2 Å: 6N30 membrane domain, 3.3 Å: 6N2D	6N2Y	Data File Jmol Viewer 6N2Y 6N30 6N2Z 6N2D	Guo et al. (2019). Guo H, Suzuki T, & Rubinstein JL (2019). Structure of a bacterial ATP synthase. Elife 8 :e43128. PubMed Id: 30724163. doi:10.7554/eLife.43128.
*F₁-ATP synthase, Binding/TS Dwell: Bacillus sp. PS3* B Bacteria (expressed in E. coli), 3.40 Å** cryo-EM structure Hydrolysis Dwell, 3.10 Å: 7L1R P_i-bound Dwell, 3.60 Å: 7L1S	7L1Q	Data File Jmol Viewer 7L1Q 7L1S 7L1R	Sobti et al. (2021). Sobti M, Ueno H, Noji H, & Stewart AG (2021). The six steps of the complete F₁-ATPase rotary catalytic cycle. Nat Commun 12 1:4690. PubMed Id: 34344897. doi:10.1038/s41467-021-25029-0.
*F₁F_o synthase, c-ring: Bacillus sp. (strain PS3)* B Bacteria (expressed in Escherichia coli), NMR Structure**	7WEM	Data File Jmol Viewer 7WEM	Todokoro et al. (2022). Todokoro Y, Kang SJ, Suzuki T, Ikegami T, Kainosho M, Yoshida M, Fujiwara T, & Akutsu H (2022). Chemical Conformation of the Essential Glutamate Site of the c-Ring within Thermophilic Bacillus F_oF₁-ATP Synthase Determined by Solid-State NMR Based on its Isolated c-Ring Structure. J Am Chem Soc 144 31:14132-14139. PubMed Id: 35905443. doi:10.1021/jacs.2c03580.
*F₁F_o synthase (complete structure; dimeric): Yarrowia lipolytica* E Eukaryota, 3.5 Å**	5FL7	Data File Jmol Viewer 5FL7	Hahn et al. (2016). Hahn A, Parey K, Bublitz M, Mills DJ, Zickermann V, Vonck J, Kühlbrandt W, & Meier T (2016). Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology. Mol Cell 63 3:445-456. PubMed Id: 27373333. doi:10.1016/j.molcel.2016.05.037.
*F₁F_o synthase (complete structure; dimeric): Polytomella sp.* E Eukaryota, 2.9 Å** cryo-EM structure The structure is a composite built from more than 50 structures. For a complete list of the individual structures go to Science Magazine	6RD4	Data File Jmol Viewer 6RD4	Murphy et al. (2019). Murphy BJ, Klusch N, Langer J, Mills DJ, Yildiz Ö, & Kühlbrandt W (2019). Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-Fo coupling. Science 364 6446. PubMed Id: 31221832. doi:10.1126/science.aaw9128.
*F₁F_o synthase in E-state: Sus scrofa* E Eukaryota, 3.45 Å** cryo-EM structure in DP-state, 3.34 Å: 6J5I tetramer with bound inhibitory protein IF1, 6.2 Å: 6J5K E-state ATP synthase F_o section, 3.94 Å: 6J54 DP-state ATP synthase F_o section, 4.35 Å: 6J5A	6J5J	Data File Jmol Viewer 6J5J 6J5K 6J5A 6J54 6J5I	Gu et al. (2019). Gu J, Zhang L, Zong S, Guo R, Liu T, Yi J, Wang P, Zhuo W, & Yang M (2019). Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1. Science 364 6445:1068-1075. PubMed Id: 31197009. doi:10.1126/science.aaw4852.
*F₁F_o synthase (complete structure; dimeric), rotational state 1: Euglena gracilis* E Eukaryota, 4.32 Å** cryo-EM structure membrane region, 2.8 Å: 6TDV peripheral stalk, rotational state 1, 3.8 Å: 6TDW rotor, rotational state 1, 3.3 Å: 3.3 Å: 6TDX OSCP/F1/c-ring in rotational state 1, 3.04 Å: 6TDY OSCP/F1/c-ring, rotational state 2, 3.14 Å: 6TDZ OSCP/F1/c-ring, rotational state 3, 3.92 Å: 6TE0	6TDU	Data File Jmol Viewer 6TDU 6TE0 6TDX 6TDY 6TDZ 6TDW 6TDV	Mühleip et al. (2019). Mühleip A, McComas SE, & Amunts A (2019). Structure of a mitochondrial ATP synthase with bound native cardiolipin. Elife 8 . PubMed Id: 31738165. doi:10.7554/eLife.51179.
*F₁F_o type III ATP synthase (composite structure, dimeric): Tetrahymena thermophila* E Eukaryota, 2.70 Å** cryo-EM structure composite structure, tetrameric. 3.10 Å: 6YNZ F_o-wing region, 2.80 Å: 6YNV central stalk/c-ring, 3.10 Å: 6YNW F_o-subcomplex, 2.50 Å: 6YNX F₁/peripheral stalk, 2.90 Å 6YO0	6YNY	Data File Jmol Viewer 6YNY 6YNX 6YO0 6YNV 6YNW 6YNZ	Flygaard et al. (2020). Flygaard RK, Mühleip A, Tobiasson V, & Amunts A (2020). Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization. Nat Commun 11 1:5342. PubMed Id: 33093501. doi:10.1038/s41467-020-18993-6.
*F₁F_o ATP synthase, complete structure in 1a state: Ovis aries* E Eukaryota, 3.50 Å** cryo-EM structure F_o domain, 3.76 Å: 6ZA9	6TT7	Data File Jmol Viewer 6TT7 6ZA9	Pinke et al. (2020). Pinke G, Zhou L, & Sazanov LA (2020). Cryo-EM structure of the entire mammalian F-type ATP synthase. Nat Struct Mol Biol 27 :1077-1085. PubMed Id: 32929284. doi:10.1038/s41594-020-0503-8.
*F₁F_o synthase, bedaquiline-free, rotational state 1: Mycolicibacterium smegmatis* B Bacteria, 3.40 Å** cryo-EM structure bedaquiline-free, state 2 (backbone model), 3.70 Å: 7JG6 bedaquiline-free, state 3 (backbone model), 3.50 Å: 7JG7 bedaquiline-saturated, state 1 (backbone model), 3.30 Å: 7JG8 bedaquiline-saturated, state 2 (backbone model), 3.40 Å: 7JG9 bedaquiline-saturated, state 3, 3.20 Å: 7JGA bedaquiline-free, F_o region, 3.50 Å: 7JGB bedaquiline-saturated, F_o region, 3.40 Å: 7JGC	7JG5	Data File Jmol Viewer 7JG5 7JG7 7JG6 7JGA 7JGB 7JG8 7JG9 7JGC	Guo et al. (2021). Guo H, Courbon GM, Bueler SA, Mai J, Liu J, & Rubinstein JL (2021). Structure of mycobacterial ATP synthase bound to the tuberculosis drug bedaquiline. Nature 589 7840:143-147. PubMed Id: 33299175. doi:10.1038/s41586-020-3004-3.
*F₁F_o synthase, state 1a: Mycolicibacterium smegmatis* B Bacteria, 2.52 Å** cryo-EM structure state 1b, 2.71 Å 7NJL state 1c, 2.84 Å 7NJM state 1d, 2.64 Å 7NJN state 1e, 2.92 Å 7NJO state 2, 2.84 Å 7NJP state 3a, 2.67 Å 7NJQ state 3b, 2.56 Å 7NJR state 3c, 2.46 Å 7NJS F_o combined all classes, 2.75 Å 7NJT F_o combined class 1, 3.74 Å 7NJU F_o combined class 2, 2.90 Å 7NJV F_o combined class 3, 3.67 Å 7NJW F_o combined class 4, 4.32 Å 7JNX F_ocombined class 5, 2.94 Å 7NJY F₁ state 1, 2.11 Å 7NK7 F_o domain state 1, 2.90 Å 7NK9 rotor state 1, 2.90 Å 7NKB b-delta state 1, 3.12 Å 7NKD F₁ state 2, 2.78 Å 7NKH F₁ state 3, 2.17 Å 7NKJ rotor state 2, 3.60 Å, 7NKK b-delta state 2, 3.67 Å 7NKL rotor state 3, 2.71 Å 7NKN F_o state 2, 4.06 Å 7NKP b-delta state 3, 2.98 Å 7NKQ F_o state 3, 2.86 Å7NL9	7NJK	Data File Jmol Viewer 7NJK 7NJU 7NJL 7NJW 7JNX 7NK9 7NKN 7NJQ 7NL9 7NKJ 7NJP 7NKQ 7NK7 7NKL 7NKK 7NJT 7NJM 7NJV 7NJY 7NKP 7NJR 7NJO 7NJN 7NKH 7NJS 7NKD 7NKB	Montgomery et al. (2021). Montgomery MG, Petri J, Spikes TE, & Walker JE (2021). Structure of the ATP synthase from Mycobacterium smegmatis provides targets for treating tuberculosis. Proc Natl Acad Sci U S A 118 47:e2111899118. PubMed Id: 34782468. doi:10.1073/pnas.2111899118.
*F₁F_o ATP synthase hexamer, composite model: Toxoplasma gondii* E Eukaryota, 4.80 Å** cryo-EM structure dimer, membrane region model, 2.80 Å: 6TMG dimer, OSCP/F₁/c-ring model, 3.10 Å: 6TMH dimer, peripheral stalk model, 3.50 Å: 6TMI dimer, rotor-stator model, 3.50 Å: 6TMJ dimer, composite model, 2.90 Å: 6TMK	6TML	Data File Jmol Viewer 6TML 6TMJ 6TMG 6TMH 6TMI 6TMK	Mühleip et al. (2021). Mühleip A, Kock Flygaard R, Ovciarikova J, Lacombe A, Fernandes P, Sheiner L, & Amunts A (2021). ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria. Nat Commun 12 1. PubMed Id: 33402698. doi:10.1038/s41467-020-20381-z.
*F₁F_o-ATP synthase, state 1: Acinetobacter baumannii* B Bacteria, 3.10 Å** cryo-EM structure state 2, 4.60 Å 7P3N state 3, 4.30 Å 7P3W	7P2Y	Data File Jmol Viewer 7P2Y 7P3N 7P3W	Demmer et al. (2022). Demmer JK, Phillips BP, Uhrig OL, Filloux A, Allsopp LP, Bublitz M, & Meier T (2022). Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii. Sci Adv 8 7:eabl5966. PubMed Id: 35171679. doi:10.1126/sciadv.abl5966.
*F₁F_o ATP synthase, state 1, combined: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.53 Å** cryo-EM structure state 1, F₁ head domain, 2.53 Å: 8H9E state 1, subregion 2, 2.95 Å: 8H9G state 1, subregion 3, 2.69 Å: 8H9F state 2, F₁ head domain, 2.77 Å: 8H9I state 2, combined, 2.77 Å: 8H9T state 2, subregion 2, 3.51 Å: 8H9K state 2, subregion 3, 3.26 Å: 8H9J state 3a, F₁ head domain, 2.61 Å: 8H9L state 3a, combined, 2.61 Å: 8H9U state 3a, subregion 2, 3.56 Å: 8H9N state 3a, subregion 3, 3.00 Å: 8H9M state 3b, F₁ head domain, 3.02 Å: 8H9P state 3b, combined, 3.02 Å: 8H9V state 3b, subregion 2, 3.97 Å: 8H9R state 3b, subregion 3, 3.47 Å: 8H9Q	8H9S	Data File Jmol Viewer 8H9S 8H9G 8H9T 8H9N 8H9Q 8H9M 8H9V 8H9P 8H9E 8H9K 8H9R 8H9J 8H9L 8H9I 8H9U 8H9F	Lai et al. (2023). Lai Y, Zhang Y, Zhou S, Xu J, Du Z, Feng Z, Yu L, Zhao Z, Wang W, Tang Y, Yang X, Guddat LW, Liu F, Gao Y, Rao Z, & Gong H (2023). Structure of the human ATP synthase. Mol Cell 83 12:2137-2147.e4. PubMed Id: 37244256. doi:10.1016/j.molcel.2023.04.029.
P-type ATPase
*Calcium ATPase; rabbit sarcoplasmic reticulum. E1 state with bound calcium: Oryctolagus cuniculus* E Eukaryota, 2.4 Å** This structure supersedes 1EUL. These ATPases are referred to as SERCA pumps; SERCA: Sarco(Endo)plasmic Reticulum CAlcium	1SU4	Data File Jmol Viewer 1SU4 Ca ATPase, SR	Toyoshima et al. (2000). Toyoshima C, Nakasako M, Nomura H, & Ogawa H (2000). Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405 :647-655. PubMed Id: 10864315.
*Calcium ATPase; rabbit sarcoplasmic reticulum. E1 state with bound calcium, magnesium, and an ATP analog: Oryctolagus cuniculus* E Eukaryota, 2.9 Å**	1VFP	Data File Jmol Viewer 1VFP	Toyoshima & Mizutani (2004). Toyoshima C & Mizutani T (2004). Crystal structure of the calcium pump with a bound ATP analogue. Nature 430 :529-35. PubMed Id: 15229613.
*Calcium ATPase; rabbit sarcoplasmic reticulum. E2 state without bound calcium: Oryctolagus cuniculus* E Eukaryota, 3.1 Å**	1IWO	Data File Jmol Viewer 1IWO	Toyoshima & Nomura (2002). Toyoshima C & Nomura H (2002). Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418 :605-611. PubMed Id: 12167852.
*Calcium ATPase; rabbit sarcoplasmic reticulum. E2 state calcium-free with bound magnesium fluoride: Oryctolagus cuniculus* E Eukaryota, 2.3 Å** E1 state with bound AlF_x and ADP, 2.40 Å: 2ZDB (supersedes 1WPE, which was superseded by 2Z9R)	1WPG	Data File Jmol Viewer 1WPG 2ZDB	Toyoshima et al. (2004). Toyoshima C, Nomura H, & Tsuda T (2004). Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 432 :361-368. PubMed Id: 15448704.
*Calcium ATPase; rabbit sarcoplamic reticulum. E1 state with bound calcium and AMPPC: Oryctolagus cuniculus* E Eukaryota, 2.6 Å** E1 state with bound calcium and ADP:AlF₄^–, 2.9 Å: 1T5T	1T5S	Data File Jmol Viewer 1T5S 1T5T	Sørensen et al. (2004). Sørensen TL, Jensen AM Møller JV, & Nissen P (2004). Phosphoryl transfer and calcium ion occlusion in the calcium pump. Science 304 :1672-1675. PubMed Id: 15192230.
*Calcium ATPase; rabbit sarcoplasmic reticulum. E2 state with bound AlF₄^– calcium-free: Oryctolagus cuniculus* E Eukaryota, 3.0 Å**	1XP5	Data File Jmol Viewer 1XP5	Olesen et al. (2004). Olesen C, Sørensen TL, Nielsen RC, Møller JV, & Nissen P (2004). Dephosphorylation of the calcium pump coupled to counterion occlusion. Science 306 :2251-2255. PubMed Id: 15618517.
*Calcium ATPase; rabbit sarcoplasmic reticulum. Ca²⁺-free, with bound BHQ and thapsigargin: Oryctolagus cuniculus* E Eukaryota, 3.0 Å**	2AGV	Data File Jmol Viewer 2AGV	Obara et al. (2005). Obara K, Miyashita N, Xu C, Toyoshima I, Sugita Y, Inesi G, & Toyoshima C (2005). Structural role of countertransport revealed in Ca²⁺pump crystal structure in the absence of Ca²⁺. Proc Natl Acad Sci U S A 102 :14489-14496. PubMed Id: 16150713.
*Calcium ATPase; rabbit sarcoplasmic reticulum. With bound synthesized derivative of thapsigargin: Oryctolagus cuniculus* E Eukaryota, 3.30 Å**	2BY4	Data File Jmol Viewer 2BY4	Søhoel et al. (2006). Søhoel H, Jensen AM, Møller JV, Nissen P, Denmeade SR, Isaacs JT, Olsen CE, Christensen SB (2006). Natural products as starting materials for development of second-generation SERCA inhibitors targeted towards prostate cancer cells. Bioorg Med Chem 14 :2810-2815. PubMed Id: 16150713.
*Calcium ATPase; rabbit sarcoplamic reticulum. Ca²⁺-free E2 state with thapsigargin and AMPPCP: Oryctolagus cuniculus* E Eukaryota, 3.10 Å** With partially occupied AMPPCP site, 2.80 Å: 2C8K With thapsigargin, 3.10 Å: 2C8L In the Ca²⁺ E1 state solved in a P1 crystal form, 3.00 Å: 2C9M	2C88	Data File Jmol Viewer 2C88 2C8L 2C8K 2C9M	Jensen et al. (2006). Jensen AM, Sørensen TL, Olesen C, Møller JV, & Nissen P (2006). Modulatory and catalytic modes of ATP binding by the calcium pump. EMBO J 25 :2305-2314. PubMed Id: 16710301.
*Calcium ATPase; rabbit sarcoplamic reticulum. Calcium-free with bound AlF₄^– and cyclopiazonic acid (CPA): Oryctolagus cuniculus* E Eukaryota, 2.65 Å** Calcium-free with bound CPA and ADP, 3.4 Å: 2OA0	2O9J	Data File Jmol Viewer 2O9J 2OA0	Moncoq et al. (2007). Moncoq K, Trieber CA, & Young HS (2007). The molecular basis for cyclopiazonic acid inhibition of the sarcoplasmic reticulum calcium pump. J Biol Chem 282 :9748-9757. PubMed Id: 17259168.
*Calcium ATPase; rabbit sarcoplamic reticulum. Ca²⁺E1~P (Ca²⁺E1~P.AMPPN): Oryctolagus cuniculus* E Eukaryota, 2.8 Å** E2P (E2-BeF₃^–), 2.65 Å: 3B9B E2-P* (E2-AlF₄^–), 3.0 Å: 3B9R	3BA6	Data File Jmol Viewer 3BA6 3B9B 3B9R	Olesen et al. (2007). Olesen C, Picard M, Winther A-M L, Gyrup C, Morth JP, Oxvig C, Møller JV & Nissen P (2007). The structural basis of calcium transport by the calcium pump. Nature 450 :1036-1042. PubMed Id: 18075584.
*Calcium ATPase; rabbit sarcoplamic reticulum. Ca²⁺-free E2 state with debutanoyl thapsigargin: Oryctolagus cuniculus* E Eukaryota, 3.10 Å** Structural analysis of the Type I crystal structure reveals the location and thickness of the lipid bilayer	2YFY	Data File Jmol Viewer 2YFY	Sonntag et al. (2011). Sonntag Y, Musgaard M, Olesen C, Schiφtt B, Mφller JV, Nissen P, & Thφgersen L. (2011). Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes. Nat Commun 2 :304. PubMed Id: 21556058. doi:10.1038/ncomms1307.
*Calcium ATPase; rabbit sarcoplasmic reticulum with bound sarcolipin: Oryctolagus cuniculus* E Eukaryota, 3.10 Å**	4H1W	Data File Jmol Viewer 4H1W	Winther et al. (2013). Winther AM, Bublitz M, Karlsen JL, Møller JV, Hansen JB, Nissen P, & & Buch-Pedersen MJ (2013). The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm. Nature 495 :265-268. PubMed Id: 23455424. doi:10.1038/nature11900.
*Calcium ATPase; rabbit sarcoplasmic reticulum with bound sarcolipin in E1^.Mg²⁺ state: Oryctolagus cuniculus* E Eukaryota, 3.01 Å** without sarcolipin, 3.20 Å: 3W5B without sarcolipin; E2 state with P_i, 2.45 Å: 3W5D	3W5A	Data File Jmol Viewer 3W5A 3W5D 3W5B	Toyoshima et al. (2013). Toyoshima C, Iwasawa S, Ogawa H, Hirata A, Tsueda J, & Inesi G (2013). Crystal structures of the calcium pump and sarcolipin in the Mg²⁺-bound E1 state. Nature 495 :260-264. PubMed Id: 23455422. doi:10.1038/nature11899.
*Calcium ATPase; rabbit sarcoplasmic reticulum with bound phospholamban: Oryctolagus cuniculus* E Eukaryota, 2.83 Å**	4KYT	Data File Jmol Viewer 4KYT	Akin et al. (2013). Akin BL, Hurley TD, Chen Z, & Jones LR (2013). The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum. J Biol Chem 288 42:30181-30191. PubMed Id: 23996003. doi:10.1074/jbc.M113.501585.
*Calcium ATPase; rabbit sarcoplasmic reticulum E309Q mutant in Ca₂E1 state: Oryctolagus cuniculus* E Eukaryota (expressed in S. cerevisiae), 3.50 Å**	4NAB	Data File Jmol Viewer 4NAB	Clausen et al. (2013). Clausen JD, Bublitz M, Arnou B, Montigny C, Jaxel C, Møller JV, Nissen P, Andersen JP, & le Maire M (2013). SERCA mutant E309Q binds two Ca(2+) ions but adopts a catalytically incompetent conformation. EMBO J. 32 :3231-3243. PubMed Id: 24270570. doi:10.1038/emboj.2013.250.
*Calcium ATPase; rabbit sarcoplamic reticulum. P21 crystal form with bound thapsigargin: Oryctolagus cuniculus* E Eukaryota, 3.10 Å** With bound CPA, 3.4 Å: 2EAS With bound CPA and thapsigargin, 2.90 Å: 2EAT With bound CPA in the presence of curcumin, 2.80 Å: 2EAU	2EAR	Data File Jmol Viewer 2EAR 2EAT 2EAS 2EAU	Takahashi et al. (2007). Takahashi M, Kondou Y, & Toyoshima C (2007). Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors. Proc Natl Acad Sci USA 104 :5800-5805. PubMed Id: 17389383.
*Calcium ATPase; structure determined by electron crystallography using ultrathin protein crystals: Oryctolagus cuniculus* E Eukaryota, 3.40 Å** Electron crystallography of the ultrathin crystals permit determination of atomic models with charges.	3J7T	Data File Jmol Viewer 3J7T	Yonekura et al. (2015). Yonekura K, Kato K, Ogasawara M, Tomita M, & Toyoshima C (2015). Electron crystallography of ultrathin 3D protein crystals: Atomic model with charges. Proc Natl Acad Sci USA 112 11:3368-3373. PubMed Id: 25730881. doi:10.1073/pnas.1500724112.
*Calcium ATPase; rabbit sarcoplasmic reticulum. E1 state with bound calcium and AMPPC by free-electron laser: Oryctolagus cuniculus* E Eukaryota, 2.80 Å** Structure determined using an x-ray free-electron laser.	4XOU	Data File Jmol Viewer 4XOU	Bublitz et al. (2015). Bublitz M, Nass K, Drachmann ND, Markvardsen AJ, Gutmann MJ, Barends TR, Mattle D, Shoeman RL, Doak RB, Boutet S, Messerschmidt M, Seibert MM, Williams GJ, Foucar L, Reinhard L, Sitsel O, Gregersen JL, Clausen JD, Boesen T, Gotfryd K, Wang KT, Olesen C, Møller JV, Nissen P, & Schlichting I (2015). Structural studies of P-type ATPase-ligand complexes using an X-ray free-electron laser. IUCrJ 2 :409-420. PubMed Id: 26175901. doi:10.1107/S2052252515008969.
*Calcium ATPase; rabbit sarcoplasmic reticulum. E2-vanadate complex bound to thapsigargin and TNP-AMPPCP: Oryctolagus cuniculus* E Eukaryota, 3.05 Å** E2.BeF₃^- complex bound to TNP-AMPPCP, 3.05 Å: 5A3R E2-vanadate complex bound to thapsigargin and TNP-ATP, 3.3 Å: 5A3S	5A3Q	Data File Jmol Viewer 5A3Q 5A3S 5A3R	Clausen et al. (2016). Clausen JD, Bublitz M, Arnou B, Olesen C, Andersen JP, Møller JV, & Nissen P (2016). Crystal Structure of the Vanadate-Inhibited Ca²⁺-ATPase. Structure 24 :617-623. PubMed Id: 27050689. doi:10.1016/j.str.2016.02.018.
*Calcium ATPase and associated phospholipids in the E1-2Ca²⁺ crystals: Oryctolagus cuniculus* E Eukaryota, 3.2 Å** in E1-ALF₄^-^.ADP-2Ca²⁺ crystals, 3.2 Å: 5XA8 in E2^.ALF₄^- (TG), C2 symmetry, 3.2 Å: 5XA9 in E2^.ALF₄^- (TG) crystals, P2₁2₁2 symmetry, 5XAA in E2(TG) crystals. 3.2 Å: 5XAB	5XA7	Data File Jmol Viewer 5XA7 5XA8 5XAA 5XAB 5XA9	Norimatsu et al. (2017). Norimatsu Y, Hasegawa K, Shimizu N, & Toyoshima C (2017). Protein-phospholipid interplay revealed with crystals of a calcium pump. Nature 545 7653:193-198. PubMed Id: 28467821. doi:10.1038/nature22357.
*Calcium ATPase, E1 state with bound calcium and AMPPC: Oryctolagus cuniculus* E Eukaryota, 3.54 Å** room temperature structure from large seeded crystals	6HEF	Data File Jmol Viewer 6HEF	Sørensen et al. (2018). Sørensen TLM, Hjorth-Jensen SJ, Oksanen E, Andersen JL, Olesen C, Møller JV, & Nissen P (2018). Membrane-protein crystals for neutron diffraction. Acta Crystallogr D Struct Biol 74 :1208-1218. PubMed Id: 30605135. doi:10.1107/S2059798318012561.
*Calcium ATPase, E2 state, E309A mutant: Oryctolagus cuniculus* E Eukaryota (expressed in Chlorocebus sabaeus), 3.3 Å** E309Q mutant, 2.5 Å: 5ZMW	5ZMV	Data File Jmol Viewer 5ZMV 5ZMW	Tsunekawa et al. (2018). Tsunekawa N, Ogawa H, Tsueda J, Akiba T, & Toyoshima C (2018). Mechanism of the E2 to E1 transition in Ca²⁺ pump revealed by crystal structures of gating residue mutants. Proc Natl Acad Sci USA 115 50:12722-12727. PubMed Id: 30482857. doi:10.1073/pnas.1815472115.
*SERCA Calcium ATPase with bound inhibitor CAD204520: Oryctolagus cuniculus* E Eukaryota, 3.40 Å**	6YAA	Data File Jmol Viewer 6YAA	Marchesini et al. (2020). Marchesini M, Gherli A, Montanaro A, Patrizi L, Sorrentino C, Pagliaro L, Rompietti C, Kitara S, Heit S, Olesen CE, Møller JV, Savi M, Bocchi L, Vilella R, Rizzi F, Baglione M, Rastelli G, Loiacono C, La Starza R, Mecucci C, Stegmaier K, Aversa F, Stilli D, Lund Winther AM, Sportoletti P, Bublitz M, Dalby-Brown W, & Roti G (2020). Blockade of Oncogenic NOTCH1 with the SERCA Inhibitor CAD204520 in T Cell Acute Lymphoblastic Leukemia. Cell Chem Biol 27 6:678-697.e13. PubMed Id: 32386594. doi:10.1016/j.chembiol.2020.04.002.
*Sarcoplasmic reticulum Calcium ATPase, structure phased using vanadium: Oryctolagus cuniculus* E Eukaryota, 3.13 Å**	6YSO	Data File Jmol Viewer 6YSO	El Omari et al. (2020). El Omari K, Mohamad N, Bountra K, Duman R, Romano M, Schlegel K, Kwong HS, Mykhaylyk V, Olesen C, Moller JV, Bublitz M, Beis K, & Wagner A (2020). Experimental phasing with vanadium and application to nucleotide-binding membrane proteins. IUCrJ 7 :1092-1101. PubMed Id: 33209320. doi:10.1107/S2052252520012312.
*Calcium ATPase sarco/endoplasmic reticulum (SERCA) E340A mutant in the Ca²⁺-E1-CaAMPPCP form: Oryctolagus cuniculus* E Eukaryota (expressed in Saccharomyces cerevisiae), 3.20 Å**	6RB2	Data File Jmol Viewer 6RB2	Geurts et al. (2020). Geurts MMG, Clausen JD, Arnou B, Montigny C, Lenoir G, Corey RA, Jaxel C, Møller JV, Nissen P, Andersen JP, le Maire M, & Bublitz M (2020). The SERCA residue Glu340 mediates interdomain communication that guides Ca²⁺ transport. Proc Natl Acad Sci U S A 117 49:31114-31122. PubMed Id: 33229570. doi:10.1073/pnas.2014896117.
*Plasma membrane Ca²⁺-ATPase 1 (PMCA1) in complex with its obligatory subunit neuroplastin (NPTP): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 4.1 Å** cryo-EM structure. The TM domain resolution is 3.9 Å.	6A69	Data File Jmol Viewer 6A69	Gong et al. (2018). Gong D, Chi X, Ren K, Huang G, Zhou G, Yan N, Lei J, & Zhou Q (2018). Structure of the human plasma membrane Ca²⁺-ATPase 1 in complex with its obligatory subunit neuroplastin. Nat Commun 9 1. PubMed Id: 30190470. doi:10.1038/s41467-018-06075-7.
*DWORF peptide associated with Ca²⁺-ATPase 1 (PMCA1): Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure** DWORF controls the activation of the ATPase	7MPA	Data File Jmol Viewer 7MPA	Reddy et al. (2022). Reddy UV, Weber DK, Wang S, Larsen EK, Gopinath T, De Simone A, Robia S, & Veglia G (2022). A kink in DWORF helical structure controls the activation of the sarcoplasmic reticulum Ca^{2+-ATPase. Structure 30 3:360-370.e6. PubMed Id: 34875216. doi:10.1016/j.str.2021.11.003.}
*Calcium ATPase sarco/endoplasmic reticulum (SERCA2a): Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.2 Å** SERCA2b, 3.45 Å: 5ZTF	6JJU	Data File Jmol Viewer 6JJU 5ZTF	Inoue et al. (2019). Inoue M, Sakuta N, Watanabe S, Zhang Y, Yoshikaie K, Tanaka Y, Ushioda R, Kato Y, Takagi J, Tsukazaki T, Nagata K, & Inaba K (2019). Structural Basis of Sarco/Endoplasmic Reticulum Ca²⁺-ATPase 2b Regulation via Transmembrane Helix Interplay. Cell Rep 27 4:1221-1230.e3. PubMed Id: 31018135. doi:10.1016/j.celrep.2019.03.106.
*Calcium ATPase sarco/endoplasmic reticulum (SERCA2a), E2-ATP state: Homo sapiens* E Eukaryota (expressed in Chlorocebus sabaeus), 3.0 Å**	7BT2	Data File Jmol Viewer 7BT2	Kabashima et al. (2020). Kabashima Y, Ogawa H, Nakajima R, & Toyoshima C (2020). What ATP binding does to the Ca²⁺ pump and how nonproductive phosphoryl transfer is prevented in the absence of Ca²⁺. Proc Natl Acad Sci USA 117 31:18448-18458. PubMed Id: 32675243. doi:10.1073/pnas.2006027117.
*Calcium ATPase sarco/endoplasmic reticulum (SERCA2b) in E1-2Ca²⁺-AMPPCP state: Homo sapiens* E Eukaryota (expressed in HEK293), 2.90 Å** cryo-EM structure in E2-BeF₃- state, 2.80 Å: 6LLY	6LLE	Data File Jmol Viewer 6LLE 6LLY	Zhang et al. (2020). Zhang Y, Inoue M, Tsutsumi A, Watanabe S, Nishizawa T, Nagata K, Kikkawa M, & Inaba K (2020). Cryo-EM structures of SERCA2b reveal the mechanism of regulation by the luminal extension tail. Sci Adv 6 33. PubMed Id: 32851169. doi:10.1126/sciadv.abb0147.
*Calcium ATPase sarco/endoplasmic reticulum (SERCA2b) in E1-2Ca²⁺ state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	7E7S	Data File Jmol Viewer 7E7S	Zhang et al. (2021). Zhang Y, Watanabe S, Tsutsumi A, Kadokura H, Kikkawa M, & Inaba K (2021). Cryo-EM analysis provides new mechanistic insight into ATP binding to Ca²⁺ -ATPase SERCA2b. EMBO J 40 19:e108482. PubMed Id: 34459010. doi:10.15252/embj.2021108482.
*Calcium ATPase sarco/endoplasmic reticulum (SERCA2b) wild-type in E1-BeF₃^- ·2Ca²⁺: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure ‘Ca²⁺-unbound’·BeF₃^- state, 3.00 Å: 7W7U ‘late’ E2P state, 3.00 Å: 7W7V E2·Pi state, 3.20 Å: 7W7W	7W7T	Data File Jmol Viewer 7W7T 7W7U 7W7V 7W7W	Zhang et al. (2022). Zhang Y, Kobayashi C, Cai X, Watanabe S, Tsutsumi A, Kikkawa M, Sugita Y, & Inaba K (2022). Multiple sub-state structures of SERCA2b reveal conformational overlap at transition steps during the catalytic cycle. Cell Rep 41 10:111760. PubMed Id: 36476867. doi:10.1016/j.celrep.2022.111760.
*Calcium ATPase sarco/endoplasmic reticulum (SERCA2a), CPA-stabilized E2-AlF^-₄ form: Sus scrofa* E Eukaryota, 3.3 Å** Ca₂E1-AMPPCP form, 4 Å: 6HXB	5MPM	Data File Jmol Viewer 5MPM 6HXB	Sitsel et al. (2019). Sitsel A, De Raeymaecker J, Drachmann ND, Derua R, Smaardijk S, Andersen JL, Vandecaetsbeek I, Chen J, De Maeyer M, Waelkens E, Olesen C, Vangheluwe P, & Nissen P (2019). Structures of the heart specific SERCA2a Ca2+-ATPase. EMBO J 38 5. PubMed Id: 30777856. doi:10.15252/embj.2018100020.
*Na,K-ATPase; pig kidney : Sus scrofa* E Eukaryota, 3.5 Å**	3B8E	Data File Jmol Viewer 3B8E	Morth et al. (2007). Morth JP, Pedersen BP, Kohl A,Toustrup-Jensen MS, Sørensen TL-M D, Petersen J, Petersen JP, Vilsen B, & Nissen P (2007). Crystal structure of the sodium-potassim pump. Nature 450 :1043-1049. PubMed Id: 18075585.
*Na,K-ATPase, phosphorylated form in complex with ouabain: Sus scrofa* E Eukaryota, 4.60 Å**	3N23	Data File Jmol Viewer 3N23	Yatime et al. (2011). Yatime L, Laursen M, Morth JP, Esmann M, Nissen P, & Fedosova NU (2011). Structural insights into the high affinity binding of cardiotonic steroids to the Na⁺,K⁺-ATPase. J Struct Biol 174 :296-306. PubMed Id: 21182963. doi:10.1016/j.jsb.2010.12.004.
*Na,K-ATPase-ouabain complex with Mg²⁺ in cation binding site: Sus scrofa* E Eukaryota, 3.40 Å**	4HYT	Data File Jmol Viewer 4HYT	Laursen et al. (2013). Laursen M, Yatime L, Nissen P, & Fedosova NU (2013). Crystal structure of the high-affinity Na⁺,K⁺-ATPase-ouabain complex with Mg⁺² bound in the cation binding site. Proc Natl Acad Sci USA 110 :10958-10963. PubMed Id: 23776223. doi:10.1073/pnas.1222308110.
*Na,K-ATPase; pig kidney in the Na⁺-bound state: Sus scrofa* E Eukaryota, 4.30 Å**	4HQJ	Data File Jmol Viewer 4HQJ	Nyblom et al. (2013). Nyblom M, Poulsen H, Gourdon P, Reinhard L, Andersson M, Lindahl E, Fedosova N, & Nissen P (2013). Crystal Structure of Na⁺, K⁺-ATPase in the Na⁺-Bound State. Science 342 :123-127. PubMed Id: 24051246.
*Na,K-ATPase with bound Na⁺ preceding the E1P state: Sus scrofa* E Eukaryota, 2.80 Å** With oligomycin, 2.80 Å: 3WGV	3WGU	Data File Jmol Viewer 3WGU 3WGV	Kanai et al. (2013). Kanai R, Ogawa H, Vilsen B, Cornelius F, & Toyoshima C (2013). Crystal structure of a Na⁺-bound Na⁺,K⁺-ATPase preceding the E1P state. Nature 502 :201-206. PubMed Id: 24089211. doi:10.1038/nature12578.
*Na,K-ATPase, phosphorylated form in complex with bufalin: Sus scrofa* E Eukaryota, 3.41 Å** in complex with digoxin, 4.00 Å: 4RET	4RES	Data File Jmol Viewer 4RES 4RET	Laursen et al. (2015). Laursen M, Gregersen JL, Yatime L, Nissen P, & Fedosova NU (2015). Structures and characterization of digoxin- and bufalin-bound Na+,K+-ATPase compared with the ouabain-bound complex. Proc Natl Acad Sci USA 112 :1755-1760. PubMed Id: 25624492. doi:10.1073/pnas.1422997112.
*Na,K-ATPase in the E2P state, with bound Mg²⁺ (P4(3)2(1)2 symmetry): Sus scrofa* E Eukaryota, 3.35 Å** with bound Mg²⁺ and anthroylouabain, 3.90 Å: 7D92 bound Mg²⁺ and anthroylouabain (P2(1)2(1)2(1) symmetry), 3.65 Å: 7D93 bound one Mg²⁺ and one Rb⁺ in the presence of bufalin, 7D94 in complex with beryllium fluoride, 4.62 Å: 4.62 Å: 7DDF in complex with istaroxime, 3.71 Å: 7DDG in complex with digoxin, 3.46 Å: 7DDH in complex with digitoxin, 3.72 Å: 7DDI in complex with ouabain, 2.90 Å: 7DDJ in complex with rostafuroxin, 3.50 Å: 7DDK in complex with bufalin, 3.20 Å: 7DDL	7D91	Data File Jmol Viewer 7D91 7DDG 7D92 7DDJ 7D94 7DDH 7DDI 7D93 7DDF 7DDK 7DDL	Kanai et al. (2021). Kanai R, Cornelius F, Ogawa H, Motoyama K, Vilsen B, & Toyoshima C (2021). Binding of cardiotonic steroids to Na⁺,K⁺-ATPase in the E2P state. Proc Natl Acad Sci U S A 118 1:e2020438118. PubMed Id: 33318128. doi:10.1073/pnas.2020438118.
*Na,K-ATPase in complex with istaroxime: Sus scrofa* E Eukaryota, 3.71 Å** in complex with ouabain, 2.90 Å: 7WYT cryo-EM structures: in the E2P state formed by ATP, 3.40 Å: 7WYU E2P state formed by ATP in the presence of 40 mM Mg²⁺, 3.70 Å: 7WYV E2P state formed by inorganic phosphate, 3.80 Å: 7WYW E2P state formed by ATP with istaroxime, 3.40 Å: 7WYX E2P state formed by inorganic phosphate with istaroxime, 3.90 Å: 7WYY E2P state formed by ATP with ouabain, 3.40 Å: 7WYZ E2P state formed by inorganic phosphate with ouabain, 3.00 Å: 7WZ0	7WYS	Data File Jmol Viewer 7WYS 7WYZ 7WYW 7WYX 7WZ0 7WYU 7WYV 7WYT 7WYY	Kanai et al. (2022). Kanai R, Cornelius F, Vilsen B, & Toyoshima C (2022). Cryoelectron microscopy of Na⁺,K⁺-ATPase in the two E2P states with and without cardiotonic steroids. Proc Natl Acad Sci U S A 119 15:e2123226119. PubMed Id: 35380894. doi:10.1073/pnas.2123226119.
*Na,K-ATPase; pig kidney (E2-BeF_x), in the initial Rb⁺ binding state: Sus scrofa* E Eukaryota, 4.05 Å** early Rb⁺ binding state, rigid body model, 6.92 Å: 7YZR late Rb⁺ binding state, rigid body model, 7.50 Å: 7Z04	7QTV	Data File Jmol Viewer 7QTV 7YZR 7Z04	Fruergaard et al. (2022). Fruergaard MU, Dach I, Andersen JL, Ozol M, Shahsavar A, Quistgaard EM, Poulsen H, Fedosova NU, & Nissen P (2022). The Na⁺,K⁺-ATPase in complex with beryllium fluoride mimics an ATPase phosphorylated state. J Biol Chem 298 9:102317. PubMed Id: 35926706. doi:10.1016/j.jbc.2022.102317.
*Na,K-ATPase; bovine kidney: Bos taurus* E Eukaryota, 3.9 Å**	4XE5	Data File Jmol Viewer 4XE5	Gregersen et al. (2016). Gregersen JL, Mattle D, Fedosova NU, Nissen P, & Reinhard L (2016). Isolation, crystallization, and crystal structure determination of bovine kidney Na⁺,K⁺-ATPase. Acta Crystallogr F Struct Biol Commun 72 :282-287. PubMed Id: 27050261. doi:10.1107/S2053230X1600279X.
*Na,K-ATPase; shark: Squalus acanthias* E Eukaryota, 2.4 Å** Includes α and β subunits plus FXYD regulatory protein. Reveals coordination of K⁺ in the transmembrane binding site.	2ZXE	Data File Jmol Viewer 2ZXE	Shinoda et al. (2009). Shinoda T, Ogawa H, Cornelius F, & Toyoshima C (2009). Crystal structure of the sodium-potassium pump at 2.4 Å resolution. Nature 459 :446-450. PubMed Id: 19458722.
*Na,K-ATPase with bound ouabain and K⁺: Squalus acanthias* E Eukaryota, 2.80 Å**	3A3Y	Data File Jmol Viewer 3A3Y	Ogawa et al. (2009). Ogawa H, Shinoda T, Cornelius F, & Toyoshima C (2009). Crystal structure of the sodium-potassium pump (Na⁺,K⁺-ATPase) with bound potassium and ouabain. Proc Natl Acad Sci USA 106 :13742-13747. PubMed Id: 19666591. doi:10.1073/pnas.0907054106.
*Na,K-ATPase, E2.MgF₄^2-, Tl⁺ substitution at 0.75 min: Squalus acanthias* E Eukaryota, 2.60 Å** Tl⁺ substitution at various times: 1.5 min, 2.70 Å: 5AVR 3.5 min, 2.90 Å: 5AVS 5.0 min, 2.90 Å: 5AVT 7.0 min, 2.55 Å: 5AVU 8.5 min, 2.90 Å: 5AVV 16.5 min, 2.60 Å: 5AVW 20.0 min, 3.30 Å: 5AVX 20.0 min, 3.45 Å: 5AVY 55.0 min, 3.20 Å: 5AVZ 85.0 min, 3.35 Å: 5AW1 85.0 min, 3.20 Å 5AW2 100.0 min, 3.35 Å: 5AW3 Rb⁺ substitution at various times: 1.5 min, 2.80 Å: 5AW4 2.2 min, 2.90 Å: 5AW5 5.5 min, 2.80 Å: 5AW6 11.3 min, 2.90 Å: 5AW7 Rb⁺ crystal, 2.80 Å: 5AW8 native 2K⁺ crystal, 2.80 Å: 5AW9	5AVQ	Data File Jmol Viewer 5AVQ 5AW5 5AVR 5AVS 5AVX 5AVV 5AW9 5AVT 5AW1 5AW3 5AW6 5AW4 5AW8 5AVU 5AVW 5AVY 5AVZ 5AW2 5AW7	Ogawa et al. (2015). Ogawa H, Cornelius F, Hirata A, & Toyoshima C (2015). Sequential substitution of K⁺ bound to Na⁺,K⁺-ATPase visualized by X-ray crystallography. Nat Commun 6 :8004. PubMed Id: 26258479. doi:10.1038/ncomms9004.
*Na,K-ATPase, Na⁺-bound, E1 state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure E1 state with ATP-gamma-S, 2.90 Å: 7E21 K⁺ bound E2 state, 2.00 Å: 7E20	7E1Z	Data File Jmol Viewer 7E1Z 7E21 7E20	Guo et al. (2022). Guo Y, Zhang Y, Yan R, Huang B, Ye F, Wu L, Chi X, Shi Y, & Zhou Q (2022). Cryo-EM structures of recombinant human sodium-potassium pump determined in three different states. Nat Commun 13 1:3957. PubMed Id: 35803952. doi:10.1038/s41467-022-31602-y.
*Na,K-ATPase, Na⁺-occluded state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.70 Å** cryo-EM structure cytoplasmic side-open state, 3.40 Å: 8D3V AMPPCP-bound cytoplasmic side-open state, 3.50 Å: 8D3W K⁺-occluded state, 4.10 Å: 8D3X exoplasmic side-open state, 3.90 Å: 8D3Y	8D3U	Data File Jmol Viewer 8D3U 8D3V 8D3Y 8D3W 8D3X	Nguyen et al. (2022). Nguyen PT, Deisl C, Fine M, Tippetts TS, Uchikawa E, Bai XC, & Levine B (2022). Structural basis for gating mechanism of the human sodium-potassium pump. Nat Commun 13 1:5293. PubMed Id: 36075933. doi:10.1038/s41467-022-32990-x.
*Na,K-ATPase Regulatory Protein FXYD1: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure**	2JO1	Data File Jmol Viewer 2JO1	Teriete et al. (2007). Teriete P, Franzin CM, Choi J, & Marassi FM (2007). Structure of the Na,K-ATPase regulatory protein FXYD1 in micelles. Biochemistry 46 :6774-6783. PubMed Id: 17511473.
*Phospholamban homopentamer: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure** See also 1FJK and 1FJP.	1ZLL	Data File Jmol Viewer 1ZLL 1FJP 1FJK phospholamban pentamer	Oxenoid and Chou (2005). Oxenoid K & Chou JJ (2005). The structure of phospholamban pentamer reveals a channel-like architecture in membranes. Proc Natl Acad Sci USA 102 :10870-10875. PubMed Id: 16043693.
*Phospholamban homopentamer in T state: Homo sapiens* E Eukaryota (expressed in E. coli), NMR Structure**	2KYV	Data File Jmol Viewer 2KYV	Verardi et al. (2011). Verardi R, Shi L, Traaseth NJ, Walsh N, & Veglia G (2011). Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method. Proc Natl Acad Sci USA 108 :9101-9106. PubMed Id: 21576492. doi:10.1073/pnas.1016535108.
*Phospholamban homopentamer in phosphorylated state: Oryctolagus cuniculus* E Eukaryota (expressed in E. coli), NMR Structure**	2M3B	Data File Jmol Viewer 2M3B	Vostrikov et al. (2013). Vostrikov VV, Mote KR, Verardi R, & Veglia G (2013). Structural dynamics and topology of phosphorylated phospholamban homopentamer reveal its role in the regulation of calcium transport. Structure 21 :2119-2130. PubMed Id: 24207128. doi:10.1016/j.str.2013.09.008.
*Plasma Membrane H⁺-ATPase: Arabidopsis thaliana* E Eukaryota, 3.6 Å**	3B8C	Data File Jmol Viewer 3B8C	Pedersen et al. (2007). Pedersen BP, Buch-Pedersen MJ, Morth JP, Palmgren MG, Lauquin GJ, & Nissen P (2007). Crystal structure of the plasma membrane proton pump. Nature 450 :1111-1114. PubMed Id: 18075595.
*Plasma membrane hexameric H⁺-ATPase, autoinhibited state (pH 7.4, C1 symmetry): Saccharomyces cerevisiae* E Eukaryota, 3.20 Å** cryo-EM structure active state (pH 6.0, BeF3^-, conformation 1, C1 symmetry), 3.80 Å 7VH6	7VH5	Data File Jmol Viewer 7VH5 7VH6	Zhao et al. (2021). Zhao P, Zhao C, Chen D, Yun C, Li H, & Bai L (2021). Structure and activation mechanism of the hexameric plasma membrane H⁺-ATPase. Nat Commun 12 1:6439. PubMed Id: 34750373. doi:10.1038/s41467-021-26782-y.
*Copper-transporting ATPase type P_1B: Legionella pneumophila* B Bacteria (expressed in E. coli), 3.20 Å** The structure suggests a three-stage copper transport pathway	3RFU	Data File Jmol Viewer 3RFU	Gourdon et al. (2011). Gourdon P, Liu XY, Skjφrringe T, Morth JP, Mφller LB, Pedersen BP, & Nissen P (2011). Crystal structure of a copper-transporting PIB-type ATPase. Nature 475 :59-64. PubMed Id: 21716286. doi:10.1038/nature10191.
*Copper-transporting ATPase type P_1B (E2P state): Legionella pneumophila* B Bacteria (expressed in E. coli), 2.75 Å**	4BBJ	Data File Jmol Viewer 4BBJ	Andersson et al. (2014). Andersson M, Mattle D, Sitsel O, Klymchuk T, Nielsen AM, Møller LB, White SH, Nissen P, & Gourdon P (2014). Copper-transporting P-type ATPases use a unique ion-release pathway. Nat Struct Mol Biol 21 :43-48. PubMed Id: 24317491. doi:10.1038/nsmb.2721.
*Copper-transporting ATPase type P_1B, E1 state in the presence of copper: Archaeoglobus fulgidus* B Bacteria (expressed in E. coli), 2.70 Å** data collected at the Cu edge, 3.31 Å: 7R0H in the absence of Cu, 4.01 Å: 7R0G	7R0I	Data File Jmol Viewer 7R0I 7R0G 7R0H	Salustros et al. (2022). Salustros N, Grønberg C, Abeyrathna NS, Lyu P, Orädd F, Wang K, Andersson M, Meloni G, & Gourdon P (2022). Structural basis of ion uptake in copper-transporting P_1B-type ATPases. Nat Commun 13 1:5121. PubMed Id: 36045128. doi:10.1038/s41467-022-32751-w.
*Cadmium-transporting ATPase type P_1B-4, E2-BeF₃⁻: Sulfitobacter sp.* B Bacteria (expressed in E. coli), 3.25 Å** E2-AlF₄⁻, 3.11 Å 7QC0	7QBZ	Data File Jmol Viewer 7QBZ 7QC0	Grønberg et al. (2021). Grønberg C, Hu Q, Mahato DR, Longhin E, Salustros N, Duelli A, Lyu P, Bågenholm V, Eriksson J, Rao KU, Henderson DI, Meloni G, Andersson M, Croll T, Godaly G, Wang K, & Gourdon P (2021). Structure and ion-release mechanism of PIB-4-type ATPases. Elife 10 :e73124. PubMed Id: 34951590. doi:10.7554/eLife.73124.
*gastric H⁺,K⁺-ATPase with bound BeF and SCH28080: Sus scrofa* E Eukaryota, 7.0 Å** 2D electron crystallographic structure in ADP-insensitive E₂ state	2XZB	Data File Jmol Viewer 2XZB	Abe et al. (2011). Abe K, Tani K, & Fujiyoshi Y (2011). Conformational rearrangement of gastric H⁺,K⁺-ATPase induced by an acid suppressant. Nat Commun 2 :155. PubMed Id: 21224846.
*gastric H⁺,K⁺-ATPase with bound BYK99: Sus scrofa* E Eukaryota, 6.5 Å** 2D electron crystallographic structure	5Y0B	Data File Jmol Viewer 5Y0B	Abe et al. (2017). Abe K, Shimokawa J, Naito M, Munson K, Vagin O, Sachs G, Suzuki H, Tani K, & Fujiyoshi Y (2017). The cryo-EM structure of gastric H⁺,K⁺-ATPase with bound BYK99, a high-affinity member of K⁺-competitive, imidazo[1,2-a]pyridine inhibitors. Sci Rep 7 :6632. PubMed Id: 28747707. doi:10.1038/s41598-017-06698-8.
*gastric H⁺,K⁺-ATPase with bound vonoprazan: Sus scrofa* E Eukaryota (expressed in HEK293S cells), 2.80 Å** with bound SCH28080, 2.80 Å: 5YLV	5YLU	Data File Jmol Viewer 5YLU 5YLV	Abe et al. (2018). Abe K, Irie K, Nakanishi H, Suzuki H, & Fujiyoshi Y (2018). Crystal structures of the gastric proton pump. Nature 556 7700:214-218. PubMed Id: 29618813. doi:10.1038/s41586-018-0003-8.
*gastric H⁺,K⁺-ATPase, Y799W mutant K⁺-bound E2-MgF state: Sus scrofa* E Eukaryota, 2.5 Å** Y799W mutant, Rb⁺-bound E2-MgF state, 2.6 Å: 6JXI Y799W mutant, Rb⁺-bound E2-AlF state, 2.5 Å: 6JXJ wild-type, Rb⁺-bound E2-MgF state, 4.3 Å: 6JXK	6JXH	Data File Jmol Viewer 6JXH 6JXJ 6JXK 6JXI	Yamamoto et al. (2019). Yamamoto K, Dubey V, Irie K, Nakanishi H, Khandelia H, Fujiyoshi Y, & Abe K (2019). A single K⁺-binding site in the crystal structure of the gastric proton pump. Elife 8 . PubMed Id: 31436534. doi:10.7554/eLife.47701.
*gastric H⁺,K⁺-ATPase complexed with tegoprazan: Sus scrofa* E Eukaryota (expressed in HEK293 cells), 3.00 Å** complexed with PF-03716556, 3.50 Å: 7W48 complexed with soraprazan, 3.10 Å: 7W49 cryo-EM structure: complexed with revaprazan, 2.76 Å: 7W4A	7W47	Data File Jmol Viewer 7W47 7W4A 7W48 7W49	Tanaka et al. (2022). Tanaka S, Morita M, Yamagishi T, Madapally HV, Hayashida K, Khandelia H, Gerle C, Shigematsu H, Oshima A, & Abe K (2022). Structural Basis for Binding of Potassium-Competitive Acid Blockers to the Gastric Proton Pump. J Med Chem 65 11:7843-7853. PubMed Id: 35604136. doi:10.1021/acs.jmedchem.2c00338.
*non-gastric (ng) H⁺,K⁺-ATPase: alpha2 in K⁺E2-AlF state: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.30 Å** X-ray structure. cryo-EM structures: K794A in (K⁺)E2-AlF state, 2.80 Å: 7X21 K794S in 2K⁺ E2-AlF state, 3.00 Å: 7X22 SPWC mutant in 3Na⁺E1-AMPPCPF state, 3.20 Å: 7X23 SPWC mutant in (2K⁺)E2-AlF state, 3.40 Å: 7X24	7X20	Data File Jmol Viewer 7X20 7X24 7X21 7X23 7X22	Young et al. (2022). Young VC, Nakanishi H, Meyer DJ, Nishizawa T, Oshima A, Artigas P, & Abe K (2022). Structure and function of H⁺/K⁺ pump mutants reveal Na⁺/K⁺ pump mechanisms. Nat Commun 13 1:5270. PubMed Id: 36085139. doi:10.1038/s41467-022-32793-0.
*P4-ATPase lipid flippase, autoinhibited Drs2p-Cdc50p: Saccharomyces cerevisiae* E Eukaryota, 2.8 Å** cryo-EM structure partially activated Drs2p-Cdc50p, 3.7 Å: 6ROI activated Drs2p-Cdc50p, 2.9 Å: 6ROJ	6ROH	Data File Jmol Viewer 6ROH 6ROI 6ROJ	Timcenko et al. (2019). Timcenko M, Lyons JA, Januliene D, Ulstrup JJ, Dieudonné T, Montigny C, Ash MR, Karlsen JL, Boesen T, Kühlbrandt W, Lenoir G, Moeller A, & Nissen P (2019). Structure and autoregulation of a P4-ATPase lipid flippase. Nature 571 7765:366-370. PubMed Id: 31243363. doi:10.1038/s41586-019-1344-7.
*P4-ATPase lipid flippase, autoinhibited Drs2p-Cdc50p, apo form: Saccharomyces cerevisiae* E Eukaryota, 2.8 Å** cryo-EM structure in the PI4P-activated form, 3.3 Å: 6SPX	6PSY	Data File Jmol Viewer 6PSY 6SPX	Bai et al. (2019). Bai L, Kovach A, You Q, Hsu HC, Zhao G, & Li H (2019). Autoinhibition and activation mechanisms of the eukaryotic lipid flippase Drs2p-Cdc50p. Nat Commun 10 1. PubMed Id: 31515475. doi:10.1038/s41467-019-12191-9.
*P4-ATPase: phosphatidylcholine flippase Dnf2-Lem3 complex in the E1-ADP state: Saccharomyces cerevisiae* E Eukaryota, 4.05 Å** cryo-EM structure in the E2P transition state, 3.98 Å: 7KY5 in the E2P state, 3.50 &Ariing;: 7KYA Dnf1-Lem3 complex in the apo E1 state, 3.10 Å: 7KY6 Dnf1-Lem3 complex in the E1-ADP state, 3.20 Å: 7KYB Dnf1-Lem3 complex in the E2P state, 2.80 Å: 7KYC Dnf2-Lem3 complex in the apo E1 state, 3.08 Å: 7KY7 Dnf2-Lem3 complex in the E1-ATP state, 3.85 Å: 7KY8	7KY9	Data File Jmol Viewer 7KY9 7KYC 7KY6 7KY7 7KY5 7KYB 7KYA 7KY8	Bai et al. (2020). Bai L, You Q, Jain BK, Duan HD, Kovach A, Graham TR, & Li H (2020). Transport mechanism of P4 ATPase phosphatidylcholine flippases. Elife 9 :e62163. PubMed Id: 33320091. doi:10.7554/eLife.62163.
*P4-ATPase lipid flippase Drs2p-Cdc50p, E1 state with PI4P and Mg²⁺ bound: Saccharomyces cerevisiae* E Eukaryota, 3.00 Å** cryo-EM structure in the E1-AlFx-ADP state, 2.90 Å: 7OH5 in the [PS]E2-AlFx state, 3.00 Å: 7OH6 in the E1-AMPPCP state with PI4P bound, 3.80 Å: 7OH7	7OH4	Data File Jmol Viewer 7OH4 7OH5 7OH6 7OH7	Timcenko et al. (2021). Timcenko M, Dieudonné T, Montigny C, Boesen T, Lyons JA, Lenoir G, & Nissen P (2021). Structural Basis of Substrate-Independent Phosphorylation in a P4-ATPase Lipid Flippase. J Mol Biol 433 16:167062. PubMed Id: 34023399. doi:10.1016/j.jmb.2021.167062.
*P4-ATPase lipid flippase Neo1 in the E2P state: Saccharomyces cerevisiae* E Eukaryota, 3.25 Å** cryo-EM structure in the E2P-transition state, 3.08 Å 7RD7 in the E1-ATP state, 5.64 Å 7RD8	7RD6	Data File Jmol Viewer 7RD6 7RD7 7RD8	Bai et al. (2021). Bai L, Jain BK, You Q, Duan HD, Takar M, Graham TR, & Li H (2021). Structural basis of the P4B ATPase lipid flippase activity. Nat Commun 12 1:5963. PubMed Id: 34645814. doi:10.1038/s41467-021-26273-0.
*P4-ATPase lipid flippase ATP8A1-CDC50 in all states, E1 state class1: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.3 Å** cryo-EM structure. Movie of structural transitions: Science Magazine E1 state class 2, 3.22 Å: 6K7H E1-ATP state class1, 3.08 Å: 6K7J E1-ATP state class2, 3.22 Å: 6K7I E1-ADP-Pi state, 3.04 Å: 6K7K E2P state class2, 2.83 Å: 6K7L E2Pi-PL state, 2.95 Å: 6K7M E1P state, 2.84 Å: 6K7N	6K7G	Data File Jmol Viewer 6K7G 6K7H 6K7J 6K7L 6K7K 6K7M 6K7N 6K7I	Hiraizumi et al. (2019). Hiraizumi M, Yamashita K, Nishizawa T, & Nureki O (2019). Cryo-EM structures capture the transport cycle of the P4-ATPase flippase. Science 365 6458:1149-1155. PubMed Id: 31416931. doi:10.1126/science.aay3353.
*P4-ATPase lipid flippase ATP8B1-CDC50A in E2P autoinhibited state: homo sapiens* E Eukaryota (expressed in Saccharomyces cerevisiae), 3.10 Å** cryo-EM structure	7PY4	Data File Jmol Viewer 7PY4	Dieudonné et al. (2022). Dieudonné T, Herrera SA, Laursen MJ, Lejeune M, Stock C, Slimani K, Jaxel C, Lyons JA, Montigny C, Pomorski TG, Nissen P, & Lenoir G (2022). Autoinhibition and regulation by phosphoinositides of ATP8B1, a human lipid flippase associated with intrahepatic cholestatic disorders. Elife 11 :e75272. PubMed Id: 35416773. doi:10.7554/eLife.75272.
*P4-ATPase lipid flippase ATP11C-CDC50A in E1-AMPPCP state: Homo sapiens* E Eukaryota, 4.0 Å** cryo-EM in E1AlF-ADP state, 3.20 Å: 7BSQ in E1AlF state, 3.30 Å: 7BSS in PtdSer-bound E2BeF state, 3.20 Å: 7BSU in PtdSer-occluded E2-AlF state, 3.00 Å: 7BSV	7BSP	Data File Jmol Viewer 7BSP 7BSQ 7BSS 7BSU 7BSV	Nakanishi et al. (2020). Nakanishi H, Nishizawa T, Segawa K, Nureki O, Fujiyoshi Y, Nagata S, & Abe K (2020). Transport Cycle of Plasma Membrane Flippase ATP11C by Cryo-EM. Cell Reports 32 13. PubMed Id: 32997992. doi:10.1016/j.celrep.2020.108208.
*P4-ATPase lipid flippase ATP11C-CDC50A in stabilized E2P conformation: Homo Sapiens* E Eukaryota (expressed in HEK293 cells), 3.90 Å**	6LKN	Data File Jmol Viewer 6LKN	Nakanishi et al. (2020). Nakanishi H, Irie K, Segawa K, Hasegawa K, Fujiyoshi Y, Nagata S, & Abe K (2020). Crystal structure of a human plasma membrane phospholipid flippase. J Biol Chem 295 30:10180-10194. PubMed Id: 32493773. doi:10.1074/jbc.RA120.014144.
*P4-ATPase lipid flippase ATP11C in a Nanodisc in PtdSer-occluded E2-P_i state.: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.90 Å** cryo-EM structure E1-P state, 3.40 Å 7VSH	7VSG	Data File Jmol Viewer 7VSG 7VSH	Nakanishi et al. (2021). Nakanishi H, Hayashida K, Nishizawa T, Oshima A, & Abe K (2021). Cryo-EM of the ATP11C flippase reconstituted in Nanodiscs shows a distended phospholipid bilayer inner membrane around transmembrane helix 2. J Biol Chem 298 1:101498. PubMed Id: 34922944. doi:10.1016/j.jbc.2021.101498.
*P4-ATPase lipid flippase ATP8A1-CDC50A in the auto-inhibited E2P state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.36 Å** cryo-EM structure CDC50B in the auto-inhibited E2P state, 3.36 Å: 7VGH ATP8B1-CDC50A in the auto-inhibited E2Pi-PS state, 7VGJ	7VGI	Data File Jmol Viewer 7VGI 7VGJ 7VGH	Cheng et al. (2022). Cheng MT, Chen Y, Chen ZP, Liu X, Zhang Z, Chen Y, Hou WT, & Zhou CZ (2022). Structural insights into the activation of autoinhibited human lipid flippase ATP8B1 upon substrate binding. Proc Natl Acad Sci U S A 119 14:e2118656119. PubMed Id: 35349344. doi:10.1073/pnas.2118656119.
*P5-ATPase Spf1 helix dislocase, apo form: Saccharomyces cerevisiae* E Eukaryota, 3.50 Å** cryo-EM structure. Name in humans: ATP13A1. AMP-PCP-bound form, 3.70 Å: 6XMQ BeF3-bound form, 3.30 Å: 6XMT endogenous substrate-bound, 3.30 Å: 6XMU	6XMP	Data File Jmol Viewer 6XMP 6XMQ 6XMU 6XMT	McKenna et al. (2020). McKenna MJ, Sim SI, Ordureau A, Wei L, Harper JW, Shao S, & Park E (2020). The endoplasmic reticulum P5A-ATPase is a transmembrane helix dislocase. Science 369 6511:1583. PubMed Id: 32973005. doi:10.1126/science.abc5809.
*P5B-ATPase, E2P inhibited state: Chaetomium thermophilum* E Eukaryota (expressed in Saccharomyces cerevisiae), 3.50 Å** cryo-EM structure E2P* state, 3.70 Å: 7OP5 E2P_i^AlF/SPM, 3.70 Å: 7OP1 E2.P_iSPM, 3.50 Å: 7OP3	7OP8	Data File Jmol Viewer 7OP8 7OP1 7OP3 7OP5	Li et al. (2021). Li P, Wang K, Salustros N, Grønberg C, & Gourdon P (2021). Structure and transport mechanism of P5B-ATPases. Nat Commun 12 1:3973. PubMed Id: 34172751. doi:10.1038/s41467-021-24148-y.
*P5B-ATPase ATP13A2, BeF-bound E2P-like state: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.80 Å** cryo-EM structure AlF-bound E2-Pi-like state, 2.50 Å 7N72 ADP-AlF-bound E1P-ADP-like state, 2.90 Å 7N73 D508N mutant in the E1-ATP-like state, 2.80 Å 7N74 E1-apo state, Conformation 1, 2.90 Å 7N75 D458N/D962N mutant in the E1-apo state, Conformation 2, 2.90 Å 7N76 D458N/D962N mutant in the AlF-bound E1P-like state, 3.20 Å 7N77 in the E2-Pi state, 3.00 Å 7N78	7N70	Data File Jmol Viewer 7N70 7N77 7N72 7N74 7N78 7N75 7N76 7N73	Sim et al. (2021). Sim SI, von Bülow S, Hummer G, & Park E (2021). Structural basis of polyamine transport by human ATP13A2 (PARK9). Mol Cell 81 22:4635-4649.e8. PubMed Id: 34715013. doi:10.1016/j.molcel.2021.08.017.
*P5B-ATPase ATP13A2, E1-ATP state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure E1P-ADP state, 3.54 Å 7VPJ SPM-bound E2P state, 3.92 Å 7VPK SPM-bound E2Pi state, 3.78 Å 7VPL	7VPI	Data File Jmol Viewer 7VPI 7VPL 7VPJ 7VPK	Tomita et al. (2021). Tomita A, Daiho T, Kusakizako T, Yamashita K, Ogasawara S, Murata T, Nishizawa T, & Nureki O (2021). Cryo-EM reveals mechanistic insights into lipid-facilitated polyamine export by human ATP13A2. Mol Cell 81 23:4799-4809.e5. PubMed Id: 34798056. doi:10.1016/j.molcel.2021.11.001.
*P5B-ATPase ATP13A2, an occluded state: homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.90 Å** cryo-EM structure inhibited state 1, 2.70 Å 7M5X inhibited state 2, 3.00 Å 7M5Y	7M5V	Data File Jmol Viewer 7M5V 7M5X 7M5Y	Tillinghast et al. (2021). Tillinghast J, Drury S, Bowser D, Benn A, & Lee KPK (2021). Structural mechanisms for gating and ion selectivity of the human polyamine transporter ATP13A2. Mol Cell 81 22:4650-4662.e4. PubMed Id: 34715014. doi:10.1016/j.molcel.2021.10.002.
*P5B-ATPase ATP13A2, E1-ATP state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure E1-like state, 5.65 Å: 8IEL E2P state, 3.35 Å: 8IEM E2-Pi state, 3.25 Å: 8IEN nominal E1P state, 3.78 Å: 8IEO putative of E2 state, 4.87 Å: 8IER E1P-ADP state, 3.73 Å: 8IES	8IEK	Data File Jmol Viewer 8IEK 8IEL 8IEN 8IEO 8IER 8IEM 8IES	Mu et al. (2023). Mu J, Xue C, Fu L, Yu Z, Nie M, Wu M, Chen X, Liu K, Bu R, Huang Y, Yang B, Han J, Jiang Q, Chan KC, Zhou R, Li H, Huang A, Wang Y, & Liu Z (2023). Conformational cycle of human polyamine transporter ATP13A2. Nat Commun 14 1:1978. PubMed Id: 37031211. doi:10.1038/s41467-023-37741-0.
*ATP7B ATPase, C983S/C985S/D1027A mutant: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure in presence of ATOX1, 3.30 Å: 7XUK with bound Cu²⁺, in presence of ATOX1, 3.80 Å: 7XUM with bound Pt²⁺, in presence of ATOX1, 3.60 Å: 7XUO with bound AMP-PNP, 4.00 Å: 8IOY	7XUN	Data File Jmol Viewer 7XUN 7XUM 7XUK 7XUO 8IOY	Yang et al. (2023). Yang GM, Xu L, Wang RM, Tao X, Zheng ZW, Chang S, Ma D, Zhao C, Dong Y, Wu S, Guo J, & Wu ZY (2023). Structures of the human Wilson disease copper transporter ATP7B. Cell Rep 42 5:112417. PubMed Id: 37074913. doi:10.1016/j.celrep.2023.112417.
Type IX Secretion System Motors These are α-helical proteins that power secretion of adhesin proteins. See Type IX Secretion System in β-barrel Proteins.
*GldLM proton-powered motor: Flavobacterium johnsoniae* B Bacteria, 3.90 Å** cryo-EM structure. See also 6H3I	6YS8	Data File Jmol Viewer 6YS8	Hennell James et al. (2021). Hennell James R, Deme JC, Kjær A, Alcock F, Silale A, Lauber F, Johnson S, Berks BC, & Lea SM (2021). Structure and mechanism of the proton-driven motor that powers type 9 secretion and gliding motility. Nat Microbiol 6 2:221-233. PubMed Id: 33432152. doi:10.1038/s41564-020-00823-6.
Decarboxylases
*Oxaloacetate Decarboxylase Sodium Pump (OAD) βγ sub-complex: Salmonella typhimurium* B Bacteria (expressed in E. coli), 3.88 Å** cryo-EM structure crystal structure, 4.4 Å: 6IVA	6IWW	Data File Jmol Viewer 6IWW 6IVA	Xu et al. (2020). Xu X, Shi H, Gong X, Chen P, Gao Y, Zhang X, & Xiang S (2020). Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump. Elife 9 . PubMed Id: 32459174. doi:10.7554/eLife.53853.
Hydrolases
*Estrone Sulfatase: Homo sapiens placenta* E Eukaryota, 2.6 Å**	1P49	Data File Jmol Viewer 1P49	Hernandez-Guzman et al. (2003). Hernandez-Guzman FG, Higashiyama T, Pangborn W, Osawa Y, & Ghosh D (2003). Structure of human estrone sulfatase suggests functional roles of membrane association. J Biol Chem 278 :22989-22997. PubMed Id: 12657638.
*Estrone Sulfatase: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.04 Å**	8EG3	Data File Jmol Viewer 8EG3	Ghosh (2022). Ghosh D (2022). Structure of human placental steroid sulfatase at 2.0 angstrom resolution: Catalysis, quaternary association, and a secondary ligand site. J Steroid Biochem Mol Biol 227 :106228. PubMed Id: 36427797. doi:10.1016/j.jsbmb.2022.106228.
*peptidoglycan release complex, SagB-SpdC: Staphylococcus aureus* B Bacteria (expressed in E. coli), 2.60 Å**	6U0O	Data File Jmol Viewer 6U0O	Schaefer et al. (2021). Schaefer K, Owens TW, Page JE, Santiago M, Kahne D, & Walker S (2021). Structure and reconstitution of a hydrolase complex that may release peptidoglycan from the membrane after polymerization. Nat Microbiol 6 1:34-43. PubMed Id: 33168989. doi:10.1038/s41564-020-00808-5.
*alkaline ceramidase 3 (ACER3) determined by Serial Crystallography (SSX) using CrystalDirect: Homo sapiens* E Eukaryota (expressed in Spodoptera frugiperda), 2.60 Å**	6YXH	Data File Jmol Viewer 6YXH	Healey et al. (2021). Healey RD, Basu S, Humm AS, Leyrat C, Cong X, Golebiowski J, Dupeux F, Pica A, Granier S, & Márquez JA (2021). An automated platform for structural analysis of membrane proteins through serial crystallography. Cell Rep Methods 1 6:100102. PubMed Id: 34723237. doi:10.1016/j.crmeth.2021.100102.
Oxygenases
*Particulate methane monooxgenase (pMMO): Methylococcus capsulatus* B Bacteria, 2.8 Å**	1YEW	Data File Jmol Viewer 1YEW Metalloenzyme pMMO subunit pmoA Metalloenzyme pMMO subunit pmoB Metalloenzyme pMMO subunit pmoC	Lieberman & Rosenzweig (2005). Lieberman RL & Rosenzweig AC (2005). Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature 434 :177-181. PubMed Id: 15674245.
*Particulate methane monooxgenase (pMMO): Methylococcus capsulatus* B Bacteria, 2.60 Å** cryo-EM structure	7EV9	Data File Jmol Viewer 7EV9	Chang et al. (2021). Chang WH, Lin HH, Tsai IK, Huang SH, Chung SC, Tu IP, Yu SS, & Chan SI (2021). Copper Centers in the Cryo-EM Structure of Particulate Methane Monooxygenase Reveal the Catalytic Machinery of Methane Oxidation. J Am Chem Soc 143 26:9922-9932. PubMed Id: 34170126. doi:10.1021/jacs.1c04082.
*Particulate methane monooxgenase (pMMO) in a native lipid nanodisc (MC01): Methylococcus capsulatus (Bath)* B Bacteria, 2.14 Å** cryo-EM structure MC02, 2.26 Å 7S4I MC03, 2.16 Å 7S4J MC04, 2.36 Å 7S4K MC05, treated with potassium cyanide, 3.62 Å 7T4O MC06, treated with potassium cyanide and copper, 3.62 Å 7T4P	7S4H	Data File Jmol Viewer 7S4H 7T4O 7S4I 7T4P 7S4J 7S4K	Koo et al. (2022). Koo CW, Tucci FJ, He Y, & Rosenzweig AC (2022). Recovery of particulate methane monooxygenase structure and activity in a lipid bilayer. Science 375 6586:1287-1291. PubMed Id: 35298269. doi:10.1126/science.abm3282.
*Particulate methane monooxgenase (pMMO) in a POPC nanodisc: Methylotuvimicrobium alcaliphilum 20Z* B Bacteria, 2.46 Å** cryo-EM structure	7S4L	Data File Jmol Viewer 7S4L	Koo et al. (2022). Koo CW, Tucci FJ, He Y, & Rosenzweig AC (2022). Recovery of particulate methane monooxygenase structure and activity in a lipid bilayer. Science 375 6586:1287-1291. PubMed Id: 35298269. doi:10.1126/science.abm3282.
*Particulate methane monooxgenase (pMMO) in POPC nanodisc: Methylocystis sp. ATCC 49242* B Bacteria, 2.42 Å** cryo-EM structure	7S4M	Data File Jmol Viewer 7S4M	Koo et al. (2022). Koo CW, Tucci FJ, He Y, & Rosenzweig AC (2022). Recovery of particulate methane monooxygenase structure and activity in a lipid bilayer. Science 375 6586:1287-1291. PubMed Id: 35298269. doi:10.1126/science.abm3282.
*Particulate methane monooxgenase (pMMO): Methylosinus trichosporium OB3b* B Bacteria, 3.90 Å**	3CHX	Data File Jmol Viewer 3CHX	Hakemian et al. (2008). Hakemian AS, Kondapalli KC, Telser J, Hoffman BM, Stemmler TL, & Rosenzweig AC (2008). The metal centers of particulate methane monooxygenase from Methylosinus trichosporium OB3b. Biochemistry 47 :6793-6801. PubMed Id: 18540635.
*kynurenine 3-monooxygenase (KMO), full length, in complex with a pyrazoyl benzoic acid inhibitor: Rattus norvegicus* E Eukaryota (expressed in Spodoptera frugiperda), 3.00 Å** in complex with an inhibitor identified via DNA-encoded chemical library screening, 3.00 Å 6LKE	6LKD	Data File Jmol Viewer 6LKD 6LKE	Mimasu et al. (2021). Mimasu S, Yamagishi H, Kubo S, Kiyohara M, Matsuda T, Yahata T, Thomson HA, Hupp CD, Liu J, Okuda T, & Kakefuda K (2021). Full-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition. Commun Biol 4 1:159. PubMed Id: 33542467. doi:10.1038/s42003-021-01666-5.
Transhydrogenases
*Nicotinamide nucleotide transhydrogenase (TH) proton channel domain, pH 8.5: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.77 Å** holo-TH, 6.92 Å: 4O9U	4O93	Data File Jmol Viewer 4O93 4O9U	Leung et al. (2015). Leung JH, Schurig-Briccio LA, Yamaguchi M, Moeller A, Speir JA, Gennis RB, & Stout CD (2015). Division of labor in transhydrogenase by alternating proton translocation and hydride transfer. Science 347 6218:178-181. PubMed Id: 25574024. doi:10.1126/science.1260451.
*Nicotinamide nucleotide transhydrogenase (TH) proton channel domain, pH 6.5: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.2 Å**	5UNI	Data File Jmol Viewer 5UNI	Padayatti et al. (2017). Padayatti PS, Leung JH, Mahinthichaichan P, Tajkhorshid E, Ishchenko A, Cherezov V, Soltis SM, Jackson JB, Stout CD, Gennis RB, & Zhang Q (2017). Critical Role of Water Molecules in Proton Translocation by the Membrane-Bound Transhydrogenase. Structure 25 :1111-1119.e3. PubMed Id: 28648609. doi:10.1016/j.str.2017.05.022.
*Nicotinamide nucleotide transhydrogenase (TH) proton channel, double face-down conformation: Ovis aries* E Eukaryota, 2.9 Å** cryo-EM structure single face-down conformation, 3.7 Å: 6QUE apo state, 3.7 Å: 6S59	6QTI	Data File Jmol Viewer 6QTI 6QUE 6S59	Kampjut & Sazanov (2019). Kampjut D, & Sazanov LA (2019). Structure and mechanism of mitochondrial proton-translocating transhydrogenase. Nature 573 7773:291-295. PubMed Id: 31462775. doi:10.1038/s41586-019-1519-2.
Mo/Wbis-MGD Oxidoreductases
*Polysulfide Reductase PsrABC (native): Thermus thermophilus* B Bacteria, 2.4 Å** w. bound quinone inhibitor PCP, 2.5 Å: 2PVY w. bound menaquinone, 3.1 Å: 2PVW w. bound quinone, 3.1 Å: 2PVX	2VPZ	Data File Jmol Viewer 2VPZ 2VPW 2VPY 2VPX	Jormakka et al. (2008). Jormakka M, Yokoyama K, Yano T, Tamakoshi M, Akimoto S, Shimamura T, Curmi P, & Iwata S (2008). Molecular mechanism of energy conservation in polysulfide respiration. Nat Struct Mol Biol 15 :730-737. PubMed Id: 18536726.
Oxidoreductases
*Sulfide:quinone oxidoreductase in complex with decylubiquinone: Aquifex aeolicus* B Bacteria, 2.0 Å** "as-purified" protein, 2.30 Å: 3HYV in complex with aurachin C, 2.9 Å: 3HYX This monotopic membrane protein is thought to be buried about 12 Å in the bilayer interface. Listed under TRANSMEMBRANE PROTEINS: ALPHA-HELICAL : Oxidoreductases, MONOTOPIC MEMBRANE PROTEINS : Oxidoreductases (Monotopic).	3HYW	Data File Jmol Viewer 3HYW 3HYV 3HYX	Marcia et al. (2009). Marcia M, Ermler U, Peng G, & Michel H (2009). The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proc Natl Acad Sci USA 106 :9625-9630. PubMed Id: 19487671.
*Electron Transfer Flavoprotein-ubiquinone oxidoreductase (ETF-QO) with bound UQ: Sus scrofa* E Eukaryota, 2.5 Å** UQ-free structure, 2.6 Å: 2GMJ. Because this is a mitochondrial respiratory chain protein, it is listed under TRANSMEMBRANE PROTEINS: ALPHA-HELICAL : Oxidoreductases and MONOTOPIC MEMBRANE PROTEINS : Oxidoreductases (Monotopic).	2GMH	Data File Jmol Viewer 2GMH 2GMJ	Zhang et al. (2006). Zhang J, Frerman FE, & Kim J-JP (2006). Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool. Proc Natl Acad Sci U S A 103 :16212-16217. PubMed Id: 17050691.
*Glycerol-3-phosphate dehydrogenase (GlpD, native): Escherichia coli* B Bacteria, 1.75 Å** SeMet-GlpD, 1.95 Å: 2R4J GlpD-2-PGA, 2.3 Å: 2R45 GlpD-PEP, 2.1 Å: 2R46 GlpD-DHAP, 2.1 Å: 2R4E Listed under MONOTOPIC MEMBRANE PROTEINS : Dehydrogenases, TRANSMEMBRANE PROTEINS: ALPHA-HELICAL : Oxidoreductases.	2QCU	Data File Jmol Viewer 2QCU 2R46 2R45 2R4J 2R4E	Yeh et al. (2008). Yeh JI, Chinte U, & Du S (2008). Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism. Proc. Natl. Acad. Sci. USA 105 :3280-3285. PubMed Id: 18296637.
*NarGHI Nitrate Reductase A: Escherichia coli* B Bacteria, 1.9 Å**	1Q16	Data File Jmol Viewer 1Q16 nitrate reductase A, NarI membrane anchor	Bertero et al. (2003). Bertero MG, Rothery RA, Palak M, Hou C, Lim D, Blasco F, Weiner JH, & Strynadka NC (2003). Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nature Structural Biol 10 :681-687. PubMed Id: 12910261.
*NarGHI Nitrate Reductase A catalytic domain NarG with FS0 cluster: Escherichia coli* B Bacteria, 2.2 Å**	1SIW	Data File Jmol Viewer 1SIW	Rothery et al. (2004). Rothery RA, Bertero MG, Cammack R, Palak M, Blasco F, Strynadka NC, & Weiner JH (2004). The catalytic subunit of Escherichia coli nitrate reductase A contains a novel [4Fe-4S] cluster with a high-spin ground state. Biochemistry 43 :5324-5333. PubMed Id: 15122898.
*NarGHI Nitrate Reductase with pentachlorophenol (PCP): Escherichia coli* B Bacteria, 2.0 Å** K86A mutant, 1.90 Å : 1Y5I. K86A w. PCP, 2.50 Å : 1Y5N. H66Y mutant, 2.50 Å : 1Y5L.	1Y4Z	Data File Jmol Viewer 1Y4Z 1Y5I 1Y5L 1Y5N	Bertero et al. (2005). Bertero MG, Rothery RA, Boroumand N, Palak M, Blasco F, Ginet N, Weiner JH, Strynadka NC (2005). Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A. J Biol Chem 280 :14836-14843. PubMed Id: 15615728.
*NrfH Cytochrome C Quinol Dehydrogenase: Desulfovibrio vulgaris* B Bacteria, 2.3 Å** In complex with NrfA cytochrome c nitrite reductase.	2J7A	Data File Jmol Viewer 2J7A NrfH	Rodrigues et al. (2006). Rodrigues ML, Oliveira TF, Pereira AC & Archer M (2006). X-ray structure of the membrane-bound cytochrome c quinol dehydrogenase NrfH reveals novel haem coordination. EMBO J 25 :5951-5960. PubMed Id: 17139260.
*DsbB-DsbA Periplasmic Oxidase Complex: Escherichia coli* B Bacteria, 3.7 Å** DsbB is a four-helix bundle membrane protein that works with the periplasmic DsbA oxidase to introduce disulfide bonds into periplasmic proteins.	2HI7	Data File Jmol Viewer 2HI7 Cysteine Oxidase DsbB	Inaba et al. (2006). Inaba K, Murakami S, Suzuki M, Nakagawa A, Yamashita E, Okada K, & Ito K (2006). Crystal structure of the DsbA-DsbB complex reveals a mechanism of disulfide bond generation. Cell 127 :789-801. PubMed Id: 17110337.
*DsbB-Fab complex: Escherichia coli* B Bacteria, 3.4 Å** Shows the principal Cys104-Cys130 disulfide Updated DsbB-DsbA complex: 3.7 Å 2ZUP	2ZUQ	Data File Jmol Viewer 2ZUQ 2ZUP	Inaba et al. (2009). Inaba K, Murakami S, Nakagawa A, Iida H, Kinjo M, Ito K, & Suzuki M (2009). Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB. EMBO J 28 :779-791. PubMed Id: 19214188.
*wtDsbB-DsbA(Cys133A)-Q8 Complex: Escherichia coli* B Bacteria, 3.7 Å**	3E9J	Data File Jmol Viewer 3E9J	Malojcic et al. (2008). Malojcic G, Owen RL, Grimshaw JP, & Glockshuber R (2008). Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB. FEBS Lett 582 :3301-3307. PubMed Id: 18775700.
*DsbB in DPC micelles: Escherichia coli* B Bacteria, NMR Structure** w. bound ubiquinone: 2K74	2K73	Data File Jmol Viewer 2K73 2K74	Zhou et al. (2008). Zhou Y, Cierpicki T, Jimenez RH, Lukasik SM, Ellena JF, Cafiso DS, Kadokura H, Beckwith J, & Bushweller JH (2008). NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation. Mol Cell 31 :896-908. PubMed Id: 18922471.
*DsbB in POPE lipid bilayer: Escherichia coli* B Bacteria, 1.35 Å** Cys41Ser mutant. Solid-state NMR used to refine the X-ray structure 2ZUQ	2LTQ	Data File Jmol Viewer 2LTQ	Tang et al. (2013). Tang M, Nesbitt AE, Sperling LJ, Berthold DA, Schwieters CD, Gennis RB, & Rienstra CM (2013). Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer. J Mol Biol 425 :1670-1682. PubMed Id: 23416557. doi:10.1016/j.jmb.2013.02.009.
*DsbB C104S with ubiquinone: Escherichia coli* B Bacteria, 2.90 Å** The protein was stabilized for crystallization using a split superfolder green fluorescent protein (from Aequorea victoria) attached to N- and C-termini of DsbB.	6WVF	Data File Jmol Viewer 6WVF	Liu et al. (2020). Liu S, Li S, Yang Y, & Li W (2020). Termini restraining of small membrane proteins enables structure determination at near-atomic resolution. Sci Adv 6 51:eabe3717. PubMed Id: 33355146. doi:10.1126/sciadv.abe3717.
*CcdA electron transporter: Archaeoglobus fulgidus* A Archaea (expressed in E. coli), NMR structure**	2N4X	Data File Jmol Viewer 2N4X	Williamson et al. (2015). Williamson JA, Cho SH, Ye J, Collet JF, Beckwith JR, & Chou JJ (2015). Structure and multistate function of the transmembrane electron transporter CcdA. Nat Struct Mol Biol 22 :809-814. PubMed Id: 26389738. doi:10.1038/nsmb.3099.
*CcdA electron transporter: Thermus thermophilus* B Bacteria (expressed in E. coli), NMR structure**	5VKV	Data File Jmol Viewer 5VKV	Zhou & Bushweller (2018). Zhou Y, & Bushweller JH (2018). Solution structure and elevator mechanism of the membrane electron transporter CcdA. Nat Struct Mol Biol 25 2:163-169. PubMed Id: 29379172. doi:10.1038/s41594-018-0022-z.
*Vitamin K epoxide reductase: Synechococcus sp.* B Bacteria (expressed in E. coli), 3.60 Å**	3KP9	Data File Jmol Viewer 3KP9	Li et al. (2010). Li W, Schulman S, Dutton RJ, Boyd D, Beckwith J, Rapoport TA (2010). Structure of a bacterial homologue of vitamin K epoxide reductase. Nature 463 :507-512. PubMed Id: 20110994.
*Vitamin K epoxide reductase, C50A mutant in dehydrated state: Synechococcus sp.* B Bacteria (expressed in E. coli), 2.80 Å** C50A mutant, hydrated state, 3.60 Å: 4NV2 C212A mutant, 4.20 Å: 4NV6	4NV5	Data File Jmol Viewer 4NV5 4NV2 4NV6	Liu et al. (2014). Liu S, Cheng W, Fowle Grider R, Shen G, & Li W (2014). Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer. Nat Commun 5 :3110. PubMed Id: 24477003. doi:10.1038/ncomms4110.
*Vitamin K epoxide reductase (VKOR) with warfarin: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 2.20 Å** with phenindione, 2.70 Å: 6WV6 with Brodifacoum, 1.99 Å: 6WVH with Chlorophacinone, 2.48 Å: 6WV7 C43S mutant with warfarin, 3.01 Å: 6WV4 C43S mutant with vitamin K1 epoxide, 2.80 Å: 6WV5	6WV3	Data File Jmol Viewer 6WV3 6WVH 6WV5 6WV6 6WV4 6WV7	Liu et al. (2021). Liu S, Li S, Shen G, Sukumar N, Krezel AM, & Li W (2021). Structural basis of antagonizing the vitamin K catalytic cycle for anticoagulation. Science 371 6524:43. PubMed Id: 33154105. doi:10.1126/science.abc5667.
*Vitamin K epoxide reductase (VKOR-like): Takifugu rubripes* E Eukaryota (expressed in Komagataella pastoris), 2.40 Å** VKOR-like with warfarin, 2.87 Å: 6WVB VKOR-like with vitamin K1 in noncatalytic state, 3.35 Å: 6WV9 VKOR-like with vitamin K1 epoxide at non-catalytic state, 3.35 Å: 6WVA VKOR-like C138S mutant with vitamin K1, 3.01 Å: 6WV8	6WVI	Data File Jmol Viewer 6WVI 6WVB 6WV9 6WV8 6WVA	Liu et al. (2021). Liu S, Li S, Shen G, Sukumar N, Krezel AM, & Li W (2021). Structural basis of antagonizing the vitamin K catalytic cycle for anticoagulation. Science 371 6524:43. PubMed Id: 33154105. doi:10.1126/science.abc5667.
*O₂-tolerant Hydrogenase-1 in complex with cytochrome b: Escherichia coli* B Bacteria, 3.30 Å** Structure includes transmembrane helices.	4GD3	Data File Jmol Viewer 4GD3	Volbeda et al. (2013). Volbeda A, Darnault C, Parkin A, Sargent F, Armstrong FA, & Fontecilla-Camps JC (2013). Crystal Structure of the O₂-Tolerant Membrane-Bound Hydrogenase 1 from Escherichia coli in Complex with Its Cognate Cytochrome b. Structure 21 :184-190. PubMed Id: 23260654. doi:10.1016/j.str.2012.11.010.
*O₂-tolerant Hydrogenase-1 (periplasmic domain): Escherichia coli* B Bacteria, 1.67 Å** Ferricyanide-oxidized form, 2.00 Å: 3USC H₂-reduced form, 1.47 Å: 3UQY	3USE	Data File Jmol Viewer 3USE 3UQY 3USC	Volbeda et al. (2012). Volbeda A, Amara P, Darnault C, Mouesca JM, Parkin A, Roessler MM, Armstrong FA, & Fontecilla-Camps JC (2012). X-ray crystallographic and computational studies of the O₂-tolerant [NiFe]-hydrogenase 1 from Escherichia coli. Proc Natl Acad Sci USA 109 :5305-5310. PubMed Id: 22431599. doi:10.1073/pnas.1119806109.
*Mitochondrial rhodoquinol-fumarate reductase: Ascaris suum* E Eukaryota, 2.81 Å** with flutolanil inhibitor and fumarate substrate, 2.91 Å: 3VRB	3VR8	Data File Jmol Viewer 3VR8 3VRB	Shimizu et al. (2012). Shimizu H, Osanai A, Sakamoto K, Inaoka DK, Shiba T, Harada S, & Kita K (2012). Crystal structure of mitochondrial quinol-fumarate reductase from the parasitic nematode Ascaris suum. J Biochem 151 :589-592. PubMed Id: 22577165. doi:10.1093/jb/mvs051.
*Cytochrome b₅₆₁: Arabidopsis thaliana* E Eukaryota (expressed in E. coli), 1.70 Å** Soaked in 1M ascorbate (10 min), 2.00 Å: 4O79 Soaked in 1M ascorbate (40 min), 2.21 Å: 4O7G	4O6Y	Data File Jmol Viewer 4O6Y 4O79 4O7G	Lu et al. (2014). Lu P, Ma D, Yan C, Gong X, Du M, & Shi Y (2014). Structure and mechanism of a eukaryotic transmembrane ascorbate-dependent oxidoreductase. Proc Natl Acad Sci USA 111 :1813-1818. PubMed Id: 24449903. doi:10.1073/pnas.1323931111.
*Na⁺-pumping NADH:quinone oxidoreductase (Na⁺-NQR): Vibrio cholerae* B Bacteria, 3.50 Å** NqrA_1-377 subunit, crystal form 1, 1.60 Å: 4U9O NqrA_1-377 subunit, crystal form 2, 2.10 Å: 4U9Q NqrC_33-257 subunit, 1.70 Å: 4U9S NrqF_129-408 subunit, 1.55 Å: 4U9U	4P6V	Data File Jmol Viewer 4P6V 4U9U 4U9S 4U9O 4U9Q	Steuber et al. (2014). Steuber J, Vohl G, Casutt MS, Vorburger T, Diederichs K, & Fritz G (2014). Structure of the V. cholerae Na⁺-pumping NADH:quinone oxidoreductase. Nature 516 7529:62-67. PubMed Id: 25471880. doi:10.1038/nature14003.
*Na⁺-translocating ferredoxin: NAD⁺ reductase (Rnf): Clostridium tetanomorphum* B Bacteria, 4.27 Å** cryo-EM structure	7ZC6	Data File Jmol Viewer 7ZC6	Vitt et al. (2022). Vitt S, Prinz S, Eisinger M, Ermler U, & Buckel W (2022). Purification and structural characterization of the Na⁺-translocating ferredoxin: NAD⁺ reductase (Rnf) complex of Clostridium tetanomorphum. Nat Commun 13 1:6315. PubMed Id: 36274063. doi:10.1038/s41467-022-34007-z.
*STEAP1 (STEAP=Six-TM epithelial antigen of the prostate) bound to three Fab120.545 fragments: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.97 Å** cryo-EM structure STEAP1 is unusual in that it lacks the NADPH binding domain and does not exhibit ferric reductase activity.	6Y9B	Data File Jmol Viewer 6Y9B	Oosterheert & Gros (2020). Oosterheert W, & Gros P (2020). Cryo-electron microscopy structure and potential enzymatic function of human six-transmembrane epithelial antigen of the prostate 1 (STEAP1). J Biol Chem 295 28:9502-9512. PubMed Id: 32409586. doi:10.1074/jbc.RA120.013690.
*STEAP4 (STEAP=Six-TM epithelial antigen of the prostate) bound to NADP, FAD, heme and Fe(III)-NTA: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure bound to NADPH, FAD and heme, 3.80 Å: 6HD1	6HCY	Data File Jmol Viewer 6HCY 6HD1	Oosterheert et al. (2018). Oosterheert W, van Bezouwen LS, Rodenburg RNP, Granneman J, Förster F, Mattevi A, & Gros P (2018). Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction. Nat Commun 9 1:4337. PubMed Id: 30337524. doi:10.1038/s41467-018-06817-7.
*DUOX1-DUOXA1 complex of the NADPH oxidase family in the absence of NADPH: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure in the dimer-of-dimer state, 2.70 Å: 6WXU complex in the presence of NADPH, 3.30 &Ariing;: 6WXV	6WXR	Data File Jmol Viewer 6WXR 6WXU 6WXV	Sun (2020). Sun J (2020). Structures of mouse DUOX1-DUOXA1 provide mechanistic insights into enzyme activation and regulation. Nat Struct Mol Biol 27 11:1086-1093. PubMed Id: 32929281. doi:10.1038/s41594-020-0501-x.
*DUOX1-DUOXA1 complex of the NADPH oxidase family, high-calcium state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.60 Å** cryo-EM structure low-calcium state, 2.80 Å: 7D3E	7D3F	Data File Jmol Viewer 7D3F 7D3E	Wu et al. (2021). Wu JX, Liu R, Song K, & Chen L (2021). Structures of human dual oxidase 1 complex in low-calcium and high-calcium states. Nat Commun 12 1:155. PubMed Id: 33420071. doi:10.1038/s41467-020-20466-9.
*NADPH oxidase NOX2: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.20 Å** cryo-EM structure	7U8G	Data File Jmol Viewer 7U8G	Noreng et al. (2022). Noreng S, Ota N, Sun Y, Ho H, Johnson M, Arthur CP, Schneider K, Lehoux I, Davies CW, Mortara K, Wong K, Seshasayee D, Masureel M, Payandeh J, Yi T, & Koerber JT (2022). Structure of the core human NADPH oxidase NOX2. Nat Commun 13 1:6079. PubMed Id: 36241643. doi:10.1038/s41467-022-33711-0.
Heme-Handling Proteins
*CcmF Cytochrome c Heme Lyase: Thermus thermophilus* B Bacteria (expressed in E. coli), 2.67 Å**	6ZMQ	Data File Jmol Viewer 6ZMQ	Brausemann et al. (2021). Brausemann A, Zhang L, Ilcu L, & Einsle O (2021). Architecture of the membrane-bound cytochrome c heme lyase CcmF. Nat Chem Biol 17 7:800-805. PubMed Id: 33958791. doi:10.1038/s41589-021-00793-8.
*Cytochrome c maturation (Ccm) protein system. CcmABCD complex, apo form, closed NBD state: Escherichia coli* B Bacteria, 3.24 Å** cryo-EM structure ligand-free, apo form, open NBD state, 3.98 Å: 7VFJ with bound AMP-PNP in closed NBD state, 3.29 Å: 7F03 in complex with Heme and ATP, 2.86 Å: 7F04 in complex with heme and single ATP, 4.03 Å: 7VFP	7F02	Data File Jmol Viewer 7F02 7VFP 7F04 7F03 7VFJ	Li et al. (2022). Li J, Zheng W, Gu M, Han L, Luo Y, Yu K, Sun M, Zong Y, Ma X, Liu B, Lowder EP, Mendez DL, Kranz RG, Zhang K, & Zhu J (2022). Structures of the CcmABCD heme release complex at multiple states. Nat Commun 13 1:6422. PubMed Id: 36307425. doi:10.1038/s41467-022-34136-5.
*Cytochrome c maturation (Ccm) protein system. CcmABCD complex, apo state: Escherichia coli* B Bacteria, 3.47 Å** cryo-EM structure E154Q mutant, 3.94 Å: 8CEA E154Q mutant, with bound ATP, 3.62 Å: 8CE5 CcmABCDE complex, 3.81 Å: 8CE8	8CE1	Data File Jmol Viewer 8CE1 8CE8 8CE5 8CEA	Ilcu et al. (2023). Ilcu L, Denkhaus L, Brausemann A, Zhang L, & Einsle O (2023). Architecture of the Heme-translocating CcmABCD/E complex required for Cytochrome c maturation. Nat Commun 14 1:5190. PubMed Id: 37626034. doi:10.1038/s41467-023-40881-y.
*CcsBA bifunctional protein (heme transporter & cyt c synthase), Open Conformation: Helicobacter hepaticus* B Bacteria (expressed in E. coli), 3.56 Å** cryo-EM structure closed conformation, 4.14 Å 7S9Z	7S9Y	Data File Jmol Viewer 7S9Y 7S9Z	Mendez et al. (2022). Mendez DL, Lowder EP, Tillman DE, Sutherland MC, Collier AL, Rau MJ, Fitzpatrick JAJ, & Kranz RG (2022). Cryo-EM of CcsBA reveals the basis for cytochrome c biogenesis and heme transport. Nat Chem Biol 18 1:101-108. PubMed Id: 34931065. doi:10.1038/s41589-021-00935-y.
Electron Transport Chain Complexes: Complex I
*Complex I membrane domain: Escherichia coli* B Bacteria, 3.90 Å**	3M9C	Data File Jmol Viewer 3M9C	Efremov et al. (2010). Efremov RG, Baradaran R, & Sazanov LA (2010). High-resolution The architecture of respiratory complex I. Nature 465 :441-445. PubMed Id: 20505720.
*Complex I membrane domain: Escherichia coli* B Bacteria, 3.00 Å**	3RKO	Data File Jmol Viewer 3RKO	Efremov & Sazanov (2011). Efremov RG & Sazanov LA (2011). Structure of the membrane domain of respiratory complex I. Nature 476 :414-420. PubMed Id: 21831629. doi:10.1038/nature10330.
*Complex I complete, focused refinement of cytoplasmic arm: Escherichia coli* B Bacteria, 2.10 Å** cryo-EM structure focused refinement of membrane arm, 3.60 Å 7NYH conformation 1, 3.30 Å 7NYR conformation 2, 3.80 Å 7NYU conformation 3, 3.70 Å 7NYV	7NZ1	Data File Jmol Viewer 7NZ1 7NYR 7NYH 7NYU 7NYV	Kolata & Efremov (2021). Kolata P, & Efremov RG (2021). Structure of Escherichia coli respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation. Elife 10 :e68710. PubMed Id: 34308841. doi:10.7554/eLife.68710.
*Complex I peripheral arm: Escherichia coli* B Bacteria, 2.73 Å** cryo-EM structure	7AWT	Data File Jmol Viewer 7AWT	Schimpf et al. (2022). Schimpf J, Oppermann S, Gerasimova T, Santos Seica AF, Hellwig P, Grishkovskaya I, Wohlwend D, Haselbach D, & Friedrich T (2022). Structure of the peripheral arm of a minimalistic respiratory complex I. Structure 30 1:80-94.e4. PubMed Id: 34562374. doi:10.1016/j.str.2021.09.005.
*Respiratory Complex I, DDM-purified, Apo, Resting state: Escherichia coli* B Bacteria, 3.60 Å** cryo-EM structure DDM-purified, with NADH, Resting state, 3.20 Å: 7P61 DDM/LMNG-purified, Apo, Open state, 2.40 Å: 7P7C DDM/LMNG-purified, Apo, Resting state, 2.70 Å: 7P7E DDM/LMNG-purified, with DQ, Open state, 2.70 Å: 7P7J DDM/LMNG-purified, with DQ, Resting state, 3.10 Å: 7P7K DDM/LMNG-purified, with NADH and FMN, Open state, 3.00 Å: 7P7L DDM/LMNG-purified, inhibited by Piericidin A, Open state, 3.20 Å: 7P7M DDM/LMNG-purified, under Turnover at pH 6, Closed state, 3.40 Å: 7P63 DDM/LMNG-purified, under Turnover at pH 6, Open state, 2.50 Å: 7P64 DDM/LMNG-purified, under Turnover at pH 6, Resting state, 3.00 Å: 7P69 DDM/LMNG-purified, under Turnover at pH 8, Closed state, 2.93 Å: 7Z80 DDM/LMNG-purified, under Turnover at pH 8, Resting state, 3.00 Å: 7ZC5 LMNG-purified, Apo, Open-ready state, 3.36 Å: 7Z7R LMNG-purified, under Turnover at pH 6, Open state, 3.10 Å: 7Z7T LMNG-purified, under Turnover at pH 6, Open-ready state, 2.29 Å: 7Z7V LMNG-purified, under Turnover at pH 6, Closed state, 2.40 Å: 7Z7S LMNG-purified, under Turnover at pH 6, Resting state, 2.69 Å: 7ZCI	7P62	Data File Jmol Viewer 7P62 7Z7R 7P7K 7ZCI 7P7E 7P64 7P61 7Z7V 7P7C 7P7M 7P7L 7ZC5 7Z80 7Z7S 7P63 7P7J 7Z7T 7P69	Kravchuk et al. (2022). Kravchuk V, Petrova O, Kampjut D, Wojciechowska-Bason A, Breese Z, & Sazanov L (2022). A universal coupling mechanism of respiratory complex I. Nature 609 7928:808-814. PubMed Id: 36104567. doi:10.1038/s41586-022-05199-7.
*Complex I complete: Thermus thermophilus* B Bacteria, 4.50 Å**	3M9S	Data File Jmol Viewer 3M9S	Efremov et al. (2010). Efremov RG, Baradaran R, & Sazanov LA (2010). High-resolution The architecture of respiratory complex I. Nature 465 :441-445. PubMed Id: 20505720.
*Complex I complete: Thermus thermophilus* B Bacteria, 3.30 Å** Membrane domain, 3.30 Å: 4HE8	4HEA	Data File Jmol Viewer 4HEA 4HE8	Baradaran et al. (2013). Baradaran R, Berrisford JM, Minhas GS, & Sazanov LA (2013). Crystal structure of the entire respiratory complex I. Nature 494 :443-448. PubMed Id: 23417064. doi:10.1038/nature11871.
*Complex I soluble domain, oxidized (4 mol/ASU): Thermus thermophilus* B Bacteria, 3.30 Å**	2FUG	Data File Jmol Viewer 2FUG	Sazanov & Hinchliffe (2006). Sazanov LA & Hinchliffe P (2006). Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus Science 311 :1430-1436. PubMed Id: 16469879. doi:10.1126/science.1123809.
*Complex I soluble domain, oxidized (2 mol/ASU): Thermus thermophilus* B Bacteria, 3.10 Å** oxidized (4 mol/ASU), 3.15 Å: 3IAS reduced (2 mol/ASU) with bound NADH, 3.10 Å: 3IAM	3I9V	Data File Jmol Viewer 3I9V 3IAM 3IAS	Berrisford & Sazanov (2009). Berrisford JM & Sazanov LA (2009). Structural basis for the mechanism of respiratory complex I J Biol Chem 284 :29773-29783. PubMed Id: 19635800. doi:10.1074/jbc.M109.032144.
*Complex I complete: Thermus thermophilus* B Bacteria, 3.11 Å** with bound NADH, 3.21 Å: 6I1P with bound Decyl-Ubiquinone, 3.60 Å: 6I0D with bound Piericidin A, 3.60 Å: 6Q8O with bound Aureothin, 3.40 Å: 6Q8W with bound Pyridaben, 3.51 Å: 6Q8X cryo-EM structures: NADH dataset, major state, 4.25 Å: 6ZIY NADH dataset, minor state, 6.10 Å: 6ZJN NAD+ dataset, major state, 4.30 Å: 6ZJL NAD+ dataset, minor state, 5.50 Å: 6ZJY	6Y11	Data File Jmol Viewer 6Y11 6ZJN 6ZIY 6ZJL 6I1P 6Q8W 6ZJY 6Q8X 6I0D 6Q8O	Gutiérrez-Fernández et al. (2020). Gutiérrez-Fernández J, Kaszuba K, Minhas GS, Baradaran R, Tambalo M, Gallagher DT, & Sazanov LA (2020). Key role of quinone in the mechanism of respiratory complex I. Nat Commun 11 1:4135. PubMed Id: 32811817. doi:10.1038/s41467-020-17957-0.
*Na⁺-pumping NADH-ubiquinone oxidoreductase, State 1: Vibrio cholerae* B Bacteria, 3.10 Å** cryo-EM structure State 2, 3.10 Å: 7XK4 State 3, 3.10 Å: 7XK5 with aurachin D-42, 3.00 Å: 7XK6 with korormicin, 2.90 Å: 7XK7	7XK3	Data File Jmol Viewer 7XK3 7XK6 7XK5 7XK4 7XK7	Kishikawa et al. (2022). Kishikawa JI, Ishikawa M, Masuya T, Murai M, Kitazumi Y, Butler NL, Kato T, Barquera B, & Miyoshi H (2022). Cryo-EM structures of Na⁺-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae. Nat Commun 13 1:4082. PubMed Id: 35882843. doi:10.1038/s41467-022-31718-1.
*Respiratory Complex I, single-particle cryo-EM structure: Bos taurus* E Eukaryota, 4.95 Å** EM map of deposited in EM Data Bank under accession number EMD-2676	4UQ8	Data File Jmol Viewer 4UQ8	Vinothkumar et al. (2014). Vinothkumar KR, Zhu J, & Hirst J (2014). Architecture of mammalian respiratory complex I. Nature 515 7525:80-84. PubMed Id: 25209663. doi:10.1038/nature13686.
*Respiratory Complex I (class 1 conformation), single-particle cryo-EM structure: Bos taurus* E Eukaryota, 4.27 Å** class 2 conformation, 4.35 Å: 5LC5 class 3 conformation, 5.6 Å: 5LDX	5LDW	Data File Jmol Viewer 5LDW 5LC5 5LDX	Zhu et al. (2016). Zhu J, Vinothkumar KR, & Hirst J (2016). Structure of mammalian respiratory complex I. Nature 536 :354-358. PubMed Id: 27509854. doi:10.1038/nature19095.
*Respiratory Complex I, deactive state: Bos taurus* E Eukaryota, 4.13 Å** cryo-EM structure	5O31	Data File Jmol Viewer 5O31	Blaza et al. (2018). Blaza JN, Vinothkumar KR, & Hirst J (2018). Structure of the Deactive State of Mammalian Respiratory Complex I. Structure 26 2:312-319.e3. PubMed Id: 29395787. doi:10.1016/j.str.2017.12.014.
*Respiratory Complex I in lipid nanodisc, Active-Q10: Bos taurus* E Eukaryota, 2.84 Å** cryo-EM structure Active-apo, 2.76 Å: 7QSL Deactive-ligand (composite), 2.30 Å: 7QSM Deactive-apo, 2.81 Å: 7QSN active state, 3.10 Å: 7QSD	7QSK	Data File Jmol Viewer 7QSK 7QSL 7QSN 7QSM 7QSD	Chung et al. (2022). Chung I, Wright JJ, Bridges HR, Ivanov BS, Biner O, Pereira CS, Arantes GM, & Hirst J (2022). Cryo-EM structures define ubiquinone-10 binding to mitochondrial complex I and conformational transitions accompanying Q-site occupancy. Nat Commun 13 1:2758. PubMed Id: 35589726. doi:10.1038/s41467-022-30506-1.
*Respiratory Complex I in the presence of IM1761092, active class i: Bos taurus* E Eukaryota, 2.30 Å** cryo-EM structure active class ii (Composite map), 2.30 Å: 7R42 active class iii (Composite map), 2.40 Å: 7R43 active class iv (Composite map), 2.40 Å: 7R44	7R41	Data File Jmol Viewer 7R41 7R44 7R42 7R43	Bridges et al. (2023). Bridges HR, Blaza JN, Yin Z, Chung I, Pollak MN, & Hirst J (2023). Structural basis of mammalian respiratory complex I inhibition by medicinal biguanides. Science 379 6630:351-357. PubMed Id: 36701435. doi:10.1126/science.ade3332.
*Respiratory Complex I, active state complex from Q10 dataset: Sus scrofa* E Eukaryota, 2.90 Å** cryo-EM structure Deactive state from Q10 dataset, 3.30 Å7V2D Active state complex rom Q10-NADH dataset, 2.80 Å 7V2E Deactive state complex from Q10-NADH dataset, 3.10 Å 7V2F Active state complex from DQ-NADH dataset, 2.50 Å 7V2H Deactive state complex from DQ-NADH dataset, 2.70 Å 7V2K Active state complex from Q1-NADH dataset, 2.60 Å 7V2R Deactive state complex from Q1-NADH dataset, 2.70 Å 7V30 Active state complex from rotenone dataset, 2.90 Å 7V31 Deactive state complex from rotenone dataset, 3.20 Å 7V32 Active state complex from rotenone-NADH dataset, 2.60 Å 7V33 Deactive state complex from rotenone-NADH dataset, 2.90 Å 7V3M	7V2C	Data File Jmol Viewer 7V2C 7V2R 7V33 7V2E 7V30 7V32 7V31 7V3M 7V2F 7V2H 7V2K 7V2D	Gu et al. (2022). Gu J, Liu T, Guo R, Zhang L, & Yang M (2022). The coupling mechanism of mammalian mitochondrial complex I. Nat Struct Mol Biol 29 2:172-182. PubMed Id: 35145322. doi:10.1038/s41594-022-00722-w.
*Respiratory Complex I, single-particle cryo-EM structure: Ovis aries* E Eukaryota, 3.9 Å**	5LNK	Data File Jmol Viewer 5LNK	Fiedorczuk et al. (2016). Fiedorczuk K, Letts JA, Degliesposti G, Kaszuba K, Skehel M, & Sazanov LA (2016). Atomic structure of the entire mammalian mitochondrial complex I. Nature 538 :406-410. PubMed Id: 27595392. doi:10.1038/nature19794.
*Respiratory Complex I, pH5.5, Open state: Ovis aries* E Eukaryota, 3.25 Å** cryo-EM structure pH5.5, Closed state, 3.44 Å: 7ZDM pH7.4, Open state, 3.16 Å: 7ZD6 pH7.4, Closed state, 3.46 Å: 7ZDH pH9, Open state, 3.88 Å: 7ZDP pH9, Closed state, 3.80 Å: 7ZEB	7ZDJ	Data File Jmol Viewer 7ZDJ 7ZD6 7ZDM 7ZDH 7ZDP 7ZEB	Kravchuk et al. (2022). Kravchuk V, Petrova O, Kampjut D, Wojciechowska-Bason A, Breese Z, & Sazanov L (2022). A universal coupling mechanism of respiratory complex I. Nature 609 7928:808-814. PubMed Id: 36104567. doi:10.1038/s41586-022-05199-7.
*Respiratory Complex I, active state: Mus musculus* E Eukaryota, 3.3 Å** cryo-EM structure in deactive state, 3.9 Å: 6G72	6G2J	Data File Jmol Viewer 6G2J 6G72	Agip et al. (2018). Agip AA, Blaza JN, Bridges HR, Viscomi C, Rawson S, Muench SP, & Hirst J (2018). Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states. Nat Struct Mol Biol 25 :548-556. PubMed Id: 29915388. doi:10.1038/s41594-018-0073-1.
*Respiratory Complex I with inhibitor piericidin A: Mus musculus* E Eukaryota, 3.00 Å** cryo-EM structure active state structure, 3.10 Å: 6ZR2	6ZTQ	Data File Jmol Viewer 6ZTQ 6ZR2	Bridges et al. (2020). Bridges HR, Fedor JG, Blaza JN, Di Luca A, Jussupow A, Jarman OD, Wright JJ, Agip AA, Gamiz-Hernandez AP, Roessler MM, Kaila VRI, & Hirst J (2020). Structure of inhibitor-bound mammalian complex I. Nat Commun 11 1. PubMed Id: 33067417. doi:10.1038/s41467-020-18950-3.
*Respiratory Complex I, deactive state: Mus musculus* E Eukaryota, 3.17 Å** cryo-EM structure ND6-P25L mutant, 3.82 Å: 7AK6	7AK5	Data File Jmol Viewer 7AK5 7AK6	Yin et al. (2021). Yin Z, Burger N, Kula-Alwar D, Aksentijević D, Bridges HR, Prag HA, Grba DN, Viscomi C, James AM, Mottahedin A, Krieg T, Murphy MP, & Hirst J (2021). Structural basis for a complex I mutation that blocks pathological ROS production. Nat Commun 12 1:707. PubMed Id: 33514727. doi:10.1038/s41467-021-20942-w.
*Respiratory Complex I inhibited by IACS-2858: Mus musculus* E Eukaryota, 3.04 Å** cryo-EM structure	7B93	Data File Jmol Viewer 7B93	Chung et al. (2021). Chung I, Serreli R, Cross JB, Di Francesco ME, Marszalek JR, & Hirst J (2021). Cork-in-bottle mechanism of inhibitor binding to mammalian complex I. Sci Adv 7 20:eabg4000. PubMed Id: 33990335. doi:10.1126/sciadv.abg4000.
*Respiratory Complex I inhibited by acetogenin: Mus musculus* E Eukaryota, 3.04 Å** cryo-EM structure	7PSA	Data File Jmol Viewer 7PSA	Grba et al. (2022). Grba DN, Blaza JN, Bridges HR, Agip AA, Yin Z, Murai M, Miyoshi H, & Hirst J (2022). Cryo-electron microscopy reveals how acetogenins inhibit mitochondrial respiratory complex I. J Biol Chem 298 3:101602. PubMed Id: 35063503. doi:10.1016/j.jbc.2022.101602.
*Respiratory Complex I, active state: Drosophila melanogaster* E Eukaryota, 3.28 Å** cryo-EM structure twisted state, 3.68 Å: 8BA0	8B9Z	Data File Jmol Viewer 8B9Z 8BA0	Agip et al. (2023). Agip AA, Chung I, Sanchez-Martinez A, Whitworth AJ, & Hirst J (2023). Cryo-EM structures of mitochondrial respiratory complex I from Drosophila melanogaster. Elife 12 . PubMed Id: 36622099. doi:10.7554/eLife.84424.
*Mitochondrial Complex I: Yarrowia lipolytica* E Eukaryota, 3.8 Å** Anisotropic crystals. Structure was refined at 3.9 Å x 3.9 Å x 3.6 Å.	4WZ7	Data File Jmol Viewer 4WZ7	Zickermann et al. (2015). Zickermann V, Wirth C, Nasiri H, Siegmund K, Schwalbe H, Hunte C, & Brandt U (2015). Structural biology. Mechanistic insight from the crystal structure of mitochondrial complex I. Science 347 6217:44-49. PubMed Id: 25554780. doi:10.1126/science.1259859.
*Mitochondrial Complex I in deactive form: Yarrowia lipolytica* E Eukaryota, 4.3 Å** cryo-EM structure	6GCS	Data File Jmol Viewer 6GCS	Parey et al. (2018). Parey K, Brandt U, Xie H, Mills DJ, Siegmund K, Vonck J, Kühlbrandt W, & Zickermann V (2018). Cryo-EM structure of respiratory complex I at work. Elife 7 :e39213. PubMed Id: 30277212. doi:10.7554/eLife.39213.
*Mitochondrial Complex I: Yarrowia lipolytica* E Eukaryota, 3.20 Å** cryo-EM structure assembly intermediate with NDUFAF2, 3.30 Å: 6RFQ mutant lacking NDUFS4, 4.04 Å: 6RFS	6RFR	Data File Jmol Viewer 6RFR 6RFS 6RFQ	Parey et al. (2019). Parey K, Haapanen O, Sharma V, Köfeler H, Züllig T, Prinz S, Siegmund K, Wittig I, Mills DJ, Vonck J, Kühlbrandt W, & Zickermann V (2019). High-resolution cryo-EM structures of respiratory complex I: Mechanism, assembly, and disease. Sci Adv 5 12:eaax9484. PubMed Id: 31844670. doi:10.1126/sciadv.aax9484.
*Mitochondrial Complex I: Yarrowia lipolytica* E Eukaryota, 2.70 Å** cryo-EM structure complex I sub-stoichiometric sulfur transferase subunit by focused refinement, 3.50 Å: 6YJ5	6YJ4	Data File Jmol Viewer 6YJ4 6YJ5	Grba & Hirst (2020). Grba DN, & Hirst J (2020). Mitochondrial complex I structure reveals ordered water molecules for catalysis and proton translocation. Nat Struct Mol Biol 27 10:892-900. PubMed Id: 32747785. doi:10.1038/s41594-020-0473-x.
*Mitochondrial Complex I, F89A mutant: Yarrowia lipolytica* E Eukaryota, 2.96 Å** cryo-EM structure	6Y79	Data File Jmol Viewer 6Y79	Galemou Yoga et al. (2020). Galemou Yoga E, Parey K, Djurabekova A, Haapanen O, Siegmund K, Zwicker K, Sharma V, Zickermann V, & Angerer H (2020). Essential role of accessory subunit LYRM6 in the mechanism of mitochondrial complex I. Nat Commun 11 1:6008. PubMed Id: 33243981. doi:10.1038/s41467-020-19778-7.
*Membrane-bound hydrogenase ancient respiratory system: Pyrococcus furiosus* A Archaea, 3.7 Å** cryo-EM structure	6CFW	Data File Jmol Viewer 6CFW	Yu et al. (2018). Yu H, Wu CH, Schut GJ, Haja DK, Zhao G, Peters JW, Adams MWW, & Li H (2018). Structure of an Ancient Respiratory System. Cell 173 7:1636-1649.e16. PubMed Id: 29754813. doi:10.1016/j.cell.2018.03.071.
*Complex I-like photosynthetic NAD(P)H, NDH-Fd structure: Thermosynechococcus elongatus* B Bacteria (expressed in E. coli), 3 Å** cryo-EM structure NDH-PQ structure, 3 Å: 6KHJ	6KHI	Data File Jmol Viewer 6KHI 6KHJ	Pan et al. (2020). Pan X, Cao D, Xie F, Xu F, Su X, Mi H, Zhang X, & Li M (2020). Structural basis for electron transport mechanism of complex I-like photosynthetic NAD(P)H dehydrogenase. Nat Commun 11 1. PubMed Id: 32001694. doi:10.1038/s41467-020-14456-0.
*ferredoxin (FD)-NDH-1L complex: Thermosynechococcus elongatus* B Bacteria (expressed in E. coli), 3.2 Å** cryo-EM structure NDH-1LdelV complex, 3.6 Å: 6L7P	6L7O	Data File Jmol Viewer 6L7O 6L7P	Zhang et al. (2020). Zhang C, Shuai J, Ran Z, Zhao J, Wu Z, Liao R, Wu J, Ma W, & Lei M (2020). Structural insights into NDH-1 mediated cyclic electron transfer. Nat Commun 11 1:888. PubMed Id: 32060291. doi:10.1038/s41467-020-14732-z.
*Mrp ancient cation/proton antiporter complex: Anoxybacillus flavithermus* B Bacteria (expressed in E.coli), 2.98 Å** cryo-EM structure	6Z16	Data File Jmol Viewer 6Z16	Steiner & Sazanov (2020). Steiner J, & Sazanov L (2020). Structure and mechanism of the Mrp complex, an ancient cation/proton antiporter. Elife 9 :e59407. PubMed Id: 32735215. doi:10.7554/eLife.59407.
*Formate hydrogenlyase complex, anaerobic preparation, without formate dehydrogenase H: Escherichia coli* B Bacteria, 2.60 Å** cryo-EM structure aerobic preparation, composite structure, 3.40 Å: 7Z0T	7Z0S	Data File Jmol Viewer 7Z0S 7Z0T	Steinhilper et al. (2022). Steinhilper R, Höff G, Heider J, & Murphy BJ (2022). Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli. Nat Commun 13 1:5395. PubMed Id: 36104349. doi:10.1038/s41467-022-32831-x.
*mitochondrial complex I from mung bean: Vigna radiata E Eukaryota, 3.90 Å** cryo-EM structure	6X89	Data File Jmol Viewer 6X89	Maldonado et al. (2020). Maldonado M, Padavannil A, Zhou L, Guo F, & Letts JA (2020). Atomic structure of a mitochondrial complex I intermediate from vascular plants. Elife 9 . PubMed Id: 32840211. doi:10.7554/eLife.56664.
*Mitochondrial Complex I: Brassica oleracea* E Eukaryota, 3.70 Å** cryo-EM structure assembly intermediate, 3.80 Å: 7A24	7A23	Data File Jmol Viewer 7A23 7A24	Soufari et al. (2020). Soufari H, Parrot C, Kuhn L, Waltz F, & Hashem Y (2020). Specific features and assembly of the plant mitochondrial complex I revealed by cryo-EM. Nat Commun 11 1:5195. PubMed Id: 33060577. doi:10.1038/s41467-020-18814-w.
*Mitochondrial Complex I: native complex, closed: Ovis aries* E Eukaryota, 3.80 Å** cryo-EM structure native complex, open1. 3.20 Å: 6ZKP native complex, open2. 3.30 Å: 6ZKQ native open3. 3.50 Å: 6ZKR with NADH, closed. 3.40 Å: 6ZKG with NADH, open1. 3.00 Å: 6ZKH with NADH, open2. 2.80 Å: 6ZKI with NADH, open3. 3.00 Å: 6ZKJ Deactive complex I, open1. 3.10 Å: 6ZKS Deactive complex I, open2. 2.80 Å: 6ZKT Deactive complex I, open3. 3.00 Å: 6ZKU Deactive complex I, open4. 2.90 Å: 6ZKV inhibited by rotenone, closed. 3.70 Å: 6ZKK inhibited by rotenone, open1. 3.10 Å: 6ZKL inhibited by rotenone, open2. 2.80 Å: 6ZKM inhibited by rotenone, open3. 2.90 Å: 6ZKN during turnover, closed. 3.10 Å: 6ZKC during turnover, open1. 2.70 Å: 6ZKD during turnover, open2. 2.60 Å: 6ZKE during turnover, open3. 2.80 Å: 6ZKF Peripheral domain of open complex I, during turnover. 2.30 Å: 6ZK9 Membrane domain of open complex I during turnover. 6ZKA Membrane domain of closed complex I during turnover. 6ZKB	6ZKO	Data File Jmol Viewer 6ZKO 6ZKP 6ZKH 6ZKA 6ZKN 6ZKE 6ZKB 6ZKT 6ZKD 6ZKK 6ZK9 6ZKC 6ZKL 6ZKU 6ZKQ 6ZKJ 6ZKR 6ZKV 6ZKG 6ZKS 6ZKM 6ZKF 6ZKI	Kampjut & Sazanov (2020). Kampjut D, & Sazanov LA (2020). The coupling mechanism of mammalian respiratory complex I. Science 370 6516. PubMed Id: 32972993. doi:10.1126/science.abc4209.
*Mitochondrial Complex I, complete composition: Arabidopsis thaliana* E Eukaryota, 3.41 Å** cryo-EM structure peripheral arm, 2.91 Å 7AQR membrane core, 3.06 Å 7AQQ membrane tip, 3.17 Å 7AQW complex-I closed conformation, 3.53 Å 7AR8	7ARB	Data File Jmol Viewer 7ARB 7AQW 7AR8 7AQQ 7AQR	Klusch et al. (2021). Klusch N, Senkler J, Yildiz Ö, Kühlbrandt W, & Braun HP (2021). A ferredoxin bridge connects the two arms of plant mitochondrial complex I. Plant Cell 33 6:2072-2091. PubMed Id: 33768254. doi:10.1093/plcell/koab092.
*Mitochondrial Complex I, complete composition: Polytomella sp. Pringsheim* E Eukaryota, 3.11 Å** cryo-EM structure peripheral arm, 2.88 Å 7ARC membrane arm, 2.97 Å 7AR9	7ARD	Data File Jmol Viewer 7ARD 7ARC 7AR9	Klusch et al. (2021). Klusch N, Senkler J, Yildiz Ö, Kühlbrandt W, & Braun HP (2021). A ferredoxin bridge connects the two arms of plant mitochondrial complex I. Plant Cell 33 6:2072-2091. PubMed Id: 33768254. doi:10.1093/plcell/koab092.
*Mitochondrial complex I, active state: Mus musculus* E Eukaryota, 2.39 Å** cryo-EM structure with bound piericidin A, 2.84 Å: 8OLT	8OM1	Data File Jmol Viewer 8OM1 8OLT	Grba et al. (2023). Grba DN, Chung I, Bridges HR, Agip AA, & Hirst J (2023). Investigation of hydrated channels and proton pathways in a high-resolution cryo-EM structure of mammalian complex I. Sci Adv 9 31:eadi1359. PubMed Id: 37531432. doi:10.1126/sciadv.adi1359.
Electron Transport Chain Complexes: Complex II
*Fumarate Reductase Complex: Escherichia coli* B Bacteria, 3.3 Å** This structure has been replaced by 1L0V, below.	1FUM	Data File Jmol Viewer 1FUM Fumarate Reductase. 15 kD anchor	Iverson et al. (1999). Iverson TM, Luna-Chavez C, Cecchini G, & Rees DC (1999). Structure of the Escherichia coli fumerate reductase respiratory complex. Science 284 :1961-1966. PubMed Id: 10373108.
*Native Fumarate Reductase Complex: Escherichia coli* B Bacteria, 3.3 Å** +HQNO, 2.7 Å, 1KF6. +DNP-19, 3.6 Å, 1KFY	1L0V	Data File Jmol Viewer 1L0V 1KF6 1KFY Fumarate Reductase. 13 kD anchor	Iverson et al. (2002). Iverson TM, Luna-Chavez C, Croal LR, Cecchini G, & Rees DC (2002). Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. J Biol Chem 277 :16124-16130. PubMed Id: 11850430.
*Fumarate Reductase Complex FrdA, E245Q mutant: Escherichia coli* B Bacteria, 4.22 Å**	5VPN	Data File Jmol Viewer 5VPN	Starbird et al. (2017). Starbird CA, Maklashina E, Sharma P, Qualls-Histed S, Cecchini G, & Iverson TM (2017). Structural and biochemical analyses reveal insights into covalent flavinylation of the Escherichia coli Complex II homolog quinol:fumarate reductase. J Biol Chem 292 :12921-12933. PubMed Id: 28615448. doi:10.1074/jbc.M117.795120.
*Fumarate Reductase Complex: Wolinella succinogenes* B Bacteria, 1.78 Å** This structure supersedes 1QLA at 2.2 Å published by Lancaster et al.. 2BS2 has small unit cell. 1QLB, 2.2 Å, has a larger unit cell.	2BS2	Data File Jmol Viewer 2BS2 1QLB Fumarate Reductase alpha subunit	Madej et al. (2006). Madej MG, Nasiri HR, Hilgendorff NS, Schwalbe H, & Lancaster CR (2006). Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex. EMBO J 25 :4963-4970. PubMed Id: 17024183. doi:10.1038/sj.emboj.7601361. See also: Lancaster et al. (1999). Lancaster CRD, Kröger A, Auer M, & Michel H (1999). Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution. Nature 402 :377-385. PubMed Id: 10586875.
*Formate dehydrogenase-N: Escherichia coli* B Bacteria, 1.6 Å (native structure)** HQNO complex, 2.8 Å: 1KQG	1KQF	Data File Jmol Viewer 1KQF 1KQG formate dehydrogenase-N, beta chain formate dehydrogenase-N, gamma chain	Jormakka et al. (2002). Jormakka M, Tornroth S, Byrne B, & Iwata S (2002). Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295 :1863-1868. PubMed Id: 11884747.
*Succinate:quinone oxidoreductase (SQR, Complex II): Escherichia coli* B Bacteria, 2.6 Å** DNP-17 Complex, 2.9 Å: 1NEN	1NEK	Data File Jmol Viewer 1NEK 1NEN succinate dehydrogenase C subunit succinate dehydrogenase D subunit	Yankovskaya et al. (2003). Yankovskaya V, Horsefield R, Törnroth S, Luna-Chavez C, Miyoshi H, Léger C, Byrne B, Cecchini G, & Iwata S (2003). Architecture of succinate dehydrogenase and reactive oxygen species generation. Science 299 :700-704. PubMed Id: 12560550.
*Succinate:quinone oxidoreductase (SQR, Complex II) with Atpenin A5: Escherichia coli* B Bacteria, 3.10 Å**	2ACZ	Data File Jmol Viewer 2ACZ	Horsefield et al. (2006). Horsefield R, Yankovskaya V, Sexton G, Whittingham W, Shiomi K, Omura S, Byrne B, Cecchini G, & Iwata S (2006). Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction. J Biol Chem 281 :7309-7316. PubMed Id: 16407191.
*Succinate:quinone oxidoreductase (SQR, Complex II) with carboxin in Q-site: Escherichia coli* B Bacteria, 2.40 Å** with pentachlorophenol in Q-site, 3.20 Å: 2WDR with empty Q-site, 3.20 Å: 2WDV	2WDQ	Data File Jmol Viewer 2WDQ 2WDR 2WDV	Ruprecht et al. (2009). Ruprecht J, Yankovskaya V, Maklashina E, Iwata S, & Cecchini G (2009). Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site. J Biol Chem 284 :29836-29846. PubMed Id: 19710024. doi:10.1074/jbc.M109.010058.
*Succinate:quinone oxidoreductase (SQR, Complex II), H207T SdhB mutant: Escherichia coli* B Bacteria, 2.70 Å**	2WP9	Data File Jmol Viewer 2WP9	Ruprecht et al. (2011). Ruprecht J, Iwata S, Rothery RA, Weiner JH, Maklashina E, & Cecchini G (2011). Perturbation of the quinone-binding site of complex II alters the electronic properties of the proximal [3Fe-4S] iron-sulfur cluster J Biol Chem 286 :12756-12765. PubMed Id: 21310949. doi:10.1074/jbc.M110.209874.
*Succinate:quinone oxidoreductase (SQR, Complex II): Escherichia coli* B Bacteria, 3.60 Å** cryo-EM structure resolution 2.50 Å: 7ZJ2	6WU6	Data File Jmol Viewer 6WU6 7ZJ2	Su et al. (2021). Su CC, Lyu M, Morgan CE, Bolla JR, Robinson CV, & Yu EW (2021). A 'Build and Retrieve' methodology to simultaneously solve cryo-EM structures of membrane proteins. Nat Methods 18 1:69-75. PubMed Id: 33408407. doi:10.1038/s41592-020-01021-2.
*Succinate:ubiquinone oxidoreductase (SQR, Complex II; pig heart): Sus scrofa* E Eukaryota, 2.4 Å** with inhibitors, 3.5 Å: 1ZP0	1ZOY	Data File Jmol Viewer 1ZOY 1ZP0 Mito. Respiratory Complex protein CybL Mito. Respiratory protein CybS	Sun et al. (2005). Sun F, Huo X, Zhai Y, Wang A, Xu J, Su D, Bartlam M, & Rao Z (2005). Crystal structure of mitochondrial respiratory membrane protein complex II. Cell 121 :1043-1057. PubMed Id: 15989954.
*Succinate:ubiquinone oxidoreductase (SQR, Complex II; chicken heart) w. carboxin inhibitor: Gallus gallus* E Eukaryota, 2.1 Å** with 3-nitropropionic acid (3-NP) inhibitor, 2.33 Å: 1YQ4 with OAA inhibitor, 2.2 Å: 1YQ3	2FBW	Data File Jmol Viewer 2FBW 1YQ4 1YQ3	Huang et al. (2006). Huang LS, Sun G, Cobessi D, Wang AC, Shen JT, Tung EY, Anderson VE, & Berry EA (2006). 3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme. J Biol Chem 281 :5965-5972. PubMed Id: 16371358.
*Succinate:ubiquinone oxidoreductase (SQR, Complex II; chicken heart) with TEO at the active site: Gallus gallus* E Eukaryota, 1.74 Å** with bound malonate at the active site, 2.40 Å: 2H89	2H88	Data File Jmol Viewer 2H88 2H89	Huang et al. (2006). Huang LS, Shen JT, Wang AC, & Berry EA (2006). Crystallographic studies of the binding of ligands to the dicarboxylate site of Complex II, and the identity of the ligand in the "oxaloacetate-inhibited" state. Biochim Biophys Acta 1757 :1073-1083. PubMed Id: 16935256.
*succinate dehydrogenase Sdh1 complex in the apo form: Mycolicibacterium smegmatis* B Bacteria, 2.88 Å** cryo-EM structure in complex with UQ1, 2.53 Å: 7D6V	7D6X	Data File Jmol Viewer 7D6X 7D6V	Zhou et al. (2021). Zhou X, Gao Y, Wang W, Yang X, Yang X, Liu F, Tang Y, Lam SM, Shui G, Yu L, Tian C, Guddat LW, Wang Q, Rao Z, & Gong H (2021). Architecture of the mycobacterial succinate dehydrogenase with a membrane-embedded Rieske FeS cluster. Proc Natl Acad Sci U S A 118 15:e2022308118. PubMed Id: 33876763. doi:10.1073/pnas.2022308118.
*respiratory complex II in the presence of ubiquinone: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.86 Å** cryo-EM structure	8GS8	Data File Jmol Viewer 8GS8	Du et al. (2023). Du Z, Zhou X, Lai Y, Xu J, Zhang Y, Zhou S, Feng Z, Yu L, Tang Y, Wang W, Yu L, Tian C, Ran T, Chen H, Guddat LW, Liu F, Gao Y, Rao Z, & Gong H (2023). Structure of the human respiratory complex II. Proc Natl Acad Sci U S A 120 18:e2216713120. PubMed Id: 37098072. doi:10.1073/pnas.2216713120.
Electron Transport Chain Complexes: Complex III (Cytochrome bc₁) Information about Cytochrome bc₁
*Cytochrome bc₁: Bos taurus* E Eukaryota, 2.7 Å** Bovine heart mitochondria, 5 subunits	1QCR	Data File Jmol Viewer 1QCR cyto. bc1 complex. Chain C cyto. bc1 complex. Chain D cyto. bc1 complex. Chain G cyto. bc1 complex. Chain J cyto. bc1 complex. Chain K cyto. bc1 complex. Chain E	Xia et al. (1997). Xia D, Yu C-A, Kim H, Xia J-Z, Kachurin AM, Zhang L, Yu L, & Deisenhofer, J (1997). Crystal structure of the cytochrome bc₁complex from bovine heart mitochondria. Science 277 :60-66. PubMed Id: 9204897.
*Cytochrome bc₁: Bos taurus* E Eukaryota, 3.0 Å** Bovine Heart Mitochondria, 11 subunits.	1BGY	Data File Jmol Viewer 1BGY cyto. bc1 complex. Chain C cyto. bc1 complex. Chain D cyto. bc1 complex. Chain G cyto. bc1 complex. Chain J cyto. bc1 complex. Chain K cyto. bc1 complex. Chain E	Iwata et al. (1998). Iwata S, Lee JW, Okada K, Lee JK, Iwata M, Rasmussen B, Link TA, Ramaswamy S, & Jap BK (1998). Complete structure of the 11-subunit bovine mitochondrial cytochrome bc₁complex. Science 281 :64-71. PubMed Id: 9651245.
*Cytochrome bc₁: Bos taurus* E Eukaryota, 2.26 Å** Bovine Heart Mitochondria, with jg144 inhibitor	2FYU	Data File Jmol Viewer 2FYU	Esser et al. (2006). Esser L, Gong X, Yang S, Yu L, Yu CA, & Xia D (2006). Surface-modulated motion switch: capture and release of iron-sulfur protein in the cytochrome bc₁complex. Proc Natl Acad Sci U S A 103 :13045-13050. PubMed Id: 16924113.
*Cytochrome bc₁: Bos taurus* E Eukaryota, 2.40 Å** Bovine Heart Mitochondria, without ubiquinone. w. ubiquinone, 2.60 Å: 1NTZ w. antimycin A₁, 2.60 Å: 1NTK w. NQNO, 3.2 Å: 1NU1	1NTM	Data File Jmol Viewer 1NTM 1NTZ 1NTK 1NU1	Gao et al. (2003). Gao X, Wen X, Esser L, Quinn B, Yu L, Yu CA, & Xia D. (2003). Structural basis for the quinone reduction in the bc₁complex: a comparative analysis of crystal structures of mitochondrial cytochrome bc₁with bound substrate and inhibitors at the Q_isite. Biochemistry 42 :9067-9080. PubMed Id: 12885240.
*Cytochrome bc₁: Bos taurus* E Eukaryota, 2.60 Å** Bovine Heart Mitochondria, w. stigmatellin w. azoxystrobin, 2.69 Å: 1SQB w. myxothiazol, 2.70 Å: 1SQP w. MOAS, 3.00 Å: 1SQQ w. UHDBT, 2.85 Å: 1SQV	1SQX	Data File Jmol Viewer 1SQX 1SQV 1SQB 1SQQ 1SQP	Esser et al. (2004). Esser L, Quinn B, Li YF, Zhang M, Elberry M, Yu L, Yu CA, & Xia D (2004). Crystallographic studies of quinol oxidation site inhibitors: a modified classification of inhibitors for the cytochrome bc₁> complex. J Mol Biol 341 :281-302. PubMed Id: 15312779.
*Cytochrome bc₁: Bos taurus* E Eukaryota, 2.10 Å** Bovine Heart Mitochondria, w. bound antimycin without antimycin, 2.10 Å: 1PP9 with bound stigmatellin, 2.10 Å: 2A06	1PPJ	Data File Jmol Viewer 1PPJ 2A06 1PP9	Huang et al. (2005). Huang LS, Cobessi D, Tung EY, & Berry EA (2005). Binding of the respiratory chain inhibitor antimycin to the mitochondrial bc₁complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern. J Mol Biol 351 :573-597. PubMed Id: 16024040.
*Cytochrome bc₁ in complex with azoxystrobin: Bos taurus* E Eukaryota, 2.8 Å**	6NHG	Data File Jmol Viewer 6NHG	Esser et al. (2019). Esser L, Zhou F, Yu CA, & Xia D (2019). Crystal structure of bacterial cytochrome bc1 in complex with azoxystrobin reveals a conformational switch of the Rieske iron-sulfur protein subunit. J Biol Chem 294 32:12007-12019. PubMed Id: 31182483. doi:10.1074/jbc.RA119.008381.
*Cytochrome bc₁ in complex with tetrahydro-quinolone inhibitor JAG021: Bos taurus* E Eukaryota, 3.50 Å**	6XVF	Data File Jmol Viewer 6XVF	McPhillie et al. (2020). McPhillie MJ, Zhou Y, Hickman MR, Gordon JA, Weber CR, Li Q, Lee PJ, Amporndanai K, Johnson RM, Darby H, Woods S, Li ZH, Priestley RS, Ristroph KD, Biering SB, El Bissati K, Hwang S, Hakim FE, Dovgin SM, Lykins JD, Roberts L, Hargrave K, Cong H, Sinai AP, Muench SP, Dubey JP, Prud'homme RK, Lorenzi HA, Biagini GA, Moreno SN, Roberts CW, Antonyuk SV, Fishwick CWG, & McLeod R (2020). Potent Tetrahydroquinolone Eliminates Apicomplexan Parasites. Front Cell Infect Microbiol 10 :203. PubMed Id: 32626661. doi:10.3389/fcimb.2020.00203.
*Cytochrome bc₁ in complex with inhibitor CK-2-67: Bos taurus* E Eukaryota, 3.20 Å**	7R3V	Data File Jmol Viewer 7R3V	Amporndanai et al. (2022). Amporndanai K, Pinthong N, O'Neill PM, Hong WD, Amewu RK, Pidathala C, Berry NG, Leung SC, Ward SA, Biagini GA, Hasnain SS, & Antonyuk SV (2022). Targeting the Ubiquinol-Reduction (Qi) Site of the Mitochondrial Cytochrome bc1 Complex for the Development of Next Generation Quinolone Antimalarials. Biology (Basel) 11 8:1109. PubMed Id: 35892964. doi:10.3390/biology11081109.
*Cytochrome bc₁: Gallus gallus* E Eukaryota, 3.16 Å** Chicken Heart Mitochondria (native structure) w. bound stigmatellin, 3.5 Å: 2BCC w. bound stigmatellin and antimycin, 3.7 Å: 3BCC	1BCC	Data File Jmol Viewer 1BCC 2BCC 3BCC cyto. bc1 complex. Chain C cyto. bc1 complex. Chain D cyto. bc1 complex. Chain G cyto. bc1 complex. Chain J cyto. bc1 complex. Chain K cyto. bc1 complex. Chain E	Zhang et al. (1998). Zhang ZL, Huang LS, Shulmeister VM, Chi Y-I, Kim K K, Hung L-W, Crofts AR, Berry EA, & Kim S-H (1998). Electron transfer by domain movement in cytochrome bc₁. Nature 392 :677-684. PubMed Id: 9565029.
*Cytochrome bc₁: Saccharomyces cerevisiae* E Eukaryota, 2.3 Å** yeast, 9 subunits.	1EZV	Data File Jmol Viewer 1EZV	Hunte et al. (2000). Hunte C, Koepe J, Lange C, Rossmanith T, & Michel H (2000). Structure at 2.3 Å resolution of cytochrome bc₁complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Structure 8 :669-684. PubMed Id: 10873857.
*Cytochrome bc₁: Saccharomyces cerevisiae* E Eukaryota, 2.3 Å** With phospholipids.	1KB9	Data File Jmol Viewer 1KB9	Lange et al. (2001). Lange C, Nett JH, Trumpower BL, & Hunte C (2001). Specific roles of protein-phospholipid interactions in the yeast cytochrome bc₁complex structure. EMBO J 20 :6591-6600. PubMed Id: 11726495.
*Cytochrome bc₁: Saccharomyces cerevisiae* E Eukaryota, 2.5 Å** With HHDBT inhibitor.	1P84	Data File Jmol Viewer 1P84	Palsdottir et al. (2003). Palsdottir H, Lojero CG, Trumpower BL, & Hunte C (2003). Structure of the yeast cytochrome bc₁complex with a hydroxyquinone anion Q_osite inhibitor bound. J Biol Chem 278 :31303-31311. PubMed Id: 12782631.
*Cytochrome bc₁: Saccharomyces cerevisiae* E Eukaryota, 2.3 Å** With bound stigmatellin.	2IBZ	Data File Jmol Viewer 2IBZ	Lancaster et al. (2007). Lancaster CR, Hunte C, Kelley J 3rd, Trumpower BL, Ditchfield R (2007). A comparison of stigmatellin conformations, free and bound to the photosynthetic reaction center and the cytochrome bc₁complex. J Mol Biol 368 :197-208. PubMed Id: 17337272.
*Cytochrome bc₁: Saccharomyces cerevisiae* E Eukaryota, 1.9 Å** With bound isoform-1 cytochrome c. With bound isoform-2 cytochrome c, 2.50 Å: 3CXH	3CX5	Data File Jmol Viewer 3CX5 3CXH	Solmaz & Hunte (2008). Solmaz SR & Hunte C (2008). Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer. J Biol Chem 283 :17452-17459. PubMed Id: 18390544.
*Cytochrome bc₁: Rhodobacter sphaeroides* B Bacteria, 3.20 Å**	2FYN	Data File Jmol Viewer 2FYN	Esser et al. (2006). Esser L, Gong X, Yang S, Yu L, Yu CA, & Xia D (2006). Surface-modulated motion switch: capture and release of iron-sulfur protein in the cytochrome bc₁complex. Proc Natl Acad Sci U S A 103 :13045-13050. PubMed Id: 16924113.
*Cytochrome bc₁ with azoxystrobin: Rhodobacter sphaeroides* B Bacteria, 3 Å** in complex with stigmatellin A, 3.6 Å: 6NIN	6NHH	Data File Jmol Viewer 6NHH 6NIN	Esser et al. (2019). Esser L, Zhou F, Yu CA, & Xia D (2019). Crystal structure of bacterial cytochrome bc1 in complex with azoxystrobin reveals a conformational switch of the Rieske iron-sulfur protein subunit. J Biol Chem 294 32:12007-12019. PubMed Id: 31182483. doi:10.1074/jbc.RA119.008381.
*Cytochrome bc₁: Rhodobacter capsulatus* B Bacteria, 3.50 Å**	1ZRT	Data File Jmol Viewer 1ZRT	Berry et al. (2004). Berry EA, Huang LS, Saechao LK, Pon NG, Valkova-Valchanova M, & Daldal F (2004). X-Ray Structure of Rhodobacter Capsulatus Cytochrome bc (1): Comparison with its Mitochondrial and Chloroplast Counterparts. Photosynth Res 81 :251-275. PubMed Id: 16034531.
*quinol:cytochrome c/HiPIP oxidoreductase (alternative complex III): Rhodothermus marinus* B Bacteria, 3.87 Å** cryo-EM structure	6F0K	Data File Jmol Viewer 6F0K	Sousa et al. (2018). Sousa JS, Calisto F, Langer JD, Mills DJ, Refojo PN, Teixeira M, Kühlbrandt W, Vonck J, & Pereira MM (2018). Structural basis for energy transduction by respiratory alternative complex III. Nat Commun 9 1. PubMed Id: 29712914. doi:10.1038/s41467-018-04141-8.
*Alternative complex III (ACIII) in SMA nanodiscs: Flavobacterium johnsoniae* B Bacteria, 3.4 Å** cryo-EM structure	6BTM	Data File Jmol Viewer 6BTM	Sun et al. (2018). Sun C, Benlekbir S, Venkatakrishnan P, Wang Y, Hong S, Hosler J, Tajkhorshid E, Rubinstein JL, & Gennis RB (2018). Structure of the alternative complex III in a supercomplex with cytochrome oxidase. Nature 557 7703:123-126. PubMed Id: 29695868. doi:10.1038/s41586-018-0061-y.
*Alternative complex III (ACIII), dithionite reduced: Roseiflexus castenholzii* B Bacteria, 3.50 Å** cryo-EM structure air-oxidized form, 3.20 Å: 6LOD	6LOE	Data File Jmol Viewer 6LOE 6LOD	Shi et al. (2020). Shi Y, Xin Y, Wang C, Blankenship RE, Sun F, & Xu X (2020). Cryo-EM structures of the air-oxidized and dithionite-reduced photosynthetic alternative complex III from Roseiflexus castenholzii. Sci Adv 6 31:eaba2739. PubMed Id: 32832681. doi:10.1126/sciadv.aba2739.
*Cytochrome bc₁ apo structure: "Aquifex aeolicus"* B Bacteria, 3.28 Å** cro-EM structure inhibited complex, 3.22 Å: 6KLV	6KLS	Data File Jmol Viewer 6KLS 6KLV	Zhu et al. (2020). Zhu G, Zeng H, Zhang S, Juli J, Pang X, Hoffmann J, Zhang Y, Morgner N, Zhu Y, Peng G, Michel H, & Sun F (2020). A 3.3 Å-Resolution Structure of Hyperthermophilic Respiratory Complex III Reveals the Mechanism of Its Thermal Stability. Angew Chem Int Ed Engl 59 1:343-351. PubMed Id: 31778296. doi:10.1002/anie.201911554.
*Complex III₂ (Cytochrome bc1 homodimer), inhibitor free: Candida albicans* E Eukaryota, 3.00 Å** cryo-EM structure Rieske head domain in b position, 3.20 Å 7RJB Rieske head domain in intermediate position, 3.30 Å 7RJC Rieske head domain in c position, 3.20 Å 7RJD Inz-5 bound, 3.30 Å 7RJE	7RJA	Data File Jmol Viewer 7RJA 7RJE 7RJD 7RJC 7RJB	Di Trani et al. (2022). Di Trani JM, Liu Z, Whitesell L, Brzezinski P, Cowen LE, & Rubinstein JL (2022). Rieske head domain dynamics and indazole-derivative inhibition of Candida albicans complex III. Structure 30 1:129-138.e4. PubMed Id: 34525326. doi:10.1016/j.str.2021.08.006.
*Complex III₂ (Cytochrome bc1 homodimer), combined datasets, consensus refinement: Yarrowia lipolytica* E Eukaryota, 2.00 Å** cryo-EM structure atovaquone and antimycin A bound, 3.30 Å: 8AB7 ascorbate-reduced with decylubiquinone, Rieske domain in b position, 2.60 Å: 8AB8 ascorbate-reduced, Rieske domain in b position, 3.30 Å: 8AB9 ascorbate-reduced, Rieske domain in intermediate position, 3.20 Å: 8ABA ascorbate-reduced, Rieske domain in c position, 3.20 Å: 8ABB ferricyanide-oxidized, Rieske domain in b position, 2.30 Å: 8ABE ferricyanide-oxidized, Rieske domain in intermediate position, 2.30 Å: 8ABF ferricyanide-oxidized, Rieske domain in c position, 2.30 Å: 8ABG antimycin A bound, Rieske domain in b position, 3.00 Å: 8ABH antimycin A bound, Rieske domain in intermediate position, 3.00 Å: 8ABI antimycin A bound, Rieske domain in c position, 3.70 Å: 8ABJ decylubiquinol bound, Rieske domain in b position, 2.50 Å: 8ABK decylubiquinol and antimycin A bound, consensus refinement, 2.10 Å: 8ABL apo, Rieske domain in b position, 2.80 Å: 8ABM apo, Rieske domain in intermediate position, 2.80 Å: 8AC3 apo, Rieske domain in c position, 2.70 Å: 8AC4 decylubiquinol bound, oxidised, Rieske domain in b position, 3.10 Å:8AC5	8AB6	Data File Jmol Viewer 8AB6 8AB7 8ABB 8ABM 8AB9 8ABH 8AC4 8AB8 8ABA 8ABE 8ABL 8ABG 8ABJ 8AC5 8ABK 8ABI 8ABF 8AC3	Wieferig & Kühlbrandt (2023). Wieferig JP, & Kühlbrandt W (2023). Analysis of the conformational heterogeneity of the Rieske iron-sulfur protein in complex III2 by cryo-EM. IUCrJ 10 :27-37. PubMed Id: 36598500. doi:10.1107/S2052252522010570.
Electron Transport Chain Complexes: Cytochrome b₆f of Oxygenic Photosynthesis
*Cytochrome b₆f complex: Mastigocladus laminosus* B Bacteria, 3.0 Å** (Original PDB file 1UM3 replaced by 1VF5)	1VF5	Data File Jmol Viewer 1VF5 1UM3 cyt. b6f complex, cyto b6 subunit cyt. b6f complex, subunit IV cyt. b6f complex, cytochrome f cyt. b6f complex, Rieske iron-sulfur protein cyt. b6f complex, PetL cyt. b6f complex, PetM cyt. b6f complex, PetG cyt. b6f complex, PetN	Kurisu et al. (2003). Kurisu G, Zhang H, Smith JL, & Cramer WA (2003). Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science 302 :1009-1014. PubMed Id: 14526088.
*Cytochrome b₆f complex: Mastigocladus laminosus* B Bacteria, 3.80 Å** In complex with quinone analogue inhibitor DBMIB.	2D2C	Data File Jmol Viewer 2D2C	Yan et al. (2006). Yan J, Kurisu G, & Cramer WA (2006). Intraprotein transfer of the quinone analogue inhibitor 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone in the cytochrome b₆f complex. Proc Natl Acad Sci U S A 103 :69-74. PubMed Id: 16371475.
*Cytochrome b₆f complex, native structure: Mastigocladus laminosus* B Bacteria, 3.00 Å** In complex with NQNO, 3.55 Å: 2E75 In complex with TDS, 3.41 Å: 2E76	2E74	Data File Jmol Viewer 2E74 2E75 2E76	Yamashita et al. (2007). Yamashita E, Zhang H, & Cramer WA (2007). Structure of the cytochrome b₆f complex: quinone analogue inhibitors as ligands of heme cn. J Mol Biol 370 :39-52. PubMed Id: 17498743.
*Cytochrome b₆f complex with bound TDS:: Mastigocladus laminosus* B Bacteria, 3.07 Å** with bound inhibitor NQNO, 3.25 Å: 4H0L	4H13	Data File Jmol Viewer 4H13 4H0L	Hasan et al. (2013). Hasan SS, Yamashita E, Baniulis D, & Cramer WA (2013). Quinone-dependent proton transfer pathways in the photosynthetic cytochrome b₆f complex. Proc Natl Acad Sci USA 110 :4297-4302. PubMed Id: 23440205. doi:10.1073/pnas.1222248110.
*Cytochrome b₆f complex: Chlamydomonas reinhardtii* E Eukaryota, 3.1 Å**	1Q90	Data File Jmol Viewer 1Q90	Stroebel et al. (2003). Stroebel D, Choquet Y, Popot JL, & Picot D (2003). An atypical haem in the cytochrome b(6)f complex. Nature 426 :413-418. PubMed Id: 14647374.
*Cytochrome b₆f complex: Nostoc sp. PCC 7120* B Bacteria, 3.0 Å**	2ZT9	Data File Jmol Viewer 2ZT9	Baniulis et al. (2010). Baniulis D, Yamashita E, Whitelegge JP, Zatsman AI, Hendrich MP, Hasan SS, Ryan CM, & Cramer WA (2010). Structure-function, stability, and chemical modification of the cyanobacterial cytochrome b₆f complex from Nostoc sp. PCC 7120. J Biol Chem 284 :9861-9869. PubMed Id: 19189962.
*Cytochrome b₆f complex: Nostoc sp. PCC 7120* B Bacteria, 2.70 Å**	4H44	Data File Jmol Viewer 4H44	Hasan et al. (2013). Hasan SS, Yamashita E, Baniulis D, & Cramer WA (2013). Quinone-dependent proton transfer pathways in the photosynthetic cytochrome b₆f complex. Proc Natl Acad Sci USA 110 :4297-4302. PubMed Id: 23440205. doi:10.1073/pnas.1222248110.
*dimeric cytochrome b₆f complex with bound thylakoid lipids and plastoquinones: Spinacia oleracea* E Eukaryota, 3.58 Å** cryo-EM structure	6RQF	Data File Jmol Viewer 6RQF	Malone et al. (2019). Malone LA, Qian P, Mayneord GE, Hitchcock A, Farmer DA, Thompson RF, Swainsbury DJK, Ranson NA, Hunter CN, & Johnson MP (2019). Cryo-EM structure of the spinach cytochrome b₆f complex at 3.6 Å resolution. Nature 575 7783:535-539. PubMed Id: 31723268. doi:10.1038/s41586-019-1746-6.
*dimeric cytochrome b₆f complex with bound plastoquinones: Spinacia oleracea* E Eukaryota, 2.70 Å** cryo-EM structure high-resolution structure, 2.13 Å resolution: 7ZYV	7QRM	Data File Jmol Viewer 7QRM 7ZYV	Sarewicz et al. (2023). Sarewicz M, Szwalec M, Pintscher S, Indyka P, Rawski M, Pietras R, Mielecki B, Koziej Ł, Jaciuk M, Glatt S, & Osyczka A (2023). High-resolution cryo-EM structures of plant cytochrome b₆f at work. Sci Adv 9 2:eadd9688. PubMed Id: 36638176. doi:10.1126/sciadv.add9688.
*Dimeric cytochrome b6f-PetP complex: Synechocystis sp. PCC 6803* E Eukaryota, 2.80 Å** cryo-EM structure without PetP, 2.80 Å: 7ZXY	7ROW	Data File Jmol Viewer 7ROW 7ZXY	Proctor et al. (2022). Proctor MS, Malone LA, Farmer DA, Swainsbury DJK, Hawkings FR, Pastorelli F, Emrich-Mills TZ, Siebert CA, Hunter CN, Johnson MP, & Hitchcock A (2022). Cryo-EM structures of the Synechocystis sp. PCC 6803 cytochrome b6f complex with and without the regulatory PetP subunit. Biochem J 479 13:1487-1503. PubMed Id: 35726684. doi:10.1042/BCJ20220124.
Electron Transport Chain Complexes: Complex IV (Cytochrome C Oxidase) ( Information about cytochrome c oxidases)
*Cytochrome C Oxidase, aa₃: Bos taurus (bovine) heart mitochndria* E Eukaryota, 2.8 Å**	1OCC	Data File Jmol Viewer 1OCC cyto. C oxidase. Subunit I cyto. C oxidase. Subunit II cyto. C oxidase. Subunit III cyto. C oxidase. Subunit IV cyto. C oxidase. Subunit VIa cyto. C oxidase. Subunit VIc cyto. C oxidase. Subunit VIIa cyto C oxidase. Subunit VIIb cyto. C oxidase. Subunit VIIc cyto. C oxidase. Subunit VIII	Tsukihara et al. (1996). Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, & Yoshikawa S (1996). The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272 :1136-1144. PubMed Id: 8638158.
*Fully Oxidized Cytochrome C Oxidase, aa₃: Bos taurus (bovine) heart mitochndria* E Eukaryota, 1.80 Å** Fully reduced form, 1.90 Å: 1V55	1V54	Data File Jmol Viewer 1V54 1V55	Tsukihara et al. (2003). Tsukihara T, Shimokata K, Katayama Y, Shimada H, Muramoto K, Aoyama H, Mochizuki M, Shinzawa-Itoh K, Yamashita E, Yao M, Ishimura Y, Yoshikawa S (2003). The low-spin heme of cytochrome c oxidase as the driving element of the proton-pumping process. Proc Natl Acad Sci USA 100 :15304-15309. PubMed Id: 14673090.
*Cytochrome C Oxidase, aa₃ with bound cyanide: Bos taurus* E Eukaryota, 2.00 Å**	3X2Q	Data File Jmol Viewer 3X2Q	Yano et al. (2015). Yano N, Muramoto K, Mochizuki M, Shinzawa-Itoh K, Yamashita E, Yoshikawa S, & Tsukihara T (2015). X-ray structure of cyanide-bound bovine heart cytochrome c oxidase in the fully oxidized state at 2.0 Å resolution. Acta Crystallogr F Struct Biol Commun 71 :726-730. PubMed Id: 26057802. doi:10.1107/S2053230X15007025.
*Cytochrome C Oxidase in complex with cytochrome c: Bos taurus* E Eukaryota, 2.0 Å** cytochrome c in the structure is from horse (Equus caballus).	5IY5	Data File Jmol Viewer 5IY5	Shimada et al. (2017). Shimada S, Shinzawa-Itoh K, Baba J, Aoe S, Shimada A, Yamashita E, Kang J, Tateno M, Yoshikawa S, & Tsukihara T (2017). Complex structure of cytochrome c-cytochrome c oxidase reveals a novel protein-protein interaction mode. EMBO J 36 :291-300. PubMed Id: 27979921. doi:10.15252/embj.201695021.
*Cytochrome C Oxidase at neutral pH: Bos taurus* E Eukaryota, 1.77 Å** crystallized using a fluorinated detergent	5XDQ	Data File Jmol Viewer 5XDQ	Luo et al. (2017). Luo F, Shinzawa-Itoh K, Hagimoto K, Shimada A, Shimada S, Yamashita E, Yoshikawa S, & Tsukihara T (2017). Structure of bovine cytochrome c oxidase crystallized at a neutral pH using a fluorinated detergent. Acta Crystallogr F Struct Biol Commun 73 :416-422. PubMed Id: 28695851. doi:10.1107/S2053230X17008834.
*Cytochrome C Oxidase with bound CO by serial femtosecond x-ray: Bos taurus* E Eukaryota, 2.3 Å** by synchrotron light source, 1.95 Å: 5WAU	5W97	Data File Jmol Viewer 5W97 5WAU	Ishigami et al. (2017). Ishigami I, Zatsepin NA, Hikita M, Conrad CE, Nelson G, Coe JD, Basu S, Grant TD, Seaberg MH, Sierra RG, Hunter MS, Fromme P, Fromme R, Yeh SR, & Rousseau DL (2017). Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature. Proc Natl Acad Sc. USA 114 :8011-8016. PubMed Id: 28698372. doi:10.1073/pnas.1705628114.
*Cytochrome c oxidase with bound azide (4-day soak, 20 mM azide): Bos taurus* E Eukaryota, 1.85 Å** 2-day soak, 20 mM azide, 1.85 Å: 5Z85 3-day soak, 20 mM azide, 1.85 Å: 5Z86 2-day soak, 2 mM azide, 1.9 Å: 5ZCO 2-day soak, 20 mM azide, 1.65 Å: 5ZCP 2-day soak, 10 mM azide, 1.65 Å: 5ZCQ alternate model of 4-day soak, 20 mM azide, 1.85 Å: 8GVM	5Z84	Data File Jmol Viewer 5Z84 5ZCQ 5Z85 5ZCO 8GVM 5ZCP 5Z86	Shimada et al. (2018). Shimada A, Hatano K, Tadehara H, Yano N, Shinzawa-Itoh K, Yamashita E, Muramoto K, Tsukihara T, & Yoshikawa S (2018). X-ray structural analyses of azide-bound cytochrome c oxidases reveal that the H-pathway is critically important for the proton-pumping activity. J Biol Chem 293 38:14868-14879. PubMed Id: 30077971. doi:10.1074/jbc.RA118.003123.
*Cytochrome C Oxidase, oxidized form: Bos taurus* E Eukaryota, 1.75 Å** time-resolved serial femtosecond structure P_R intermediate, 2.4 Å: 6NKN reduced form, 1.75 Å: 6NMF	6NMP	Data File Jmol Viewer 6NMP 6NKN 6NMF	Ishigami et al. (2019). Ishigami I, Lewis-Ballester A, Echelmeier A, Brehm G, Zatsepin NA, Grant TD, Coe JD, Lisova S, Nelson G, Zhang S, Dobson ZF, Boutet S, Sierra RG, Batyuk A, Fromme P, Fromme R, Spence JCH, Ros A, Yeh SR, & Rousseau DL (2019). Snapshot of an oxygen intermediate in the catalytic reaction of cytochrome c oxidase. Proc Natl Acad Sci USA 116 9:3572-3577. PubMed Id: 30808749. doi:10.1073/pnas.1814526116.
*Cytochrome C Oxidase under low-dose x-ray conditions: Bos taurus* E Eukaryota, 1.9 Å**	6J8M	Data File Jmol Viewer 6J8M	Ueno et al. (2019). Ueno G, Shimada A, Yamashita E, Hasegawa K, Kumasaka T, Shinzawa-Itoh K, Yoshikawa S, Tsukihara T, & Yamamoto M (2019). Low-dose X-ray structure analysis of cytochrome c oxidase utilizing high-energy X-rays. J Synchrotron Radiat 26 :912-921. PubMed Id: 31274413. doi:10.1107/S1600577519006805.
*Cytochrome C Oxidase, monomeric, fully-oxidized state: Bos taurus* E Eukaryota, 1.85 Å** fully reduced state, 1.95 Å: 6JY4	6JY3	Data File Jmol Viewer 6JY3 6JY4	Shinzawa-Itoh et al. (2019). Shinzawa-Itoh K, Sugimura T, Misaki T, Tadehara Y, Yamamoto S, Hanada M, Yano N, Nakagawa T, Uene S, Yamada T, Aoyama H, Yamashita E, Tsukihara T, Yoshikawa S, & Muramoto K (2019). Monomeric structure of an active form of bovine cytochrome c oxidase. Proc Natl Acad Sci USA 116 40:19945-19951. PubMed Id: 31533957. doi:10.1073/pnas.1907183116.
*Cytochrome C Oxidase with P-form and F-form intermediates: Bos taurus* E Eukaryota, 1.80 Å**	6JUW	Data File Jmol Viewer 6JUW	Shimada et al. (2020). Shimada A, Etoh Y, Kitoh-Fujisawa R, Sasaki A, Shinzawa-Itoh K, Hiromoto T, Yamashita E, Muramoto K, Tsukihara T, & Yoshikawa S (2020). X-ray structures of catalytic intermediates of cytochrome c oxidase provide insights into its O₂ activation and unidirectional proton-pump mechanisms. J Biol Chem 295 17:5818-5833. PubMed Id: 32165497. doi:10.1074/jbc.RA119.009596.
*Cytochrome C Oxidase, catalytic intermediate, IO10: Bos taurus* E Eukaryota, 1.74 Å** catalytic intermediate of O, 1.84 Å 7D5W catalytic intermediate of E, 1.76 Å 7CP5	7D5X	Data File Jmol Viewer 7D5X 7CP5 7D5W	Shimada et al. (2021). Shimada A, Hara F, Shinzawa-Itoh K, Kanehisa N, Yamashita E, Muramoto K, Tsukihara T, & Yoshikawa S (2021). Critical roles of the Cu_B site in efficient proton pumping as revealed by crystal structures of mammalian cytochrome c oxidase catalytic intermediates. J Biol Chem 297 3:100967. PubMed Id: 34274318. doi:10.1016/j.jbc.2021.100967.
*Cytochrome C Oxidase, oxidized, with reduced metal centers induced by synchrotron X-ray exposure: Bos taurus* E Eukaryota, 2.35 Å** annealed structure, 2.45 Å 7TII by synchrotron X-rays, 1.90 Å 7TIE reduced form obtained by synchrotron X-rays, 1.93 Å 7THU	7TIH	Data File Jmol Viewer 7TIH 7TII 7TIE 7THU	Ishigami et al. (2022). Ishigami I, Russi S, Cohen A, Yeh SR, & Rousseau DL (2022). Temperature-dependent structural transition following X-ray-induced metal center reduction in oxidized cytochrome c oxidase. J Biol Chem 298 4:101799. PubMed Id: 35257742. doi:10.1016/j.jbc.2022.101799.
*Cytochrome C Oxidase, fully oxidized state: Bos taurus* E Eukaryota, 1.50 Å** fully reduced state, 1.60 Å: 5B1B alternate model of fully oxidized state, 1.50 Å: 7YPY	5B1A	Data File Jmol Viewer 5B1A 5B1B 7YPY	Yano et al. (2016). Yano N, Muramoto K, Shimada A, Takemura S, Baba J, Fujisawa H, Mochizuki M, Shinzawa-Itoh K, Yamashita E, Tsukihara T, & Yoshikawa S (2016). The Mg²⁺-containing Water Cluster of Mammalian Cytochrome c Oxidase Collects Four Pumping Proton Equivalents in Each Catalytic Cycle. J Biol Chem 291 46:23882-23894. PubMed Id: 27605664.
*Cytochrome C Oxidase, apo form: Bos taurus* E Eukaryota, 2.20 Å** with bound an allosteric inhibitor T113, 2.20 Å: 7XMB	7XMA	Data File Jmol Viewer 7XMA 7XMB	Nishida et al. (2022). Nishida Y, Yanagisawa S, Morita R, Shigematsu H, Shinzawa-Itoh K, Yuki H, Ogasawara S, Shimuta K, Iwamoto T, Nakabayashi C, Matsumura W, Kato H, Gopalasingam C, Nagao T, Qaqorh T, Takahashi Y, Yamazaki S, Kamiya K, Harada R, Mizuno N, Takahashi H, Akeda Y, Ohnishi M, Ishii Y, Kumasaka T, Murata T, Muramoto K, Tosha T, Shiro Y, Honma T, Shigeta Y, Kubo M, Takashima S, & Shintani Y (2022). Identifying antibiotics based on structural differences in the conserved allostery from mitochondrial heme-copper oxidases. Nat Commun 13 1:7591. PubMed Id: 36481732. doi:10.1038/s41467-022-34771-y.
*Cytochrome C Oxidase with bound Ca²⁺, fully oxidized state: Bos taurus* E Eukaryota, 1.70 Å** fully reduced state, 1.70 Å:8H8S	8H8R	Data File Jmol Viewer 8H8R 8H8S	Muramoto & Shinzawa-Itoh (2023). Muramoto K, & Shinzawa-Itoh K (2023). Calcium-bound structure of bovine cytochrome c oxidase. Biochim Biophys Acta Bioenerg 1864 2:148956. PubMed Id: 36708913. doi:10.1016/j.bbabio.2023.148956.
*Cytochrome C Oxidase, by serial femtosecond crystallography (SFX): Bos taurus* E Eukaryota, 2.38 Å**	8GCQ	Data File Jmol Viewer 8GCQ	Ishigami et al. (2023). Ishigami I, Sierra RG, Su Z, Peck A, Wang C, Poitevin F, Lisova S, Hayes B, Moss FR 3rd, Boutet S, Sublett RE, Yoon CH, Yeh SR, & Rousseau DL (2023). Structural insights into functional properties of the oxidized form of cytochrome c oxidase. Nat Commun 14 1:5752. PubMed Id: 37717031. doi:10.1038/s41467-023-41533-x.
*Cytochrome C Oxidase, aa₃: Paracoccus denitrificans* B Bacteria, 2.70 Å**	1AR1	Data File Jmol Viewer 1AR1	Iwata et al. (1995). Iwata S, Ostermeier C, Ludwig B, & Michel H (1995). Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376 :660-669. PubMed Id: 7651515. See also: Ostermeier et al. (1997). Ostermeier C, Harrenga A, Ermler U, & Michel H (1997). Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment. Proc Natl Acad Sci USA 94 :10547-10553. PubMed Id: 9380672.
*Cytochrome C Oxidase, aa₃, Fully Oxidized: Paracoccus denitrificans* B Bacteria, 3.00 Å**	1QLE	Data File Jmol Viewer 1QLE cyto. C oxidase. Subunit I cyto. C oxidase. Subunit II cyto. C oxidase. Subunit III cyto. C oxidase. Subunit IV	Harrenga & Michel H (1999). Harrenga A & Michel H (1999). The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction. J Biol Chem 274 :33296-33299. PubMed Id: 10559205.
*Cytochrome C Oxidase, aa₃, N131D variant: Paracoccus denitrificans* B Bacteria, 2.32 Å**	3EHB	Data File Jmol Viewer 3EHB	Dürr et al. (2008). Dürr KL, Koepke J, Hellwig P, Müller H, Angerer H, Peng G, Olkhova E, Richter OM, Ludwig B, Michel H (2008). A D-pathway mutation decouples the Paracoccus denitrificans cytochrome c oxidase by altering the side-chain orientation of a distant conserved glutamate. J Mol Biol 384 :865-877. PubMed Id: 18930738.
*Cytochrome C Oxidase, aa₃: Paracoccus denitrificans* B Bacteria, 2.25 Å**	3HB3	Data File Jmol Viewer 3HB3	Koepke et al. (2009). Koepke J, Olkhova E, Angerer H, Müller H, Peng G, Michel H (2009). High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase: new insights into the active site and the proton transfer pathways. Biochim Biophys Acta 1787 :635-645. PubMed Id: 19374884.
*Cytochrome Oxidase, cbb₃: Pseudomonas stutzeri* B Bacteria, 3.2 Å**	3MK7	Data File Jmol Viewer 3MK7	Buschmann et al. (2010). Buschmann S, Warkentin E, Xie H, Langer JD, Ermler U, Michel H. (2010). The structure of cbb₃cytochrome oxidase provides insights into proton pumping. Science 329 :327-330. PubMed Id: 20576851.
*Cytochrome ba₃: Thermus thermophilus* B Bacteria, 2.40 Å**	1EHK	Data File Jmol Viewer 1EHK cyto.c oxidase. Chain I cyto.c oxidase. Chain II cyto.c oxidase. Chain IIa	Soulimane et al. (2000). Soulimane T, Buse G, Bourenkov GP, Bartunik HD, Huber R, & Than ME (2000). Structure and mechanism of the aberrant ba₃-cytochrome c oxidase from Thermus thermophilus. EMBO J 19 :1766-1776. PubMed Id: 10775261. See also: Soulimane et al. (2000). Soulimane T, Than ME, Dewor M, Huber R, & Buse G (2000). Primary structure of a novel subunit in ba₃-cytochrome oxidase from Thermus thermophilus. Protein Sci 9 :2068-2073. PubMed Id: 11152118. doi:10.1110/ps.9.11.2068.
*Cytochrome ba₃ with bound xenon: Thermus thermophilus* B Bacteria, 3.37 Å**	3BVD	Data File Jmol Viewer 3BVD	Luna et al. (2008). Luna VM, Chen Y, Fee JA, & Stout CD (2008). Crystallographic studies of Xe and Kr binding within the large internal Cavity of Cytochrome ba₃from Thermus thermophilus: Structural Analysis and Role of Oxygen Transport Channels in the Heme-Cu Oxidases. Biochemistry 47 :4657-4665. PubMed Id: 18376849.
*Cytochrome C Oxidase, caa₃: Thermus thermophilus* B Bacteria, 2.36 Å** Crystallized in meso	2YEV	Data File Jmol Viewer 2YEV	Lyons et al. (2012). Lyons JA, Aragão D, Slattery O, Pisliakov AV, Soulimane T, & Caffrey M (2012). Structural insights into electron transfer in caa₃-type cytochrome oxidase. Nature 487 :514-518. PubMed Id: 22763450. doi:10.1038/nature11182.
*Cytochrome C Oxidase wild-type: Rhodobacter sphaeroides* B Bacteria, 2.30 Å** EQ(I-286) mutant, 3.00 Å: 1M57	1M56	Data File Jmol Viewer 1M56 1M57	Svensson-Ek et al. (2002). Svensson-Ek M, Abramson J, Larsson G, Törnroth S, Brzezinski P, & Iwata S (2002). The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J Mol Biol 321 :329-339. PubMed Id: 12144789.
*Cytochrome C Oxidase, two-subunit catalytic core: Rhodobacter sphaeroides* B Bacteria, 2.0 Å**	2GSM	Data File Jmol Viewer 2GSM	Qin et al. (2006). Qin G, Hiser C, Mulichak A, Garavito RM, & Ferguson-Miller S (2006). Identification of conserved lipid/detergent-binding sites in a high-resolution structure of the membrane protein cytochrome c oxidase. Proc. Natl. Acad. Sci. USA 103 :16117-16122. PubMed Id: 17050688.
*Ubiquinol Oxidase, cytochrome bo₃: Escherichia coli* B Bacteria, 3.5 Å**	1FFT	Data File Jmol Viewer 1FFT ubiquinol oxidase subunit I ubiquinol oxidase subunit II ubiquinol oxidase subunit III	Abramson et al. (2000). Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, & Wikstrom M (2000). The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat Struct Biol 7 :910-917. PubMed Id: 11017202.
*Ubiquinol Oxidase, cytochrome bo₃: Escherichia coli* B Bacteria, 2.20 Å** cryo-EM structure	6WTI	Data File Jmol Viewer 6WTI	Su et al. (2021). Su CC, Lyu M, Morgan CE, Bolla JR, Robinson CV, & Yu EW (2021). A 'Build and Retrieve' methodology to simultaneously solve cryo-EM structures of membrane proteins. Nat Methods 18 1:69-75. PubMed Id: 33408407. doi:10.1038/s41592-020-01021-2.
*Ubiquinol Oxidase, cytochrome bo₃ in native membrane: Escherichia coli* B Bacteria, 2.55 Å** cryo-EM structure Ubiquinol Binding Site, 2.63 Å 7CUW in native membrane, 2.55 Å 7CUQ in MSP nanodisc, 2.19 Å 7N9Z	7CUB	Data File Jmol Viewer 7CUB 7N9Z 7CUW 7CUQ	Li et al. (2021). Li J, Han L, Vallese F, Ding Z, Choi SK, Hong S, Luo Y, Liu B, Chan CK, Tajkhorshid E, Zhu J, Clarke O, Zhang K, & Gennis R (2021). Cryo-EM structures of Escherichia coli cytochrome bo₃ reveal bound phospholipids and ubiquinone-8 in a dynamic substrate binding site. Proc Natl Acad Sci U S A 118 34:e2106750118. PubMed Id: 34417297. doi:10.1073/pnas.2106750118.
*Ubiquinol Oxidase, cytochrome bo₃, apo form: Escherichia coli* B Bacteria, 3.09 Å** cryo-EM structure with bound an allosteric inhibitor N4, 2.99 Å: 7XMD	7XMC	Data File Jmol Viewer 7XMC 7XMD	Nishida et al. (2022). Nishida Y, Yanagisawa S, Morita R, Shigematsu H, Shinzawa-Itoh K, Yuki H, Ogasawara S, Shimuta K, Iwamoto T, Nakabayashi C, Matsumura W, Kato H, Gopalasingam C, Nagao T, Qaqorh T, Takahashi Y, Yamazaki S, Kamiya K, Harada R, Mizuno N, Takahashi H, Akeda Y, Ohnishi M, Ishii Y, Kumasaka T, Murata T, Muramoto K, Tosha T, Shiro Y, Honma T, Shigeta Y, Kubo M, Takashima S, & Shintani Y (2022). Identifying antibiotics based on structural differences in the conserved allostery from mitochondrial heme-copper oxidases. Nat Commun 13 1:7591. PubMed Id: 36481732. doi:10.1038/s41467-022-34771-y.
*Cytochrome bd-type oxidase (anisotropy corrected): Geobacillus thermodenitrificans* B Bacteria, 3.05 Å** anisotropic structure, 3.8 Å: 5IR6	5DOQ	Data File Jmol Viewer 5DOQ 5IR6	Safarian et al. (2016). Safarian S, Rajendran C, Müller H, Preu J, Langer JD, Ovchinnikov S, Hirose T, Kusumoto T, Sakamoto J, & Michel H (2016). Structure of a bd oxidase indicates similar mechanisms for membrane-integrated oxygen reductases. Science 352 :583-586. PubMed Id: 27126043. doi:10.1126/science.aaf2477.
*Cytochrome bd-type oxidase in nanodiscs: Escherichia coli* B Bacteria, 2.7 Å** cryo-EM structure	6RKO	Data File Jmol Viewer 6RKO	Safarian et al. (2019). Safarian S, Hahn A, Mills DJ, Radloff M, Eisinger ML, Nikolaev A, Meier-Credo J, Melin F, Miyoshi H, Gennis RB, Sakamoto J, Langer JD, Hellwig P, Kühlbrandt W, & Michel H (2019). Active site rearrangement and structural divergence in prokaryotic respiratory oxidases. Science 366 6461:100-104. PubMed Id: 31604309. doi:10.1126/science.aay0967.
*Cytochrome bd-type oxidase in nanodiscs treated w. specific inhibitor aurachin: Escherichia coli* B Bacteria, 3.3 Å** cryo-EM structure	6RX4	Data File Jmol Viewer 6RX4	Theßeling et al. (2019). Theßeling A, Rasmussen T, Burschel S, Wohlwend D, Kägi J, Müller R, Böttcher B, & Friedrich T (2019). Homologous bd oxidases share the same architecture but differ in mechanism. Nat Commun 10 1:5138. PubMed Id: 31723136. doi:10.1038/s41467-019-13122-4.
*Cytochrome bd-II type oxidase with bound aurachin D: Escherichia coli* B Bacteria, 3.00 Å** cryo-EM structure	7OSE	Data File Jmol Viewer 7OSE	Grauel et al. (2021). Grauel A, Kägi J, Rasmussen T, Makarchuk I, Oppermann S, Moumbock AFA, Wohlwend D, Müller R, Melin F, Günther S, Hellwig P, Böttcher B, & Friedrich T (2021). Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin D. Nat Commun 12 1:6498. PubMed Id: 34764272. doi:10.1038/s41467-021-26835-2.
*Cytochrome bd-II type oxidase: Escherichia coli* B Bacteria, 2.06 Å** cryo-EM structure	7OY2	Data File Jmol Viewer 7OY2	Grund et al. (2021). Grund TN, Radloff M, Wu D, Goojani HG, Witte LF, Jösting W, Buschmann S, Müller H, Elamri I, Welsch S, Schwalbe H, Michel H, Bald D, & Safarian S (2021). Mechanistic and structural diversity between cytochrome bd isoforms of Escherichia coli. Proc Natl Acad Sci U S A 118 50:e2114013118. PubMed Id: 34873041. doi:10.1073/pnas.2114013118.
*Cytochrome bd-type oxidase: Mycolicibacterium smegmatis* B Bacteria (expressed in E. coli), 2.79 Å** cryo-EM structure	7D5I	Data File Jmol Viewer 7D5I	Wang et al. (2021). Wang W, Gao Y, Tang Y, Zhou X, Lai Y, Zhou S, Zhang Y, Yang X, Liu F, Guddat LW, Wang Q, Rao Z, & Gong H (2021). Cryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels. Nat Commun 12 1:4621. PubMed Id: 34330928. doi:10.1038/s41467-021-24924-w.
*Cytochrome bd-type oxidase: Mycobacterium tuberculosis* B Bacteria (expressed in Mycolicibacterium smegmatis), 2.50 Å** cryo-EM structure	7NK2	Data File Jmol Viewer 7NK2	Safarian et al. (2021). Safarian S, Opel-Reading HK, Wu D, Mehdipour AR, Hards K, Harold LK, Radloff M, Stewart I, Welsch S, Hummer G, Cook GM, Krause KL, & Michel H (2021). The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB. Nat Commun 12 1:5236. PubMed Id: 34475399. doi:10.1038/s41467-021-25537-z.
*Heme A synthase (HAS): Bacillus subtilis* B Bacteria (expressed in E. coli), 2.2 Å** from S-anomalous dataset, 3.0 Å: 6IED	6A2J	Data File Jmol Viewer 6A2J 6IED	Niwa et al. (2018). Niwa S, Takeda K, Kosugi M, Tsutsumi E, Mogi T, & Miki K (2018). Crystal structure of heme A synthase from Bacillus subtilis. Proc Natl Acad Sci USA 115 47:11953-11957. PubMed Id: 30397130. doi:10.1073/pnas.1813346115.
*cytochrome aa₃-600 menaquinol oxidase: Bacillus subtilis* B Bacteria, 3.6 Å** in complex with 3-iodo-N-oxo-2-heptyl-4-hydroxyquinoline, 3.8 Å: 6KOC in complex with N-oxo-2-heptyl-4-hydroxyquinoline, 3.75 Å: 6KOE	6KOB	Data File Jmol Viewer 6KOB 6KOE 6KOC	Xu et al. (2020). Xu J, Ding Z, Liu B, Yi SM, Li J, Zhang Z, Liu Y, Li J, Liu L, Zhou A, Gennis RB, & Zhu J (2020). Structure of the cytochrome aa₃-600 heme-copper menaquinol oxidase bound to inhibitor HQNO shows TM0 is part of the quinol binding site. Proc Natl Acad Sci USA 117 2:872-876. PubMed Id: 31888984. doi:10.1073/pnas.1915013117.
*Cytochrome C Oxidase: Saccharomyces cerevisiae* E Eukaryota, 3.87 Å** cryo-EM structure	7Z10	Data File Jmol Viewer 7Z10	Ing et al. (2022). Ing G, Hartley AM, Pinotsis N, & Maréchal A (2022). Cryo-EM structure of a monomeric yeast S. cerevisiae complex IV isolated with maltosides: Implications in supercomplex formation. Biochim Biophys Acta Bioenerg 1863 7:148591. PubMed Id: 35839926. doi:10.1016/j.bbabio.2022.148591.
*Cox13 subunit of cytochrome C oxidase: Saccharomyces cerevisiae* E Eukaryota (expressed in E. coli), NMR structure**	6ZDB	Data File Jmol Viewer 6ZDB	Zhou et al. (2021). Zhou S, Pettersson P, Björck ML, Dawitz H, Brzezinski P, Mäler L, & Ädelroth P (2021). NMR structural analysis of the yeast cytochrome c oxidase subunit Cox13 and its interaction with ATP. BMC Biol 19 1:98. PubMed Id: 33971868. doi:10.1186/s12915-021-01036-x.
Electron Transport Chain Supercomplexes (Respirasome)
*Electron Transport Chain (ETC) Super Complex comprised of ETC complexes I, III, and IV, tight respirasome: Ovis aries* E Eukaryota, 5.8 Å** cryo-EM structure loose respirasome, 6.7 Å: 5J7Y supercomplex I-III₂, 7.8 Å: 5J8K	5J4Z	Data File Jmol Viewer 5J4Z 5J8K 5J7Y	Letts et al. (2016). Letts JA, Fiedorczuk K, & Sazanov LA (2016). The architecture of respiratory supercomplexes. Nature 537 :644-648. PubMed Id: 27654913. doi:10.1038/nature19774.
*Electron Transport Chain (ETC) Super Complex I+III₂, closed class: Ovis aries* E Eukaryota, 4.2 Å** cryo-EM structure. Protein stabilized with amphipols. open class 1, 4.2 Å: 6QC3 open class 2, 4.2 Å: 6QC2 open class 3, 4.6 Å: 6QC4 CI Peripheral Arm focused refinement, 3.8 Å: 6Q9D CI Membrane Arm focused refinement, 3.9 Å: 6Q9B Complex III₂ focused refinement, 3.9 Å: 6Q9E Isolated complex I class refinement, 4.1 Å: 6QA9 complex I FRC closed class 1, 4.3 Å: 6QC5 complex I FRC open class 1, 4.1 Å: 6QC6 complex I FRC open class 2, 4.2 Å: 6QC8 complex I FRC open class, 4.4 Å: 6QC7 complex I FRC open class 4, 5.7 Å: 6QC9 complex I FRC open class 5, 6.2 Å: 6QCA complex I FRC open class 6, 6.5 Å: 6QCF	6QBX	Data File Jmol Viewer 6QBX 6Q9B 6Q9D 6Q9E 6QC2 6QC6 6QC7 6QC3 6QC9 6QA9 6QCA 6QC4 6QC8 6QC5 6QCF	Letts et al. (2019). Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, & Sazanov LA (2019). Structures of Respiratory Supercomplex I+III2 Reveal Functional and Conformational Crosstalk. Mol. Cell 75 6:1131-1146.e6. PubMed Id: 31492636. doi:10.1016/j.molcel.2019.07.022.
*Electron Transport Chain (ETC) Super Complex comprised of ETC complexes I, III, and IV: Sus scrofa* E Eukaryota, 5.4 Å** cryo-EM structure	5GPN	Data File Jmol Viewer 5GPN	Gu et al. (2016). Gu J, Wu M, Guo R, Yan K, Lei J, Gao N, & Yang M (2016). The architecture of the mammalian respirasome. Nature 537 :639-643. PubMed Id: 27654917. doi:10.1038/nature19359.
*Electron Transport Chain (ETC) Super Complex I₁III₂IV₁: Sus scrofa* E Eukaryota, 4.0 Å** Cryo-EM structure	5GUP	Data File Jmol Viewer 5GUP	Wu et al. (2016). Wu M, Gu J, Guo R, Huang Y, & Yang M (2016). Structure of Mammalian Respiratory Supercomplex I₁III₂IV₁. Cell 167 :1598-1609.e10. PubMed Id: 27912063. doi:10.1016/j.cell.2016.11.012.
*Respiratory supercomplex CIII₂CIV₂SOD₂: Mycobacterium smegmatis* B Bacteria, 3.5 Å** cryo-EM structure	6ADQ	Data File Jmol Viewer 6ADQ	Gong et al. (2018). Gong H, Li J, Xu A, Tang Y, Ji W, Gao R, Wang S, Yu L, Tian C, Li J, Yen HY, Man Lam S, Shui G, Yang X, Sun Y, Li X, Jia M, Yang C, Jiang B, Lou Z, Robinson CV, Wong LL, Guddat LW, Sun F, Wang Q, & Rao Z (2018). An electron transfer path connects subunits of a mycobacterial respiratory supercomplex. Science 362 6418:eaat8923. PubMed Id: 30361386. doi:10.1126/science.aat8923.
*Respiratory supercomplex CIII₂CIV₂: Mycobacterium smegmatis* B Bacteria, 3.3 Å** cryo-EM structure	6HWH	Data File Jmol Viewer 6HWH	Wiseman et al. (2018). Wiseman B, Nitharwal RG, Fedotovskaya O, Schäfer J, Guo H, Kuang Q, Benlekbir S, Sjöstrand D, Ädelroth P, Rubinstein JL, Brzezinski P, & Högbom M (2018). Structure of a functional obligate complex III2IV2 respiratory supercomplex from Mycobacterium smegmatis. Nat Struct Mol Biol 25 12:1128-1136. PubMed Id: 30518849. doi:10.1038/s41594-018-0160-3.
*Respiratory supercomplex CIII₂CIV₂ with bound Telacebec (Q203): Mycolicibacterium smegmatis* B Bacteria, 3.00 Å** cryo-EM structure Inhibitor free, 3.00 Å 7RH5 nhibitor free, -Lpqe cyt cc open, 3.50 Å 7RH6	7RH7	Data File Jmol Viewer 7RH7 7RH6 7RH5	Yanofsky et al. (2021). Yanofsky DJ, Di Trani JM, Król S, Abdelaziz R, Bueler SA, Imming P, Brzezinski P, & Rubinstein JL (2021). Structure of mycobacterial CIII2CIV2 respiratory supercomplex bound to the tuberculosis drug candidate telacebec (Q203). Elife 10 :e71959. PubMed Id: 34590581. doi:10.7554/eLife.71959.
*Electron Transport Chain (ETC) Super Complex III₂IV: Saccharomyces cerevisiae* E Eukaryota, 3.23 Å** cryo-EM structure	6GIQ	Data File Jmol Viewer 6GIQ	Rathore et al. (2019). Rathore S, Berndtsson J, Marin-Buera L, Conrad J, Carroni M, Brzezinski P, & Ott M (2019). Cryo-EM structure of the yeast respiratory supercomplex. Nat Struct Mol Biol 26 1:50-57. PubMed Id: 30598556. doi:10.1038/s41594-018-0169-7.
*Rcf1 protein involved in electron chain super-complex formation: Saccharomyces cerevisiae* E Eukaryota (expressed in E. coli), NMR structure**	5NF8	Data File Jmol Viewer 5NF8	Zhou et al. (2018). Zhou S, Pettersson P, Huang J, Sjöholm J, Sjöstrand D, Pomès R, Högbom M, Brzezinski P, Mäler L, & Ädelroth P (2018). Solution NMR structure of yeast Rcf1, a protein involved in respiratory supercomplex formation. Proc Natl Acad Sci USA 115 12:3048-3053. PubMed Id: 29507228. doi:10.1073/pnas.1712061115.
*Electron Transport Chain (ETC) Super Complex III₂IV₂: Saccharomyces cerevisiae* E Eukaryota, 3.35 Å** cryo-EM structure	6HU9	Data File Jmol Viewer 6HU9	Hartley et al. (2019). Hartley AM, Lukoyanova N, Zhang Y, Cabrera-Orefice A, Arnold S, Meunier B, Pinotsis N, & Maréchal A (2019). Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome bc1. Nat Struct Mol Biol 26 1:78-83. PubMed Id: 30598554. doi:10.1038/s41594-018-0172-z.
*III₂-IV(5B)1 respiratory supercomplex: Saccharomyces cerevisiae* E Eukaryota, 3.29 Å** cryo-EM structure III₂-IV(5B)2 respiratory supercomplex, 2.80 Å: 6T0B	6T15	Data File Jmol Viewer 6T15 6T0B	Hartley et al. (2020). Hartley AM, Meunier B, Pinotsis N, & Maréchal A (2020). Rcf2 revealed in cryo-EM structures of hypoxic isoforms of mature mitochondrial III-IV supercomplexes. Proc Natl Acad Sci USA 117 17:9329-9337. PubMed Id: 32291341. doi:10.1073/pnas.1920612117.
*Respiratory supercomplex Factor 2: Saccharomyces cerevisiae* E Eukaryota (expressed in E. coli), NMR structure**	6LUL	Data File Jmol Viewer 6LUL	Zhou et al. (2021). Zhou S, Pettersson P, Huang J, Brzezinski P, Pomès R, Mäler L, & Ädelroth P (2021). NMR Structure and Dynamics Studies of Yeast Respiratory Supercomplex Factor 2. Structure 29 3:275-283.e4. PubMed Id: 32905793. doi:10.1016/j.str.2020.08.008.
*CIII₂/CIV respiratory supercomplex: Saccharomyces cerevisiae* E Eukaryota, 3.17 Å** cryo-EM structure Cytochrome c oxidase, 3.41 Å 6YMY	6YMX	Data File Jmol Viewer 6YMX 6YMY	Berndtsson et al. (2020). Berndtsson J, Aufschnaiter A, Rathore S, Marin-Buera L, Dawitz H, Diessl J, Kohler V, Barrientos A, Büttner S, Fontanesi F, & Ott M (2020). Respiratory supercomplexes enhance electron transport by decreasing cytochrome c diffusion distance. EMBO Rep 21 12:e51015. PubMed Id: 33016568. doi:10.15252/embr.202051015.
*Electron Transport Chain (ETC) Super Complex III₂IV₂ with bound 4 UQ6 (ubiquinone): S. cerevisiae* E Eukaryota, 3.20 Å** cryo-EM structure Complex III₂IV, cardiolipin-lacking mutant, 3.30 Å: 8EC0	8E7S	Data File Jmol Viewer 8E7S 8EC0	Hryc et al. (2023). Hryc CF, Mallampalli VKPS, Bovshik EI, Azinas S, Fan G, Serysheva II, Sparagna GC, Baker ML, Mileykovskaya E, & Dowhan W (2023). Structural insights into cardiolipin replacement by phosphatidylglycerol in a cardiolipin-lacking yeast respiratory supercomplex. Nat Commun 14 1:2783. PubMed Id: 37188665. doi:10.1038/s41467-023-38441-5.
*Respiratory supercomplex III₂-IV: Vigna radiata* E Eukaryota, 3.80 Å** cryo-EM structure complex III₂, 3.20 Å: 7JRG complex IV, 3.80 Å: 7JRO	7JRP	Data File Jmol Viewer 7JRP 7JRG 7JRO	Maldonado et al. (2021). Maldonado M, Guo F, & Letts JA (2021). Atomic structures of respiratory complex III₂, complex IV, and supercomplex III₂-IV from vascular plants. Elife 10 :e62047. PubMed Id: 33463523. doi:10.7554/eLife.62047.
*Respiratory supercomplex III₂-IV. CIII₂: Rhodobacter capsulatus* B Bacteria, 3.30 Å** cryo-EM structure with both FeS proteins in c position (CIII₂ c-c), 3.75 Å: 6XKT with one FeS protein in b position and one in c position (CIII₂ b-c), 4.20 Å: 6XKU with both FeS proteins in b position (CIII₂ b-b), 3.50 Å: 6XKV CIII₂CIV bipartite super-complex with CcoH/cy, 5.20 Å: 6XKW CIII₂CIV tripartite super-complex, conformation A, 6.10 Å: 6XKX CIII₂CIV tripartite super-complex, conformation B, 7.20 Å: 6XKZ	6XI0	Data File Jmol Viewer 6XI0 6XKU 6XKT 6XKW 6XKZ 6XKV 6XKX	Steimle et al. (2021). Steimle S, van Eeuwen T, Ozturk Y, Kim HJ, Braitbard M, Selamoglu N, Garcia BA, Schneidman-Duhovny D, Murakami K, & Daldal F (2021). Cryo-EM structures of engineered active bc₁-cbb₃ type CIII₂CIV super-complexes and electronic communication between the complexes. Nat Commun 12 1:929. PubMed Id: 33568648. doi:10.1038/s41467-021-21051-4.
Electron Transport Chain (ETC) hybrid Super Complex comprised of M. tuberculosis complexIII and M. smegmatis complexIV: Mycobacterium tuberculosis B Bacteria (expressed in Mycobacterium smegmatis), 2.68 Å cryo-EM structure hybrid complex in the presence Q203, 2.67 Å 7E1W hybrid complex in the presence of TB47, 2.93 Å 7E1X	7E1V	Data File Jmol Viewer 7E1V 7E1X 7E1W	Zhou et al. (2021). Zhou S, Wang W, Zhou X, Zhang Y, Lai Y, Tang Y, Xu J, Li D, Lin J, Yang X, Ran T, Chen H, Guddat LW, Wang Q, Gao Y, Rao Z, & Gong H (2021). Structure of Mycobacterium tuberculosis cytochrome bcc in complex with Q203 and TB47, two anti-TB drug candidates. Elife 10 :e69418. PubMed Id: 34819223. doi:10.7554/eLife.69418.
*ETC Super Complex comprised of ETC complexes CIII₂CIV, intermediate locked conformation: Mus musculus* E Eukaryota, 3.60 Å** cryo-EM structure assembled locked conformation, 3.20 Å 7O37 mature unlocked conformation, 3.30 Å 7O3C focus-refined from supercomplex CICIII₂, 2.60 Å 7O3H	7O3E	Data File Jmol Viewer 7O3E 7O3H 7O3C 7O37	Vercellino & Sazanov (2021). Vercellino I, & Sazanov LA (2021). Structure and assembly of the mammalian mitochondrial supercomplex CIII₂C_IV. Nature 598 7880:364-367. PubMed Id: 34616041. doi:10.1038/s41586-021-03927-z.
*III₂-IV₂ respiratory supercomplex: Corynebacterium glutamicum* E Eukaryota, 2.90 Å** cryo-EM structure	7Q21	Data File Jmol Viewer 7Q21	Moe et al. (2022). Moe A, Kovalova T, Król S, Yanofsky DJ, Bott M, Sjöstrand D, Rubinstein JL, Högbom M, & Brzezinski P (2022). The respiratory supercomplex from C. glutamicum. Structure 30 3:338-349.e3. PubMed Id: 34910901. doi:10.1016/j.str.2021.11.008.
*III₂-IV₂ respiratory supercomplex, native: Corynebacterium glutamicum* E Eukaryota, 3.10 Å** cryo-EM structure stigmatellin and azide bound, 2.80 Å 7QHM	7QHO	Data File Jmol Viewer 7QHO 7QHM	Kao et al. (2022). Kao WC, Ortmann de Percin Northumberland C, Cheng TC, Ortiz J, Durand A, von Loeffelholz O, Schilling O, Biniossek ML, Klaholz BP, & Hunte C (2022). Structural basis for safe and efficient energy conversion in a respiratory supercomplex. Nat Commun 13 1:545. PubMed Id: 35087070. doi:10.1038/s41467-022-28179-x.
*respiratory chain super-complex CI+III₂: Tetrahymena thermophila* E Eukaryota, 2.60 Å** cryo-EM structure complex IV, composite dimer model, 3.02 Å 7W5Z	7TGH	Data File Jmol Viewer 7TGH 7W5Z	Zhou et al. (2022). Zhou L, Maldonado M, Padavannil A, Guo F, & Letts JA (2022). Structures of Tetrahymena's respiratory chain reveal the diversity of eukaryotic core metabolism. Science 376 6595:831-839. PubMed Id: 35357889. doi:10.1126/science.abn7747.
*Respiratory chain super-complex, IV₂+(I+III₂+II)₂: Tetrahymena thermophila* E Eukaryota, 2.96 Å** cryo-EM structure Megacomplex (IV₂+I+III₂+II)₂	8GYM	Data File Jmol Viewer 8GYM	Han et al. (2023). Han F, Hu Y, Wu M, He Z, Tian H, & Zhou L (2023). Structures of Tetrahymena thermophila respiratory megacomplexes on the tubular mitochondrial cristae. Nat Commun 14 1:2542. PubMed Id: 37248254. doi:10.1038/s41467-023-38158-5.
*Electron Transport Chain (ETC) Super Complex, optimized supercomplex state1: Bos taurus* E Eukaryota, 5.00 Å** cryo-EM structure optimized supercomplex state2, 4.60 Å: 7DGR optimized supercomplex state3, 7.80 Å: 7DGS optimized supercomplex state4, 8.30 Å: 7DKF Activity optimized complex I (closed form), 3.80 Å: 7DGZ Activity optimized complex I (open form), 4.20 Å: 7DH0	7DGQ	Data File Jmol Viewer 7DGQ 7DGR 7DGS 7DH0 7DKF 7DGZ	Jeon et al. (2022). Jeon TJ, Lee SG, Yoo SH, Kim M, Song D, Ryu J, Park H, Kim DS, Hyun J, Kim HM, & Ryu SE (2022). A Dynamic Substrate Pool Revealed by cryo-EM of a Lipid-Preserved Respiratory Supercomplex. Antioxid Redox Signal 36 16:1101-1118. PubMed Id: 34913730. doi:10.1089/ars.2021.0114.
Nitric Oxide Reductases
*Nitric Oxide Reductase: Pseudomonas aeruginosa* B Bacteria, 2.70 Å** Crystallized with cNOR antibody (Fab)	3O0R	Data File Jmol Viewer 3O0R	Hino et al. (2010). Hino T, Matsumoto Y, Nagano S, Sugimoto H, Fukumori Y, Murata T, Iwata S, & Shiro Y (2010). Structural basis of biological N₂O generation by bacterial nitric oxide reductase. Science 330 :1666-1670. PubMed Id: 21109633.
*Nitric Oxide Reductase qNOR wild-type: Geobacillus stearothermophilus* B Bacteria (expressed in E. coli), 2.5 Å** HQNO complex, 2.7 Å: 3AYG	3AYF	Data File Jmol Viewer 3AYF 3AYG	Matsumoto et al. (2012). Matsumoto Y, Tosha T, Pisliakov AV, Hino T, Sugimoto H, Nagano S, Sugita Y, & Shiro Y (2012). Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus. Nat Struct Mol Biol 19 :238-245. PubMed Id: 22266822. doi:10.1038/nsmb.2213.
*Nitric Oxide Reductase qNOR: Alcaligenes xylosoxydans* B Bacteria (expressed in E. coli), 3.9 Å** cryo-EM structure V495A mutant, 3.3 Å: 6QQ6	6QQ5	Data File Jmol Viewer 6QQ5 6QQ6	Gopalasingam et al. (2019). Gopalasingam CC, Johnson RM, Chiduza GN, Tosha T, Yamamoto M, Shiro Y, Antonyuk SV, Muench SP, & Hasnain SS (2019). Dimeric structures of quinol-dependent nitric oxide reductases (qNORs) revealed by cryo-electron microscopy. Sci Adv 5 8:eaax1803. PubMed Id: 31489376. doi:10.1126/sciadv.aax1803.
*Nitric Oxide Reductase qNOR: Achromobacter xylosoxidans* B Bacteria (expressed in E. coli), 2.20 Å** cryo-EM structure	8BGW	Data File Jmol Viewer 8BGW	Flynn et al. (2023). Flynn AJ, Antonyuk SV, Eady RR, Muench SP, & Hasnain SS (2023). A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases. Nat Commun 14 1:3416. PubMed Id: 37296134. doi:10.1038/s41467-023-39140-x.
*Nitric Oxide Reductase BC complex: Roseobacter denitrificans* B Bacteria, 2.85 Å**	4XYD	Data File Jmol Viewer 4XYD	Crow et al. (2016). Crow A, Matsuda Y, Arata H, & Oubrie A (2016). Structure of the Membrane-intrinsic Nitric Oxide Reductase from Roseobacter denitrificans. Biochemistry 55 23:3198-3203. PubMed Id: 27185533. doi:10.1021/acs.biochem.6b00332.
*Nitric Oxide Reductase qNOR: Neisseria meninigitidis* B Bacteria (expressed in E. coli), 3.06 Å** cryo-EM structure x-ray structure: monomeric oxidized state with zinc complex, 3.15 Å: 6L1X	6L3H	Data File Jmol Viewer 6L3H 6L1X	Jamali et al. (2020). Jamali MAM, Gopalasingam CC, Johnson RM, Tosha T, Muramoto K, Muench SP, Antonyuk SV, Shiro Y, & Hasnain SS (2020). The active form of quinol-dependent nitric oxide reductase from Neisseria meningitidis is a dimer. IUCrJ 7 :404-415. PubMed Id: 32431824. doi:10.1107/S2052252520003656.
*Nitric Oxide Reductase qNOR, Glu-494-Ala inactive monomer: Achromobacter xylosoxidans* B Bacteria (expressed in E. coli), 4.50 Å** cryo-EM structure	6T6V	Data File Jmol Viewer 6T6V	Jamali et al. (2020). Jamali MAM, Gopalasingam CC, Johnson RM, Tosha T, Muramoto K, Muench SP, Antonyuk SV, Shiro Y, & Hasnain SS (2020). The active form of quinol-dependent nitric oxide reductase from Neisseria meningitidis is a dimer. IUCrJ 7 :404-415. PubMed Id: 32431824. doi:10.1107/S2052252520003656.
Photosystems
*Photosystem I: Thermosynechococcus elongatus* B Bacteria, 4.0 Å**	2PPS	Data File Jmol Viewer 2PPS	Schubert et al. (1997). Schubert W-D, Klukas O, Krauß N, Saenger W, Fromme P, & Witt HT (1997). Photosystem I of Synechococcus elongatus at 4 Å resolution: Comprehensive structure analysis. J Mol Biol 272 :741-769. PubMed Id: 9368655.
*Photosystem I: Thermosynechococcus elongatus* B Bacteria, 2.5 Å**	1JB0	Data File Jmol Viewer 1JB0 photosystem I A subunit photosystem I B subunit photosystem I F subunit photosystem I I subunit photosystem I J subunit photosystem I K subunit photosystem I L subunit photosystem I M subunit photosystem I X subunit	Jordan et al. (2001). Jordan P, Fromme P, Witt HT, Klukas O, Saenger W, & Krauss N (2001). Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411 :909-917. PubMed Id: 11418848.
*Photosynthetic complex I: Thermosynechococcus elongatus* B Bacteria, 3.34 Å** cryo-EM structure	6HUM	Data File Jmol Viewer 6HUM	Schuller et al. (2019). Schuller JM, Birrell JA, Tanaka H, Konuma T, Wulfhorst H, Cox N, Schuller SK, Thiemann J, Lubitz W, Sétif P, Ikegami T, Engel BD, Kurisu G, & Nowaczyk MM (2019). Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer. Science 363 6424:257-260. PubMed Id: 30573545. doi:10.1126/science.aau3613.
*Photosystem I, megahertz XFEL structure: Thermosynechococcus elongatus* B Bacteria, 2.9 Å** synchrotron structure, 2.9 Å: 6PFY	6PGK	Data File Jmol Viewer 6PGK 6PFY	Gisriel et al. (2019). Gisriel C, Coe J, Letrun R, Yefanov OM, Luna-Chavez C, Stander NE, Lisova S, Mariani V, Kuhn M, Aplin S, Grant TD, Dörner K, Sato T, Echelmeier A, Cruz Villarreal J, Hunter MS, Wiedorn MO, Knoska J, Mazalova V, Roy-Chowdhury S, Yang JH, Jones A, Bean R, Bielecki J, Kim Y, Mills G, Weinhausen B, Meza JD, Al-Qudami N, Bajt S, Brehm G, Botha S, Boukhelef D, Brockhauser S, Bruce BD, Coleman MA, Danilevski C, Discianno E, Dobson Z, Fangohr H, Martin-Garcia JM, Gevorkov Y, Hauf S, Hosseinizadeh A, Januschek F, Ketawala GK, Kupitz C, Maia L, Manetti M, Messerschmidt M, Michelat T, Mondal J, Ourmazd A, Previtali G, Sarrou I, Schön S, Schwander P, Shelby ML, Silenzi A, Sztuk-Dambietz J, Szuba J, Turcato M, White TA, Wrona K, Xu C, Abdellatif MH, Zook JD, Spence JCH, Chapman HN, Barty A, Kirian RA, Frank M, Ros A, Schmidt M, Fromme R, Mancuso AP, Fromme P, & Zatsepin NA (2019). Membrane protein megahertz crystallography at the European XFEL. Nat Commun 10 1:5021. PubMed Id: 31685819. doi:10.1038/s41467-019-12955-3.
*Photosynthetic complex I, composite data set: Thermosynechococcus elongatus* B Bacteria, 3.1 Å** cryo-EM structure using data set 1, 3.1 Å: 6NBQ using data set 2, 3.1 Å: 6NBX	6NBY	Data File Jmol Viewer 6NBY 6NBX 6NBQ	Laughlin et al. (2019). Laughlin TG, Bayne AN, Trempe JF, Savage DF, & Davies KM (2019). Structure of the complex I-like molecule NDH of oxygenic photosynthesis. Nature 566 7744:411-414. PubMed Id: 30742075. doi:10.1038/s41586-019-0921-0.
*NDH-1MS complex of photosynthetic complex I: Thermosynechococcus elongatus* B Bacteria, 3.2 Å** cryo-EM structure	6TJV	Data File Jmol Viewer 6TJV	Schuller et al. (2020). Schuller JM, Saura P, Thiemann J, Schuller SK, Gamiz-Hernandez AP, Kurisu G, Nowaczyk MM, & Kaila VRI (2020). Redox-coupled proton pumping drives carbon concentration in the photosynthetic complex I. Nat Commun 11 1:494. PubMed Id: 31980611. doi:10.1038/s41467-020-14347-4.
*Photosystem I, monomer: Thermosynechococcus elongatus* B Bacteria, 3.20 Å** cryo-EM structure at 6.5 Å: 7BW2	6LU1	Data File Jmol Viewer 6LU1 7BW2	Çoruh et al. (2021). Çoruh O, Frank A, Tanaka H, Kawamoto A, El-Mohsnawy E, Kato T, Namba K, Gerle C, Nowaczyk MM, & Kurisu G (2021). Cryo-EM structure of a functional monomeric Photosystem I from Thermosynechococcus elongatus reveals red chlorophyll cluster. Commun Biol 4 1:304. PubMed Id: 33686186. doi:10.1038/s42003-021-01808-9.
*tetrameric photosystem I: Anabaena sp. PCC7120* B Bacteria, 2.37 Å** cryo-EM structure	6K61	Data File Jmol Viewer 6K61	Zheng et al. (2019). Zheng L, Li Y, Li X, Zhong Q, Li N, Zhang K, Zhang Y, Chu H, Ma C, Li G, Zhao J, & Gao N (2019). Structural and functional insights into the tetrameric photosystem I from heterocyst-forming cyanobacteria. Nat Plants 5 10:1087-1097. PubMed Id: 31595062. doi:10.1038/s41477-019-0525-6.
*tetrameric photosystem I: Anabaena sp. PCC7120* B Bacteria, 3.3 Å** cryo-EM structure	6JEO	Data File Jmol Viewer 6JEO	Kato et al. (2019). Kato K, Nagao R, Jiang TY, Ueno Y, Yokono M, Chan SK, Watanabe M, Ikeuchi M, Shen JR, Akimoto S, Miyazaki N, & Akita F (2019). Structure of a cyanobacterial photosystem I tetramer revealed by cryo-electron microscopy. Nat Commun 10 1:4929. PubMed Id: 31666526. doi:10.1038/s41467-019-12942-8.
*tetrameric photosystem I: Anabaena sp. PCC7120* B Bacteria, 3.20 Å** cryo-EM structure	6TCL	Data File Jmol Viewer 6TCL	Chen et al. (2020). Chen M, Perez-Boerema A, Zhang L, Li Y, Yang M, Li S, & Amunts A (2020). Distinct structural modulation of photosystem I and lipid environment stabilizes its tetrameric assembly. Nat Plants 6 3:314-320. PubMed Id: 32170279. doi:10.1038/s41477-020-0610-x.
*Photosystem I grown under white light conditions: Halomicronema hongdechloris* B Bacteria, 2.35 Å** grown under far-red light conditions, 2.41 Å: 6KMX	6KMW	Data File Jmol Viewer 6KMW 6KMX	Kato et al. (2020). Kato K, Shinoda T, Nagao R, Akimoto S, Suzuki T, Dohmae N, Chen M, Allakhverdiev SI, Shen JR, Akita F, Miyazaki N, & Tomo T (2020). Structural basis for the adaptation and function of chlorophyll f in photosystem I. Nat Commun 11 1. PubMed Id: 31932639. doi:10.1038/s41467-019-13898-5.
*Photosystem I (plant): Pisum sativum* E Eukaryota, 4.44 Å**	1QZV	Data File Jmol Viewer 1QZV	Ben-Shem et al. (2003). Ben-Shem A, Frolow F, & Nelson N (2003). Crystal structure of plant photosystem I. Nature 426 :630-635. PubMed Id: 14668855.
*Photosystem I (plant): Pisum sativum* E Eukaryota, 3.40 Å**	2O01	Data File Jmol Viewer 2O01	Amunts et al. (2007). Amunts A, Drory O, & Nelson N (2007). The structure of a plant photosystem I supercomplex at 3.4 Å resolution. Nature 447 :58-63. PubMed Id: 17476261.
*Photosystem I (Plant): Pisum sativum* E Eukaryota, 3.30 Å**	2WSC	Data File Jmol Viewer 2WSC	Amunts et al. (2010). Amunts A, Toporik H, Borovikova A, & Nelson N (2010). Structure determination and improved model of plant photosystem I. J Biol Chem 285 :3478-3486. PubMed Id: 19923216. doi:10.1074/jbc.M109.072645.
*Photosystem I (plant): Pisum sativum* E Eukaryota, 2.80 Å**	4XK8	Data File Jmol Viewer 4XK8	Qin et al. (2015). Qin X, Suga M, Kuang T, & Shen JR (2015). Photosynthesis. Structural basis for energy transfer pathways in the plant PSI-LHCI supercomplex. Science 348 :989-995. PubMed Id: 26023133. doi:10.1126/science.aab0214.
*Photosystem I + ferredoxin supercomplex: Pisum sativum* E Eukaryota, 2.50 Å** cryo-EM structure +ferredoxin+plastocyanin supercomplex, 2.70 Å: 6YEZ	6YAC	Data File Jmol Viewer 6YAC 6YEZ	Caspy et al. (2020). Caspy I, Borovikova-Sheinker A, Klaiman D, Shkolnisky Y, & Nelson N (2020). The structure of a triple complex of plant photosystem I with ferredoxin and plastocyanin. Nat Plants 6 10:1300-1305. PubMed Id: 33020607. doi:10.1038/s41477-020-00779-9.
*Photosystem I/plastocyanin complex: Pisum sativum* E Eukaryota, 2.74 Å** cryo-EM structure	6ZOO	Data File Jmol Viewer 6ZOO	Caspy et al. (2021). Caspy I, Fadeeva M, Kuhlgert S, Borovikova-Sheinker A, Klaiman D, Masrati G, Drepper F, Ben-Tal N, Hippler M, & Nelson N (2021). Structure of plant photosystem I-plastocyanin complex reveals strong hydrophobic interactions. Biochem J 478 12:2371-2384. PubMed Id: 34085703. doi:10.1042/BCJ20210267.
*Photosystem I. XFEL room temperature structure, dark state, LCLS/SwissFel: Thermosynechococcus vestitus* B Bacteria, 2.75 Å** PAL source, 3.00 Å, 7M76 SACLA PS I, 3.00 Å 7M78	7M75	Data File Jmol Viewer 7M75 7M78 7M76	Keable et al. (2021). Keable SM, Kölsch A, Simon PS, Dasgupta M, Chatterjee R, Subramanian SK, Hussein R, Ibrahim M, Kim IS, Bogacz I, Makita H, Pham CC, Fuller FD, Gul S, Paley D, Lassalle L, Sutherlin KD, Bhowmick A, Moriarty NW, Young ID, Blaschke JP, de Lichtenberg C, Chernev P, Cheah MH, Park S, Park G, Kim J, Lee SJ, Park J, Tono K, Owada S, Hunter MS, Batyuk A, Oggenfuss R, Sander M, Zerdane S, Ozerov D, Nass K, Lemke H, Mankowsky R, Brewster AS, Messinger J, Sauter NK, Yachandra VK, Yano J, Zouni A, & Kern J (2021). Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I. Sci Rep 11 1:21787. PubMed Id: 34750381. doi:10.1038/s41598-021-00236-3.
*Photosystem I in the presence of ferredoxin and cytochrome c6: Thermosynechococcus vestitus* E Eukaryota, 1.97 Å** cryo-EM structure	7FIX	Data File Jmol Viewer 7FIX	Li et al. (2022). Li J, Hamaoka N, Makino F, Kawamoto A, Lin Y, Rögner M, Nowaczyk MM, Lee YH, Namba K, Gerle C, & Kurisu G (2022). Structure of cyanobacterial photosystem I complexed with ferredoxin at 1.97 Å resolution. Commun Biol 5 1:951. PubMed Id: 36097054. doi:10.1038/s42003-022-03926-4.
*Photosystem I utilizing far-red light, trimer: Acaryochloris marina* B Bacteria, 2.50 Å** cryo-EM structure	7COY	Data File Jmol Viewer 7COY	Hamaguchi et al. (2021). Hamaguchi T, Kawakami K, Shinzawa-Itoh K, Inoue-Kashino N, Itoh S, Ifuku K, Yamashita E, Maeda K, Yonekura K, & Kashino Y (2021). Structure of the far-red light utilizing photosystem I of Acaryochloris marina. Nat Commun 12 1:2333. PubMed Id: 33879791. doi:10.1038/s41467-021-22502-8.
*Minimal Photosystem I: Dunaliella salina* E Eukaryota, 3.2 Å** cryo-EM structure x-ray structure, 3.4 Å: 6QPH	6RHZ	Data File Jmol Viewer 6RHZ 6QPH	Perez-Boerema et al. (2020). Perez-Boerema A, Klaiman D, Caspy I, Netzer-El SY, Amunts A, & Nelson N (2020). Structure of a minimal photosystem I from the green alga Dunaliella salina. Nat Plants 6 3:321-327. PubMed Id: 32123351. doi:10.1038/s41477-020-0611-9.
*Photosystem I chimera: Synechocystis sp. PCC 6803* E Eukaryota, 3.10 Å** cryo-EM structure	6UZV	Data File Jmol Viewer 6UZV	Toporik et al. (2020). Toporik H, Khmelnitskiy A, Dobson Z, Riddle R, Williams D, Lin S, Jankowiak R, & Mazor Y (2020). The structure of a red-shifted photosystem I reveals a red site in the core antenna. Nat Commun 11 1:5279. PubMed Id: 33077842. doi:10.1038/s41467-020-18884-w.
*Minimal Photosystem I: Synechocystis sp. PCC 6803* B Bacteria, 4.31 Å** cryo-EM structure	7O1V	Data File Jmol Viewer 7O1V	Akhtar et al. (2021). Akhtar P, Caspy I, Nowakowski PJ, Malavath T, Nelson N, Tan HS, & Lambrev PH (2021). Two-Dimensional Electronic Spectroscopy of a Minimal Photosystem I Complex Reveals the Rate of Primary Charge Separation. J Am Chem Soc 143 36:14601-14612. PubMed Id: 34472838. doi:10.1021/jacs.1c05010.
*NDH-PSI Cyclic electron transport supercomplex: Arabidopsis thaliana* E Eukaryota, 3.89 Å** cryo-EM structure Left PSI in the cyclic electron transport supercomplex, 3.25 Å 7WFD Right PSI in the cyclic electron transfer supercomplex, 3.25 Å 7WFE Subcomplexes B,M and L, 3.59 Å 7WFF Subcomplexes A and E, 4.33 Å 7WFG	7WG5	Data File Jmol Viewer 7WG5 7WFF 7WFE 7WFD 7WFG	Su et al. (2022). Su X, Cao D, Pan X, Shi L, Liu Z, Dall'Osto L, Bassi R, Zhang X, & Li M (2022). Supramolecular assembly of chloroplast NADH dehydrogenase-like complex with photosystem I from Arabidopsis thaliana. Mol Plant 15 3:454-467. PubMed Id: 35123031. doi:10.1016/j.molp.2022.01.020.
*trimeric high-light-tolerant photosystem I: Cyanobacterium aponinum* B Bacteria, 2.70 Å** cryo-EM structure	6VPV	Data File Jmol Viewer 6VPV	Dobson et al. (2021). Dobson Z, Ahad S, Vanlandingham J, Toporik H, Vaughn N, Vaughn M, Williams D, Reppert M, Fromme P, & Mazor Y (2021). The structure of photosystem I from a high-light-tolerant cyanobacteria. Elife 10 :e67518. PubMed Id: 34435952. doi:10.7554/eLife.67518.
*Photosystem I from a chlorophyll d-containing cyanobacterium: Acaryochloris marina* B Bacteria, 3.30 Å** cryo-EM structure	7DWQ	Data File Jmol Viewer 7DWQ	Xu et al. (2021). Xu C, Zhu Q, Chen JH, Shen L, Yi X, Huang Z, Wang W, Chen M, Kuang T, Shen JR, Zhang X, & Han G (2021). A unique photosystem I reaction center from a chlorophyll d-containing cyanobacterium Acaryochloris marina. J Integr Plant Biol 63 10:1740-1752. PubMed Id: 34002536. doi:10.1111/jipb.13113.
*PSI-NADH dehydrogenase-like (NDH) supercomplex: Hordeum vulgare* E Eukaryota, 4.50 Å** cryo-EM structure NDH complex, 3.70 Å 7EU3 photosystem I-LHCI-Lhca5 supercomplex, 3.40 Å 7EW6 photosystem I-LHCI-Lhca6 supercomplex, 3.88 Å 7EWK	7F9O	Data File Jmol Viewer 7F9O 7EW6 7EWK 7EU3	Shen et al. (2022). Shen L, Tang K, Wang W, Wang C, Wu H, Mao Z, An S, Chang S, Kuang T, Shen JR, Han G, & Zhang X (2022). Architecture of the chloroplast PSI-NDH supercomplex in Hordeum vulgare. Nature 601 7894:649-654. PubMed Id: 34879391. doi:10.1038/s41586-021-04277-6.
*primordial cyanobacterial photosystem I: Gloeobacter violaceus* B Bacteria, 2.04 Å** cryo-EM structure	7F4V	Data File Jmol Viewer 7F4V	Kato et al. (2022). Kato K, Hamaguchi T, Nagao R, Kawakami K, Ueno Y, Suzuki T, Uchida H, Murakami A, Nakajima Y, Yokono M, Akimoto S, Dohmae N, Yonekura K, & Shen JR (2022). Structural basis for the absence of low-energy chlorophylls in a photosystem I trimer from Gloeobacter violaceus. Elife 11 :e73990. PubMed Id: 35404232. doi:10.7554/eLife.73990.
*Photosystem II: Thermosynechococcus elongatus* B Bacteria, 3.8 Å**	1FE1	Data File Jmol Viewer 1FE1	Zouni et al. (2001). Zouni A, Horst-Tobias W, Kern J, Fromme P, Krauss N, Saenger W, & Orth P (2001). Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature 409 :739-743. PubMed Id: 11217865.
*Photosystem II: Thermosynechococcus elongatus* B Bacteria, 3.5 Å** Resolution sufficient to reveal oxygen-evolving center.	1S5L	Data File Jmol Viewer 1S5L Photosystem II Q(B) protein photosystem II core light harvesting protein Photosystem II CP43 protein Photosystem II D2 protein Photosystem II Cytochrome b559 alpha subunit Photosystem II Cytochrome b559 beta subunit Photosystem II PsbH protein Photosystem II PsbI protein Photosystem II PsbJ protein Photosystem II PsbK protein Photosystem II PsbL protein Photosystem II PsbM protein Photosystem II PsbT protein Photosystem II PsbX protein Photosystem II PsbN protein Photosystem II PsbZ protein	Ferreira et al. (2004). Ferreira KN, Iverson TM, Maghlaoui K, Barber J, & Iwata S (2004). Architecture of the photosynthetic oxygen-evolving center. Science 303 :1831-1838. PubMed Id: 14764885.
*Photosystem II: Thermosynechococcus elongatus* B Bacteria, 3.0 Å** Shows locations of 77 cofactors per monomer and provides info on Mn₄Ca cluster.	2AXT	Data File Jmol Viewer 2AXT	Loll et al. (2005). Loll B, Kern J, Saenger W, Zouni A, & Biesiadka J (2005). Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II. Nature 438 :1040-1044. PubMed Id: 16355230.
*Photosystem II: Thermosynechococcus elongatus* B Bacteria, 2.9 Å** Includes all 20 protein subunits and all 35 chlorophyll a molecules. Part 2 of coördinate file: 3BZ2	3BZ1	Data File Jmol Viewer 3BZ1 3BZ2	Guskov et al. (2009). Guskov A, Kern J, Gabdulkhakov A, Broser M, Zouni A, & Saenger W (2009). Cyanobacterial photosystem II at 2.9-Å resolution and the role of quinones, lipids, channels and chloride. Nat Struct Mol Biol 16 :334-342. PubMed Id: 19219048.
*Photosystem II in S1 state by femtosecond x-ray laser: Thermosynechococcus elongatus* B Bacteria, 5.00 Å** In S state after two flashes (S3), 5.50 Å: 4Q54	4PBU	Data File Jmol Viewer 4PBU 4Q54	Kupitz et al. (2014). Kupitz C, Basu S, Grotjohann I, Fromme R, Zatsepin NA, Rendek KN, Hunter MS, Shoeman RL, White TA, Wang D, James D, Yang JH, Cobb DE, Reeder B, Sierra RG, Liu H, Barty A, Aquila AL, Deponte D, Kirian RA, Bari S, Bergkamp JJ, Beyerlein KR, Bogan MJ, Caleman C, et al. & Fromme P (2014). Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser. Nature 513 7517:261-265. PubMed Id: 25043005. doi:10.1038/nature13453.
*Photosystem II imaged using imperfect crystals (Bragg peaks only): Thermosynechococcus elongatus* B Bacteria, 4.5 Å** pseudo-crystal refinement, 3.5 Å: 5E79	5E7C	Data File Jmol Viewer 5E7C 5E79	Ayyer et al. (2016). Ayyer K, Yefanov OM, Oberthür D, Roy-Chowdhury S, Galli L, Mariani V, Basu S, Coe J, Conrad CE, Fromme R, Schaffer A, Dörner K, James D, Kupitz C, Metz M, Nelson G, Xavier PL, Beyerlein KR, Schmidt M, Sarrou I, Spence JC, Weierstall U, White TA, Yang JH, Zhao Y, Liang M, Aquila A, Hunter MS, Robinson JS, Koglin JE, Boutet S, Fromme P, Barty A, & Chapman HN (2016). Macromolecular diffractive imaging using imperfect crystals. Nature 530 :202-206. PubMed Id: 26863980. doi:10.1038/nature16949.
*Photosystem II at room temperature in dark state: Thermosynechococcus elongatus* E Eukaryota, 3.0 Å** XFEL structure Native doubly illuminated complex, 2.25 Å: 5TIS Structure 500 ms after the 2nd illumination, 2.8 Å: 5KAI	5KAF	Data File Jmol Viewer 5KAF 5KAI 5TIS	Young et al. (2016). Young ID, Ibrahim M, Chatterjee R, Gul S, Fuller FD, Koroidov S, Brewster AS, Tran R, Alonso-Mori R, Kroll T, Michels-Clark T, Laksmono H, Sierra RG, Stan CA, Hussein R, Zhang M, Douthit L, Kubin M, de Lichtenberg C, Vo Pham L, Nilsson H, Cheah MH, Shevela D, Saracini C, Bean MA, Seuffert I, Sokaras D, Weng TC, Pastor E, Weninger C, Fransson T, Lassalle L, Bräuer P, Aller P, Docker PT, Andi B, Orville AM, Glownia JM, Nelson S, Sikorski M, Zhu D, Hunter MS, Lane TJ, Aquila A, Koglin JE, Robinson J, Liang M, Boutet S, Lyubimov AY, Uervirojnangkoorn M, Moriarty NW, Liebschner D, Afonine PV, Waterman DG, Evans G, Wernet P, Dobbek H, Weis WI, Brunger AT, Zwart PH, Adams PD, Zouni A, Messinger J, Bergmann U, Sauter NK, Kern J, Yachandra VK, & Yano J (2016). Structure of photosystem II and substrate binding at room temperature. Nature 540 :453-457. PubMed Id: 27871088. doi:10.1038/nature20161.
*Photosystem II (0F, S1-rich): Thermosynechococcus elongatus* E Eukaryota, 2.08 Å** XFEL structure one-flash state (1F, S2-rich), 2.26 Å: 6W1P 50 microseconds after the second illumination, 2.27 Å: 6W1Q 150 microseconds after the second illumination, 2.23 Å: 6W1R 250 microseconds after the second illumination, 2.01 Å: 6W1T 400 microseconds after the second illumination, 2.09 Å: 6W1U two-flash state of Photosystem II (2F, S3-rich), 2.09 Å: 6W1V	6W1O	Data File Jmol Viewer 6W1O 6W1P 6W1T 6W1U 6W1Q 6W1R 6W1V	Ibrahim et al. (2020). Ibrahim M, Fransson T, Chatterjee R, Cheah MH, Hussein R, Lassalle L, Sutherlin KD, Young ID, Fuller FD, Gul S, Kim IS, Simon PS, de Lichtenberg C, Chernev P, Bogacz I, Pham CC, Orville AM, Saichek N, Northen T, Batyuk A, Carbajo S, Alonso-Mori R, Tono K, Owada S, Bhowmick A, Bolotovsky R, Mendez D, Moriarty NW, Holton JM, Dobbek H, Brewster AS, Adams PD, Sauter NK, Bergmann U, Zouni A, Messinger J, Kern J, Yachandra VK, & Yano J (2020). Untangling the sequence of events during the S2 ? S3 transition in photosystem II and implications for the water oxidation mechanism. Proc Natl Acad Sci USA 117 23:12624-12635. PubMed Id: 32434915. doi:10.1073/pnas.2000529117.
*Photosystem II assembly intermediates, PSII-M: Thermosynechococcus elongatus* E Eukaryota, 2.66 Å** cryo-EM structure PSII with Psb27, Psb28, and Psb34; 2.72 Å: 7NHP PSII with Psb28, and Psb34; 2.68 Å: 7NHQ	7NHO	Data File Jmol Viewer 7NHO 7NHQ 7NHP	Zabret et al. (2021). Zabret J, Bohn S, Schuller SK, Arnolds O, Möller M, Meier-Credo J, Liauw P, Chan A, Tajkhorshid E, Langer JD, Stoll R, Krieger-Liszkay A, Engel BD, Rudack T, Schuller JM, & Nowaczyk MM (2021). Structural insights into photosystem II assembly. Nat Plants 7 4:524-538. PubMed Id: 33846594. doi:10.1038/s41477-021-00895-0.
*Photosystem II, RT XFEL structure averaged across all S-states: Thermosynechococcus vestitus* B Bacteria, 1.89 Å** dark-stable state (0F, S1 rich), 2.08 Å 7RF2 one-flash state (1F, S2-rich), 2.26 Å 7FR3 50 microseconds after the second illumination, 2.27 Å 7RF4 150 microseconds after the second illumination, 2.23 Å 7RF5 250 microseconds after the second illumination, 2.01 Å 7RF6 400 microseconds after the second illumination, 2.09 Å 7RF7	7RF1	Data File Jmol Viewer 7RF1 7RF6 7RF2 7RF5 7FR3 7RF7 7RF4	Hussein et al. (2021). Hussein R, Ibrahim M, Bhowmick A, Simon PS, Chatterjee R, Lassalle L, Doyle M, Bogacz I, Kim IS, Cheah MH, Gul S, de Lichtenberg C, Chernev P, Pham CC, Young ID, Carbajo S, Fuller FD, Alonso-Mori R, Batyuk A, Sutherlin KD, Brewster AS, Bolotovsky R, Mendez D, Holton JM, Moriarty NW, Adams PD, Bergmann U, Sauter NK, Dobbek H, Messinger J, Zouni A, Kern J, Yachandra VK, & Yano J (2021). Structural dynamics in the water and proton channels of photosystem II during the S2 to S3 transition. Nat Commun 12 1:6531. PubMed Id: 34764256. doi:10.1038/s41467-021-26781-z.
*Photosystem II: Thermosynechococcus vulcanus* B Bacteria, 3.7 Å**	1IZL	Data File Jmol Viewer 1IZL	Kamiya & Shen (2003). Kamiya N & Shen JR (2003). Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Å resolution. Proc Natl Acad Sci USA 100 :98-103. PubMed Id: 12518057.
*Photosystem II, Br-substituted: Thermosynechococcus vulcanus* B Bacteria, 3.7 Å** Br-substitution reveals location of chlorides. I-substituted, 4.0 Å: 3A0H	3A0B	Data File Jmol Viewer 3A0B 3A0H	Kawakami et al. (2009). Kawakami K, Umena Y, Kamiya N, & Shen JR (2009). Location of chloride and its possible functions in oxygen-evolving photosystem II revealed by X-ray crystallography. Proc Natl Acad Sci USA 106 :8567-8572. PubMed Id: 19433803.
*Photosystem II: Thermosynechococcus vulcanus* B Bacteria, 1.90 Å** Reveals the structure of the Mn₄CaO₅ cluster and all of their ligands. More than 1300 water molecules are observed in each monomer.	3ARC	Data File Jmol Viewer 3ARC	Umena et al. (2011). Umena Y, Kawakami K, Shen JR, & Kamiya N (2011). Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å; Nature 473 :55-60. PubMed Id: 21499260. doi:10.1038/nature09913.
*Photosystem II, Sr-substituted: Thermosynechococcus vulcanus* B Bacteria, 2.10 Å**	4IL6	Data File Jmol Viewer 4IL6	Koua et al. (2013). Koua FH, Umena Y, Kawakami K, & Shen JR (2013). Structure of Sr-substituted photosystem II at 2.1 Å resolution and its implications in the mechanism of water oxidation. Proc Natl Acad Sci USA 110 :3889-3894. PubMed Id: 23426624. doi:10.1073/pnas.1219922110.
*Photosystem II by femtosecond X-ray pulses, data set 1: Thermosynechococcus vulcanus* B Bacteria, 1.95 Å** Data set 2, 1.95 Å: 4UB8	4UB6	Data File Jmol Viewer 4UB6 4UB8	Suga et al. (2015). Suga M, Akita F, Hirata K, Ueno G, Murakami H, Nakajima Y, Shimizu T, Yamashita K, Yamamoto M, Ago H, & Shen J (2015). Native structure of photosystem II at 1.95 Å resolution viewed by femtosecond X-ray pulses. Nature 517 :99-103. PubMed Id: 25470056. doi:10.1038/nature13991.
*Photosystem II by femtosecond X-ray pulses, preflash dark state: Thermosynechococcus vulcanus* E Eukaryota, 2.35 Å** preflash-2F data, 2.35 Å: 5WS6 dark data, 2.50 Å: 5GTH 2F-data, 2.50 Å: 5GTI	5WS5	Data File Jmol Viewer 5WS5 5GTH 5GTI 5WS6	Suga et al. (2017). Suga M, Akita F, Sugahara M, Kubo M, Nakajima Y, Nakane T, Yamashita K, Umena Y, Nakabayashi M, Yamane T, Nakano T, Suzuki M, Masuda T, Inoue S, Kimura T, Nomura T, Yonekura S, Yu LJ, Sakamoto T, Motomura T, Chen JH, Kato Y, Noguchi T, Tono K, Joti Y, Kameshima T, Hatsui T, Nango E, Tanaka R, Naitow H, Matsuura Y, Yamashita A, Yamamoto M, Nureki O, Yabashi M, Ishikawa T, Iwata S, & Shen JR (2017). Light-induced structural changes and the site of O=O bond formation in PSII caught by XFEL. Nature 543 :131-135. PubMed Id: 28219079. doi:10.1038/nature21400.
*Photosystem II by femtosecond X-ray pulses, dark state, dataset1: Thermosynechococcus vulcanus* E Eukaryota, 2.15 Å** 1F state, dataset1, 2.15 Å: 6JLK 2F state, dataset1, 2.15 Å: 6JLL dark state, dataset2, 2.35 Å: 6JLM 1F state, dataset2, 2.4 Å: 6JLN 2F state, dataset2, 2.4 Å: 6JLO 3F state, dataset2, 2.5 Å: 6JLP	6JLJ	Data File Jmol Viewer 6JLJ 6JLP 6JLL 6JLK 6JLO 6JLM 6JLN	Suga et al. (2019). Suga M, Akita F, Yamashita K, Nakajima Y, Ueno G, Li H, Yamane T, Hirata K, Umena Y, Yonekura S, Yu LJ, Murakami H, Nomura T, Kimura T, Kubo M, Baba S, Kumasaka T, Tono K, Yabashi M, Isobe H, Yamaguchi K, Yamamoto M, Ago H, & Shen JR (2019). An oxyl/oxo mechanism for oxygen-oxygen coupling in PSII revealed by an x-ray free-electron laser. Science 366 6463:334-338. PubMed Id: 31624207. doi:10.1126/science.aax6998.
*Psb27-Photosystem II complex, dimeric state: Thermosynechococcus vulcanus* B Bacteria, 3.78 Å** cryo-EM structure	7CZL	Data File Jmol Viewer 7CZL	Huang et al. (2021). Huang G, Xiao Y, Pi X, Zhao L, Zhu Q, Wang W, Kuang T, Han G, Sui SF, & Shen JR (2021). Structural insights into a dimeric Psb27-photosystem II complex from a cyanobacterium Thermosynechococcus vulcanus. Proc Natl Acad Sci U S A 118 5:e2018053118. PubMed Id: 33495333. doi:10.1073/pnas.2018053118.
*Photosystem II, high-dose data set: Thermosynechococcus vulcanus* E Eukaryota, 1.95 Å** cryo-EM structure low-dose data set, 2.08 Å: 7D1U	7D1T	Data File Jmol Viewer 7D1T 7D1U	Kato et al. (2021). Kato K, Miyazaki N, Hamaguchi T, Nakajima Y, Akita F, Yonekura K, & Shen JR (2021). High-resolution cryo-EM structure of photosystem II reveals damage from high-dose electron beams. Commun Biol 4 1:382. PubMed Id: 33753866. doi:10.1038/s42003-021-01919-3.
*Photosystem II monomer: Thermosynechococcus vulcanus* B Bacteria, 2.78 Å** cryo-EM structure	7EDA	Data File Jmol Viewer 7EDA	Yu et al. (2021). Yu H, Hamaguchi T, Nakajima Y, Kato K, Kawakami K, Akita F, Yonekura K, & Shen JR (2021). Cryo-EM structure of monomeric photosystem II at 2.78 Å resolution reveals factors important for the formation of dimer. Biochim Biophys Acta Bioenerg 1862 10:148471. PubMed Id: 34216574. doi:10.1016/j.bbabio.2021.148471.
*Photosystem II, in the dark S1 state: Thermostichus vulcanus* B Bacteria, 2.25 Å** in the S1 state, 2.35 Å 7CJI in the S2 state, 2.40 Å 7CJJ	7COU	Data File Jmol Viewer 7COU 7CJI 7CJJ	Li et al. (2021). Li H, Nakajima Y, Nomura T, Sugahara M, Yonekura S, Chan SK, Nakane T, Yamane T, Umena Y, Suzuki M, Masuda T, Motomura T, Naitow H, Matsuura Y, Kimura T, Tono K, Owada S, Joti Y, Tanaka R, Nango E, Akita F, Kubo M, Iwata S, Shen JR, & Suga M (2021). Capturing structural changes of the S1 to S2 transition of photosystem II using time-resolved serial femtosecond crystallography. IUCrJ 8 :431-443. PubMed Id: 33953929. doi:10.1107/S2052252521002177.
*Photosystem II intermediate Psb28-RC47: Thermostichus vulcanus* E Eukaryota, 3.14 Å** cryo-EM structure intermediate Psb28-PSII complex, 3.14 Å: 7DXH	7DXA	Data File Jmol Viewer 7DXA 7DXH	Xiao et al. (2021). Xiao Y, Huang G, You X, Zhu Q, Wang W, Kuang T, Han G, Sui SF, & Shen JR (2021). Structural insights into cyanobacterial photosystem II intermediates associated with Psb28 and Tsl0063. Nat Plants 7 8:1132-1142. PubMed Id: 34226692. doi:10.1038/s41477-021-00961-7.
*Photosystem II complex, with bound DCBQ: Thermostitchus vulcanus* E Eukaryota, 2.15 Å** with bound DBBQ, 2.10 Å: 8GN1 with bound PPBQ, 1.95 Å: 8GN2	8GN0	Data File Jmol Viewer 8GN0 8GN1 8GN2	Kamada et al. (2023). Kamada S, Nakajima Y, & Shen JR (2023). Structural insights into the action mechanisms of artificial electron acceptors in photosystem II. J Biol Chem 299 7:104839. PubMed Id: 37209822. doi:10.1016/j.jbc.2023.104839.
*Photosystem II from a red alga: Cyanidium caldarium* E Eukaryota, 2.77 Å**	4YUU	Data File Jmol Viewer 4YUU	Ago et al. (2016). Ago H, Adachi H, Umena Y, Tashiro T, Kawakami K, Kamiya N, Tian L, Han G, Kuang T, Liu Z, Wang F, Zou H, Enami I, Miyano M, & Shen JR (2016). Novel Features of Eukaryotic Photosystem II Revealed by Its Crystal Structure Analysis from a Red Alga. J Biol Chem 291 :5676-5687. PubMed Id: 26757821. doi:10.1074/jbc.M115.711689.
*C2S2M2-type Photosystem II supercomplex: Arabidopsis thaliana* E Eukaryota, 2.79 Å** cryo-EM structure	7OUI	Data File Jmol Viewer 7OUI	Graça et al. (2021). Graça AT, Hall M, Persson K, & Schröder WP (2021). High-resolution model of Arabidopsis Photosystem II reveals the structural consequences of digitonin-extraction. Sci Rep 11 1:15534. PubMed Id: 34330992. doi:10.1038/s41598-021-94914-x.
*Photosystem II, full electron dose: Synechocystis sp. PCC 6803* B Bacteria, 1.93 Å** cryo-EM structure low electron dose, 2.01 Å 7RCV	7N8O	Data File Jmol Viewer 7N8O 7RCV	Gisriel et al. (2022). Gisriel CJ, Wang J, Liu J, Flesher DA, Reiss KM, Huang HL, Yang KR, Armstrong WH, Gunner MR, Batista VS, Debus RJ, & Brudvig GW (2022). High-resolution cryo-electron microscopy structure of photosystem II from the mesophilic cyanobacterium, Synechocystis sp. PCC 6803. Proc Natl Acad Sci U S A 119 1:e2116765118. PubMed Id: 34937700. doi:10.1073/pnas.2116765118.
Light-Harvesting Complexes
*Light-Harvesting Complex: Rhodoblastus acidophilus* B Bacteria, 2.50 Å** Former species name: Rhodopseudomonas acidophila	1KZU	Data File Jmol Viewer 1KZU Light Harvesting Complex. alpha chain Light Harvesting Complex. beta chain	Prince et al. (1997). Prince SM, Papiz MZ, Freer AA, McDermott G, Hawthornthwaite-Lawless AM, Cogdell RJ, & Isaacs NW (1997). Apoprotein structure in the LH2 complex from Rhodopseudomonas acidophila strain 10050: modular assembly and protein pigment interactions. J Mol Biol 268 :412-423. PubMed Id: 9159480. doi:10.1006/jmbi.1997.0966. See also: McDermott et al. (1995) McDermott G, Prince SM, Freer AA, Hawthornthwaite-Lawless AM, Papiz MZ, Cogdell RJ & Isaacs NW (1995). Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria. Nature 374 :517-521. doi:10.1038/374517a0.
*Light-Harvesting Complex: Rhodoblastus acidophila* B Bacteria, 2.0 Å** Former species name: Rhodopseudomonas acidophila	1NKZ	Data File Jmol Viewer 1NKZ	Papiz et al. (2003). Papiz MZ, Prince SM, Howard T, Cogdell RJ, & Isaacs NW (2003). The structure and thermal motion of the B800-850 LH2 complex from Rps.acidophila at 2.0A resolution and 100K: new structural features and functionally relevant motions. J Mol Biol 278 :31303-31311. PubMed Id: 12595263.
*Light-Harvesting Complex: Rhodospirillum molischianum* B Bacteria, 2.4 Å**	1LGH	Data File Jmol Viewer 1LGH Light Harvesting Complex. alpha chain Light Harvesting Complex. beta chain	Koepke et al. (1996). Koepke J, Hu XC, Muenke C, Schulten K, & Michel H (1996). The crystal structure of the light-harvesting complex II (B800- 850) from Rhodospirillum molischianum. Structure 4 :581-597. PubMed Id: 8736556.
*Light-Harvesting Complex LHC-II, Spinach Photosystem II: Spinacia oleracea* E Eukaryota, 2.72 Å**	1RWT	Data File Jmol Viewer 1RWT LHC-II	Liu et al. (2004). Liu Z, Yan H, Wang K, Kuang T, Zhang J, Gui L, An X, & Chang W (2004). Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution. Nature 428 :287-292. PubMed Id: 15029188.
*Light-Harvesting Complex CP29, Spinach Photosystem II: Spinacia oleracea* E Eukaryota, 2.80 Å**	3PL9	Data File Jmol Viewer 3PL9	Pan et al. (2011). Pan X, Li M, Wan T, Wang L, Jia C, Hou Z, Zhao X, Zhang J, & Chang W (2011). Structural insights into energy regulation of light-harvesting complex CP29 from spinach. Nat Struc Mol Biol 18 :309-315. PubMed Id: 21297637.
*Light-Harvesting Complex LHC-II, Pea Photosystem II: Pisum sativum* E Eukaryota, 2.50 Å**	2BHW	Data File Jmol Viewer 2BHW	Standfuss et al. (2005). Standfuss J, Terwisscha van Scheltinga AC, Lamborghini M, Kühlbrandt W (2005). Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 Å resolution. EMBO J 24 :919-928. PubMed Id: 15719016.
*fucoxanthin and chlorophyll a/c complex: Phaeodactylum tricornutum* E Eukaryota, 1.8 Å**	6A2W	Data File Jmol Viewer 6A2W	Wang et al. (2019). Wang W, Yu LJ, Xu C, Tomizaki T, Zhao S, Umena Y, Chen X, Qin X, Xin Y, Suga M, Han G, Kuang T, & Shen JR (2019). Structural basis for blue-green light harvesting and energy dissipation in diatoms. Science 363 6427. PubMed Id: 30733387. doi:10.1126/science.aav0365.
*Light-Harvesting Complex LHC-II: Marichromatium purpuratum* B Bacteria, 2.38 Å** cryo-EM structure	6ZXA	Data File Jmol Viewer 6ZXA	Gardiner et al. (2021). Gardiner AT, Naydenova K, Castro-Hartmann P, Nguyen-Phan TC, Russo CJ, Sader K, Hunter CN, Cogdell RJ, & Qian P (2021). The 2.4 Å cryo-EM structure of a heptameric light-harvesting 2 complex reveals two carotenoid energy transfer pathways. Sci Adv 7 7:eabe4650. PubMed Id: 33579696. doi:10.1126/sciadv.abe4650.
*Light-Harvesting Complex LHC-II: Cereibacter sphaeroides* B Bacteria, 2.10 Å** cryo-EM structure	7PBW	Data File Jmol Viewer 7PBW	Qian et al. (2021). Qian P, Swainsbury DJK, Croll TI, Castro-Hartmann P, Divitini G, Sader K, & Hunter CN (2021). Cryo-EM Structure of the Rhodobacter sphaeroides Light-Harvesting 2 Complex at 2.1 Å. Biochemistry 60 44:3302-3314. PubMed Id: 34699186. doi:10.1021/acs.biochem.1c00576.
Photosystem+Light-Harvesting Complex Supercomplex
*Photosystem I-Light harvesting complex supercomplex with 5 Lhcr antennae: Cyanidioschyzon merolae* E Eukaryota, 3.63 Å** with 3 Lhcr antennae, 3.82 Å: 5ZGH	5ZGB	Data File Jmol Viewer 5ZGB 5ZGH	Pi et al. (2018). Pi X, Tian L, Dai HE, Qin X, Cheng L, Kuang T, Sui SF, & Shen JR (2018). Unique organization of photosystem I-light-harvesting supercomplex revealed by cryo-EM from a red alga. Proc Natl Acad Sci USA 115 17:4423-4428. PubMed Id: 29632169. doi:10.1073/pnas.1722482115.
*Photosystem I supercomplex with light-harvesting complexes I & II: Zea mays* E Eukaryota, 3.3 Å** cryo-EM structure	5ZJI	Data File Jmol Viewer 5ZJI	Pan et al. (2018). Pan X, Ma J, Su X, Cao P, Chang W, Liu Z, Zhang X, & Li M (2018). Structure of the maize photosystem I supercomplex with light-harvesting complexes I and II. Science 360 6393:1109-1113. PubMed Id: 29880686. doi:10.1126/science.aat1156.
*Photosystem I supercomplex with 8 light-harvesting complexes I: Chlamydomonas reinhardtii* E Eukaryota, 2.89 Å** cryo-EM structure with 10 LHCI, 3.3 Å: 6IJO	6IJJ	Data File Jmol Viewer 6IJJ 6IJO	Su et al. (2019). Su X, Ma J, Pan X, Zhao X, Chang W, Liu Z, Zhang X, & Li M (2019). Antenna arrangement and energy transfer pathways of a green algal photosystem-I-LHCI supercomplex. Nat Plants 5 3:273-281. PubMed Id: 30850819. doi:10.1038/s41477-019-0380-5.
*Photosystem I supercomplex with 10 light-harvesting complexes I: Chlamydomonas reinhardtii* E Eukaryota, 2.9 Å** cryo-EM structure with 8 light-harvesting complexes, 2.9 Å: 6JO6	6JO5	Data File Jmol Viewer 6JO5 6JO6	Suga et al. (2019). Suga M, Ozawa SI, Yoshida-Motomura K, Akita F, Miyazaki N, & Takahashi Y (2019). Structure of the green algal photosystem I supercomplex with a decameric light-harvesting complex I. Nat Plants 5 6:626-636. PubMed Id: 31182847. doi:10.1038/s41477-019-0438-4.
*Photosystem I-LHCI-LHCII supercomplex from from double phosphatase mutant pph1: Chlamydomonas reinhardtii* E Eukaryota, 2.84 Å** cryo-EM structure from the LhcbM1 lacking mutant, 3.16 Å 7DZ8 from the double phosphatase mutant pph1;pbcp, 3.13 Å 7E0J double phosphatase mutant pph1;pbcp, 3.09 Å 7E0K from the LhcbM1 lacking mutant, 3.75 Å 7E0H from the LhcbM1 lacking mutant, 3.53 Å 7E0I	7DZ7	Data File Jmol Viewer 7DZ7 7E0K 7E0J 7E0H 7E0I 7DZ8	Pan et al. (2021). Pan X, Tokutsu R, Li A, Takizawa K, Song C, Murata K, Yamasaki T, Liu Z, Minagawa J, & Li M (2021). Structural basis of LhcbM5-mediated state transitions in green algae. Nat Plants 7 8:1119-1131. PubMed Id: 34239095. doi:10.1038/s41477-021-00960-8.
*Photosystem I-LHCI supercomplex: Chlamydomonas reinhardtii* E Eukaryota, 3.40 Å**	8H2U	Data File Jmol Viewer 8H2U	Gerle et al. (2023). Gerle C, Misumi Y, Kawamoto A, Tanaka H, Kawai-Kubota H, Tokutsu R, Kim E, Chorev D, Abe K, Robinson CV, Mitsuoka K, Minagawa J, & Kurisu G (2023). Three structures of PSI-LHCI from Chlamydomonas reinhardtii suggest a resting state re-activated by ferredoxin. Biochim Biophys Acta Bioenerg . PubMed Id: 37270022. doi:10.1016/j.bbabio.2023.148986.
*Photosystem I IsiA supercomplex: Synechocystis sp.* B Bacteria, 3.48 Å** cryo-EM structure	6NWA	Data File Jmol Viewer 6NWA	Toporik et al. (2019). Toporik H, Li J, Williams D, Chiu PL, & Mazor Y (2019). The structure of the stress-induced photosystem I-IsiA antenna supercomplex. Nat Struct Mol Biol 26 6:443-449. PubMed Id: 31133699. doi:10.1038/s41594-019-0228-8.
*Photosystem I-IsiA supercomplex: Thermosynechococcus vulcanus* B Bacteria, 2.74 Å** cryo-EM structure	6K33	Data File Jmol Viewer 6K33	Akita et al. (2020). Akita F, Nagao R, Kato K, Nakajima Y, Yokono M, Ueno Y, Suzuki T, Dohmae N, Shen JR, Akimoto S, & Miyazaki N (2020). Structure of a cyanobacterial photosystem I surrounded by octadecameric IsiA antenna proteins. Commun Biol 3 1. PubMed Id: 32393811. doi:10.1038/s42003-020-0949-6.
*Photosystem I-IsiA-flavodoxin supercomplex: Synechococcus elongatus PCC 7942* B Bacteria (expressed in E. coli), 3.30 Å** cryo-EM structure Photosystem I-IsiA supercomplex, 2.90 Å: 6KIG	6KIF	Data File Jmol Viewer 6KIF 6KIG	Cao et al. (2020). Cao P, Cao D, Si L, Su X, Tian L, Chang W, Liu Z, Zhang X, & Li M (2020). Structural basis for energy and electron transfer of the photosystem I-IsiA-flavodoxin supercomplex. Nat Plants 6 2:167-176. PubMed Id: 32042157. doi:10.1038/s41477-020-0593-7.
*Photosystem I in complex with Light-Harvesting Complex: Physcomitrium patens* E Eukaryota, 3.23 Å** cryo-EM structure	6L35	Data File Jmol Viewer 6L35	Yan et al. (2021). Yan Q, Zhao L, Wang W, Pi X, Han G, Wang J, Cheng L, He YK, Kuang T, Qin X, Sui SF, & Shen JR (2021). Antenna arrangement and energy-transfer pathways of PSI-LHCI from the moss Physcomitrella patens. Cell Discov 7 1:10. PubMed Id: 33589616. doi:10.1038/s41421-021-00242-9.
*Photosystem I in complex with Light-Harvesting Complex: Physcomitrium patens* E Eukaryota, 2.80 Å** cryo-EM structure without PsaO subunit, 2.80 Å 7KUX PsaO alone, 3.76 Å 7KU5	7KSQ	Data File Jmol Viewer 7KSQ 7KUX 7KU5	Gorski et al. (2022). Gorski C, Riddle R, Toporik H, Da Z, Dobson Z, Williams D, & Mazor Y (2022). The structure of the Physcomitrium patens photosystem I reveals a unique Lhca2 paralogue replacing Lhca4. Nat Plants 8 3:307-316. PubMed Id: 35190662. doi:10.1038/s41477-022-01099-w.
*Photosystem II in complex with Light-Harvesting Complex: Chaetoceros gracilis* E Eukaryota, 3.02 Å** cryo-EM structure	6JLU	Data File Jmol Viewer 6JLU	Pi et al. (2019). Pi X, Zhao S, Wang W, Liu D, Xu C, Han G, Kuang T, Sui SF, & Shen JR (2019). The pigment-protein network of a diatom photosystem II-light-harvesting antenna supercomplex. Science 365 6452. PubMed Id: 31371578. doi:10.1126/science.aax4406.
*Photosystem II in complex with Light-Harvesting Complex II: Spinacia oleracea* E Eukaryota, 3.2 Å** Cryo-EM structure	3CJU	Data File Jmol Viewer 3CJU	Wei et al. (2016). Wei X, Su X, Cao P, Liu X, Chang W, Li M, Zhang X, & Liu Z (2016). Structure of spinach photosystem II-LHCII supercomplex at 3.2?Å resolution. Nature 534 :69-74. PubMed Id: 27251276. doi:10.1038/nature18020.
*stacked C₂S₂M₂-type PSII-LHCII complex: Pisum sativum* E Eukaryota, 2.7 Å** cryo-EM structure unstacked form, 3.2 Å: 5XNM M-LHCII and CP24 complexes in the stacked form, 3.6 Å: 5XNN M-LHCII and CP24 complexes in the unstacked form, 3.5 Å: 5XNO	5XNL	Data File Jmol Viewer 5XNL 5XNO 5XNM 5XNN	Su et al. (2017). Su X, Ma J, Wei X, Cao P, Zhu D, Chang W, Liu Z, Zhang X, & Li M (2017). Structure and assembly mechanism of plant C₂S₂M₂-type PSII-LHCII supercomplex. Science 357 :815-820. PubMed Id: 28839073. doi:10.1126/science.aan0327.
*photosystem I-light harvesting complex I supercomplex: Pisum sativum* E Eukaryota, 2.39 Å**	7DKZ	Data File Jmol Viewer 7DKZ	Wang et al. (2021). Wang J, Yu LJ, Wang W, Yan Q, Kuang T, Qin X, & Shen JR (2021). Structure of plant photosystem I-light harvesting complex I supercomplex at 2.4 Å resolution. J Integr Plant Biol 63 7:1367-1381. PubMed Id: 33788400. doi:10.1111/jipb.13095.
*C₂S₂M₂N₂-type PSII-LHCII supercomplex: Chlamydomonas reinhardtii* E Eukaryota, 3.73 Å** cryo-EM structure	6KAF	Data File Jmol Viewer 6KAF	Shen et al. (2019). Shen L, Huang Z, Chang S, Wang W, Wang J, Kuang T, Han G, Shen JR, & Zhang X (2019). Structure of a C₂S₂M₂N₂-type PSII-LHCII supercomplex from the green alga Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 116 42:21246-21255. PubMed Id: 31570614. doi:10.1073/pnas.1912462116.
*photosystem I-LHCI-LHCII super complex in state 2: Chlamydomonas reinhardtii* E Eukaryota, 3.42 Å** cryo-EM structure	7D0J	Data File Jmol Viewer 7D0J	Huang et al. (2021). Huang Z, Shen L, Wang W, Mao Z, Yi X, Kuang T, Shen JR, Zhang X, & Han G (2021). Structure of photosystem I-LHCI-LHCII from the green alga Chlamydomonas reinhardtii in State 2. Nat Commun 12 1:1100. PubMed Id: 33597543. doi:10.1038/s41467-021-21362-6.
*single-PBS-PSII-PSI-LHCs megacomplex, in situ: Porphyridium purpureum* E Eukaryota, 3.30 Å** cryo-EM structure PBS-PSII-PSI-LHCs, 3.30 Å: 7Y4L Lateral hexamer, 6.30 Å: 7Y1A In situ double-PBS-PSII-PSI-LHCs megacomplex, 7Y7A	7Y5E	Data File Jmol Viewer 7Y5E 7Y1A 7Y7A 7Y4L	You et al. (2023). You X, Zhang X, Cheng J, Xiao Y, Ma J, Sun S, Zhang X, Wang HW, & Sui SF (2023). In situ structure of the red algal phycobilisome-PSII-PSI-LHC megacomplex. Nature 616 7955:199-206. PubMed Id: 36922595. doi:10.1038/s41586-023-05831-0.
Photoprotection Proteins These proteins limit photo-oxidative damage to plants
*PsbS photoprotection protein: Spinacia oleracea* E Eukaryota, 2.35 Å** DCCD-modified, 2.70 Å: 4RI3	4RI2	Data File Jmol Viewer 4RI2 4RI3	Fan et al. (2015). Fan M, Li M, Liu Z, Cao P, Pan X, Zhang H, Zhao X, Zhang J, & Chang W (2015). Crystal structures of the PsbS protein essential for photoprotection in plants. Nat Struct Mol Biol 22 :729-735. PubMed Id: 26258636. doi:10.1038/nsmb.3068.
Photosynthetic Reaction Centers
*Photosynthetic Reaction Center: Blastochloris viridis* B Bacteria, 2.3 Å** The first high-resolution crystallographic structure of a membrane protein Former species name: Rhodopseudomonas virdis	1PRC	Data File Jmol Viewer 1PRC Reaction center. Chain H Reaction center. Chain L Reaction center. Chain M	Deisenhofer et al. (1985). Deisenhofer J, Epp O, Miki K, Huber R, & Michel H (1985). Structure of the protein subunits in the photosynthetic reaction centre of Rhodospeudomonas viridis at 3 Å resolution. Nature 318 :618-624. PubMed Id: 22439175.
*Photosynthetic Reaction Center: Blastochloris viridis* B Bacteria, 1.86 Å** Lipidic sponge-phase structure. Reveals lipids on protein surface. Low x-ray dose structure, 1.95 Å: 2WJM	2WJN	Data File Jmol Viewer 2WJN 2WJM	Wöhri et al. (2009). Wöhri AB, Wahlgren WY, Malmerberg E, Johansson LC, Neutze R, & Katona G (2009). Lipidic sponge phase crystal structure of a photosynthetic reaction center reveals lipids on the protein surface. Biochemistry 48 :9831-9838. PubMed Id: 19743880.
*Photosynthetic Reaction Center: Blastochloris viridis* B Bacteria, 3.50 Å** Structure determined by serial femtosecond crystallography	4CAS	Data File Jmol Viewer 4CAS	Johansson et al. (2013). Johansson LC, Arnlund D, Katona G, White TA, Barty A et al. (2013). Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography. Nat Commun 4 :2911. PubMed Id: 24352554. doi:10.1038/ncomms3911.
*Photosynthetic Reaction Center, microcrystals for femtosecond crystallography: Blastochloris viridis* B Bacteria, 2.80 Å** microcrystals, 2.40 Å: 5NJ4 5 ps structure, 2.80 Å: 6ZI4 5 ps structure, 2.80 Å: 6ZID 20 ps structure, 2.80 Å: 6ZI6 300 ps structure, 2.80 Å: 6ZI5 300 ps structure, 2.80 Å: 6ZI9 8 μs structure, 2.80 Å: 6ZIA	5O4C	Data File Jmol Viewer 5O4C 6ZIA 6ZID 6ZI5 5NJ4 6ZI9 6ZI6 6ZI4	Dods et al. (2021). Dods R, Båth P, Morozov D, Gagnér VA, Arnlund D, Luk HL, Kübel J, Maj M, Vallejos A, Wickstrand C, Bosman R, Beyerlein KR, Nelson G, Liang M, Milathianaki D, Robinson J, Harimoorthy R, Berntsen P, Malmerberg E, Johansson L, Andersson R, Carbajo S, Claesson E, Conrad CE, Dahl P, Hammarin G, Hunter MS, Li C, Lisova S, Royant A, Safari C, Sharma A, Williams GJ, Yefanov O, Westenhoff S, Davidsson J, DePonte DP, Boutet S, Barty A, Katona G, Groenhof G, Brändén G, & Neutze R (2021). Ultrafast structural changes within a photosynthetic reaction centre. Nature 589 7841:310-314. PubMed Id: 33268896. doi:10.1038/s41586-020-3000-7.
*Photosynthetic Reaction Center, lipidic cubic phase for femtosecond crystallography, at SACLA: Blastochloris viridis* B Bacteria, 2.40 Å** at SwissFEL, 2.25 Å: 7Q7Q	7Q7P	Data File Jmol Viewer 7Q7P 7Q7Q	Båth et al. (2022). Båth P, Banacore A, Börjesson P, Bosman R, Wickstrand C, Safari C, Dods R, Ghosh S, Dahl P, Ortolani G, Björg Ulfarsdottir T, Hammarin G, García Bonete MJ, Vallejos A, Ostojić L, Edlund P, Linse JB, Andersson R, Nango E, Owada S, Tanaka R, Tono K, Joti Y, Nureki O, Luo F, James D, Nass K, Johnson PJM, Knopp G, Ozerov D, Cirelli C, Milne C, Iwata S, Brändén G, & Neutze R (2022). Lipidic cubic phase serial femtosecond crystallography structure of a photosynthetic reaction centre. Acta Crystallogr D Struct Biol 78 :698-708. PubMed Id: 35647917. doi:10.1107/S2059798322004144.
*Photosynthetic Reaction Center: Rhodobacter sphaeroides* B Bacteria, 2.80 Å** also known as Cereibacter sphaeroides	4RCR	Data File Jmol Viewer 4RCR Reaction center. Chain H Reaction center. Chain L Reaction center. Chain M	Allen et al. (1987). Allen JP, Feher G, Yeates TO, Komiya H, & Rees DC (1987). Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits. Proc Natl Acad Sci USA 84 :6162-6166. PubMed Id: 2819866. See also: Yeates et al. (1988). Yeates TO, Komiya H, Chirino A, Rees DC, Allen JP, & Feher G (1988). Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: protein-cofactor (bacteriochlorophyll, bacteriopheophytin, and carotenoid) interactions. Proc Natl Acad Sci USA 85 :7993-7997. PubMed Id: 3186702. Allen et al. (1987). Allen JP, Feher G, Yeates TO, Komiya H, & Rees DC (1987). Structure of the reaction center from Rhodobacter sphaeroides R-26: the cofactors. Proc Natl Acad Sci USA 84 :5730-5734. PubMed Id: 3303032.
*Photosynthetic Reaction Center: Rhodobacter sphaeroides* B Bacteria, 3.1 Å**	2RCR	Data File Jmol Viewer 2RCR Reaction center. Chain H Reaction center. Chain L Reaction center. Chain M	Chang et al. (1991). Chang CH, Elkabbani O, Tiede D, Norris J, & Schiffer M. (1991). Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry 30 :5352-5360. PubMed Id: 2036404.
*Photosynthetic Reaction Center: Rhodobacter sphaeroides* B Bacteria, 3.00 Å** M202HL mutant, 3.00 Å: 1PST	1PSS	Data File Jmol Viewer 1PSS 1PST	Chirino et al. (1994). Chirino AJ, Lous EJ, Huber M, Allen JP, Schenck CC, Paddock ML, Feher G, & Rees DC (1994). Crystallographic analyses of site-directed mutants of the photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry 33 :4584-4593. PubMed Id: 8161514. doi:10.1021/bi00181a020.
*Photosynthetic Reaction Center: Rhodobacter sphaeroides (dark state)* B Bacteria, 2.2 Å** Illuminated state, 2.60 Å 1AIG	1AIJ	Data File Jmol Viewer 1AIJ 1AIG	Stowell et al. (1997). Stowell MH, McPhillips TM, Rees DC, Soltis SM, Abresch E, & Feher G (1997). Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Science 276 :812-816. PubMed Id: 9115209.
*Photosynthetic Reaction Center: Rhodobacter sphaeroides* B Bacteria, 2.35 Å** Lipidic cubic phase crystallization.	1OGV	Data File Jmol Viewer 1OGV	Katona et al. (2003). Katona K, Andréasson U, Landau EM, Andr?asson L-K, & Neutze R (2003). Lipidic cubic phase crystal structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.35 Å. J Mol Biol 331 :681-692. PubMed Id: 12899837.
*Photosynthetic Reaction Center: Rhodobacter sphaeroides* B Bacteria, 1.87 Å** pH 8 neutral state. pH 8 charge-separated state, 2.07 Å: 2J8D	2J8C	Data File Jmol Viewer 2J8C 2J8D	Koepke et al. (2007). Koepke J, Krammer EM, Klingen AR, Sebban P, Ullmann GM, & Fritzsch G. (2007). pH modulates the quinone position in the photosynthetic reaction center from Rhodobacter sphaeroides in the neutral and charge separated states. J Mol Biol 371 :396-409. PubMed Id: 17570397.
*Photosynthetic Reaction Center, Zn-substituted: Rhodobacter sphaeroides* B Bacteria, 2.85 Å** M(L214H) variant, 2.85 Å: 4N7L	4N7K	Data File Jmol Viewer 4N7K 4N7L	Saer et al. (2014). Saer RG, Pan J, Hardjasa A, Lin S, Rosell F, Mauk AG, Woodbury NW, Murphy ME, & Beatty JT (2014). Structural and kinetic properties of Rhodobacter sphaeroides photosynthetic reaction centers containing exclusively Zn-coordinated bacteriochlorophyll as bacteriochlorin cofactors. Biochim Biophys Acta 1837 :366-374. PubMed Id: 24316146. doi:10.1016/j.bbabio.2013.11.015.
*Photosynthetic Reaction Center, by in surfo* crystallization: Rhodobacter sphaeroides B Bacteria, 2.10 Å** by LCP crystallization, 2.10 Å: 6Z27 by co-crystallization with spheroidene, 2.10 Å: 6Z1J	6Z02	Data File Jmol Viewer 6Z02 6Z27 6Z1J	Selikhanov et al. (2020). Selikhanov G, Fufina T, Vasilieva L, Betzel C, & Gabdulkhakov A (2020). Novel approaches for the lipid sponge phase crystallization of the Rhodobacter sphaeroides photosynthetic reaction center. IUCrJ 7 :1084-1091. PubMed Id: 33209319. doi:10.1107/S2052252520012142.
*Photosynthetic Reaction Center, M subunit F197H mutant: Cereibacter sphaeroides* B Bacteria, 2.10 Å** by fixed-target serial synchrotron crystallography (room temperature, 26keV), 2.04 Å 7P2C	7OD5	Data File Jmol Viewer 7OD5 7P2C	Selikhanov et al. (2022). Selikhanov G, Fufina T, Guenther S, Meents A, Gabdulkhakov A, & Vasilieva L (2022). X-ray structure of the Rhodobacter sphaeroides reaction center with an M197 Phe→His substitution clarifies the properties of the mutant complex. IUCrJ 9 :261-271. PubMed Id: 35371503. doi:10.1107/S2052252521013178.
*Photosynthetic Reaction Center, L subunit I177H and M subunit F197H double mutant: Cereibacter sphaeroides* B Bacteria, 2.60 Å**	8C3F	Data File Jmol Viewer 8C3F	Fufina et al. (2023). Fufina TY, Selikhanov GK, Gabdulkhakov AG, & Vasilieva LG (2023). Properties and Crystal Structure of the Cereibacter sphaeroides Photosynthetic Reaction Center with Double Amino Acid Substitution I(L177)H + F(M197)H. Membranes (Basel) 13 2:157. PubMed Id: 36837660. doi:10.3390/membranes13020157.
*Photosynthetic Reaction Center: Thermochromatium tepidum* B Bacteria, 2.2 Å**	1EYS	Data File Jmol Viewer 1EYS reaction center chain H reaction center chain L reaction center chain M	Nogi et al. (2000). Nogi T, Fathir I, Kobayashi M, Nozawa T, & Miki K (2000). Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer. Proc Natl Acad Sci USA 97 :6031-6036. PubMed Id: 11095707.
*Homodimeric photosynthetic reaction center: Heliobacterium modesticaldum* B Bacteria, 2.2 Å** This the simplest known reaction center.	5V8K	Data File Jmol Viewer 5V8K	Gisriel et al. (2017). Gisriel C, Sarrou I, Ferlez B, Golbeck JH, Redding KE, & Fromme R (2017). Structure of a symmetric photosynthetic reaction center-photosystem. Science 357 :1021-1025. PubMed Id: 28751471. doi:10.1126/science.aan5611.
*Reaction center bound with cytochrome c (the larger form): Chloracidobacterium thermophilum* B Bacteria, 2.61 Å** cryo-EM structure bound with cytochrome c (the smaller form), 2.22 Å: 7VZR	7VZG	Data File Jmol Viewer 7VZG 7VZR	Dong et al. (2022). Dong S, Huang G, Wang C, Wang J, Sui SF, & Qin X (2022). Structure of the Acidobacteria homodimeric reaction center bound with cytochrome c. Nat Commun 13 1:7745. PubMed Id: 36517472. doi:10.1038/s41467-022-35460-6.
Light-Harvesting+Reaction Center Complexes
*LH1-RC complex, P2₁ crystal form: Thermochromatium tepidum* B Bacteria, 3.01 Å** Supersedes 3WMN. C2 crystal form. 3.01 Å: 3WMM	4V8K	Data File Jmol Viewer 4V8K 3WMM	Niwa et al. (2014). Niwa S, Yu LJ, Takeda K, Hirano Y, Kawakami T, Wang-Otomo ZY, & Miki K (2014). Structure of the LH1-RC complex from Thermochromatium tepidum at 3.0 Å. Nature 508 7495:228-232. PubMed Id: 24670637. doi:10.1038/nature13197.
*LH1-RC complex: Thermochromatium tepidum* B Bacteria, 1.9 Å**	5Y5S	Data File Jmol Viewer 5Y5S	Yu et al. (2018). Yu LJ, Suga M, Wang-Otomo ZY, & Shen JR (2018). Structure of photosynthetic LH1-RC supercomplex at 1.9 Å resolution. Nature 556 7700:209-213. PubMed Id: 29618814. doi:10.1038/s41586-018-0002-9.
*LH1-RC complex with bound electron donor HiPIP: Thermochromatium tepidum* E Eukaryota, 2.89 Å**	7C52	Data File Jmol Viewer 7C52	Kawakami et al. (2021). Kawakami T, Yu LJ, Liang T, Okazaki K, Madigan MT, Kimura Y, & Wang-Otomo ZY (2021). Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP. Nat Commun 12 1:1104. PubMed Id: 33597527. doi:10.1038/s41467-021-21397-9.
*Photosynthetic assembly RC-FMO₂: Chlorobaculum tepidum* B Bacteria, 3.08 Å** cryo-EM structure RC-FMO₁, 3.49 Å: 7UEB	7UEB	Data File Jmol Viewer 7UEB 7UEB	Puskar et al. (2022). Puskar R, Du Truong C, Swain K, Chowdhury S, Chan KY, Li S, Cheng KW, Wang TY, Poh YP, Mazor Y, Liu H, Chou TF, Nannenga BL, & Chiu PL (2022). Molecular asymmetry of a photosynthetic supercomplex from green sulfur bacteria. Nat Commun 13 1:5824. PubMed Id: 36192412. doi:10.1038/s41467-022-33505-4.
*LH1-RC complex: Blastochloris viridis* B Bacteria, 2.87 Å** cryo-EM structure	6ET5	Data File Jmol Viewer 6ET5	Qian et al. (2018). Qian P, Siebert CA, Wang P, Canniffe DP, & Hunter CN (2018). Cryo-EM structure of the Blastochloris viridis LH1-RC complex at 2.9 Å. Nature 556 7700:203-208. PubMed Id: 29618818. doi:10.1038/s41586-018-0014-5.
*RC-LH core complex: Roseiflexus castenholzii* B Bacteria, 4.1 Å** cryo-EM structure	5YQ7	Data File Jmol Viewer 5YQ7	Xin et al. (2018). Xin Y, Shi Y, Niu T, Wang Q, Niu W, Huang X, Ding W, Yang L, Blankenship RE, Xu X, & Sun F (2018). Cryo-EM structure of the RC-LH core complex from an early branching photosynthetic prokaryote. Nat Commun 9 1. PubMed Id: 29674684. doi:10.1038/s41467-018-03881-x.
*RC-LH1₁₄-W complex: Rhodopseudomonas palustris* B Bacteria, 2.65 Å** cryo-EM structure RC-LH1₁₆ complex, 2.80 Å: 6Z5R	6Z5S	Data File Jmol Viewer 6Z5S 6Z5R	Swainsbury et al. (2021). Swainsbury DJK, Qian P, Jackson PJ, Faries KM, Niedzwiedzki DM, Martin EC, Farmer DA, Malone LA, Thompson RF, Ranson NA, Canniffe DP, Dickman MJ, Holten D, Kirmaier C, Hitchcock A, & Hunter CN (2021). Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels. Sci Adv 7 3. PubMed Id: 33523887. doi:10.1126/sciadv.abe2631.
*LH1-RC super complex: Rhodospirillum rubrum* B Bacteria, 2.76 Å** cryo-EM structure	7EQD	Data File Jmol Viewer 7EQD	Tani et al. (2021). Tani K, Kanno R, Ji XC, Hall M, Yu LJ, Kimura Y, Madigan MT, Mizoguchi A, Humbel BM, & Wang-Otomo ZY (2021). Cryo-EM Structure of the Photosynthetic LH1-RC Complex from Rhodospirillum rubrum. Biochemistry 60 :2483-2491. PubMed Id: 34323477. doi:10.1021/acs.biochem.1c00360.
*LH1-RC super complex: Rhodospirillum rubrum* B Bacteria, 2.50 Å** cryo-EM structure	7OY8	Data File Jmol Viewer 7OY8	Qian et al. (2021). Qian P, Croll TI, Swainsbury DJK, Castro-Hartmann P, Moriarty NW, Sader K, & Hunter CN (2021). Cryo-EM structure of the Rhodospirillum rubrum RC-LH1 complex at 2.5 Å. Biochem J 478 17:3253-3263. PubMed Id: 34402504. doi:10.1042/BCJ20210511.
*LH1-RC super complex: Rhodobacter sphaeroides* B Bacteria, 2.94 Å** cryo-EM structure	7F0L	Data File Jmol Viewer 7F0L	Tani et al. (2021). Tani K, Nagashima KVP, Kanno R, Kawamura S, Kikuchi R, Hall M, Yu LJ, Kimura Y, Madigan MT, Mizoguchi A, Humbel BM, & Wang-Otomo ZY (2021). A previously unrecognized membrane protein in the Rhodobacter sphaeroides LH1-RC photocomplex. Nat Commun 12 1:6300. PubMed Id: 34728609. doi:10.1038/s41467-021-26561-9.
*RC-LH1-PufXY monomer complex: Rhodobacter sphaeroides* B Bacteria, 2.50 Å** cryo-EM structure	7PIL	Data File Jmol Viewer 7PIL	Qian et al. (2021). Qian P, Swainsbury DJK, Croll TI, Salisbury JH, Martin EC, Jackson PJ, Hitchcock A, Castro-Hartmann P, Sader K, & Hunter CN (2021). Cryo-EM structure of the monomeric Rhodobacter sphaeroides RC-LH1 core complex at 2.5 Å. Biochem J 478 20:3775-3790. PubMed Id: 34590677. doi:10.1042/BCJ20210631.
*LH1-RC super complex dimer: Cereibacter sphaeroides* B Bacteria, 2.75 Å** cryo-EM structure structure lacking protein-U, 2.63 Å 7VY3	7VY2	Data File Jmol Viewer 7VY2 7VY3	Tani et al. (2022). Tani K, Kanno R, Kikuchi R, Kawamura S, Nagashima KVP, Hall M, Takahashi A, Yu LJ, Kimura Y, Madigan MT, Mizoguchi A, Humbel BM, & Wang-Otomo ZY (2022). Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1-RC complex. Nat Commun 13 1:1904. PubMed Id: 35393413. doi:10.1038/s41467-022-29453-8.
*LH1-RC super complex dimer, in class 1: Cereibacter sphaeroides* B Bacteria, 2.74 Å** cryo-EM structure in class-2, 2.90 Å 7VOT PufX-KO RC-LH1, 4.20 Å 7VOY WT RC-LH1 monomer, 2.79 Å 7VNY PufY-KO RC-LH1 monomer, 2.86 Å 7VNM PufY-KO RC-LH1 dimer type-1, 3.08 Å 7VA9 PufY-KO RC-LH1 dimer type-2, 3.45 Å 7VB9	7VOR	Data File Jmol Viewer 7VOR 7VA9 7VNM 7VNY 7VB9 7VOT 7VOY	Cao et al. (2022). Cao P, Bracun L, Yamagata A, Christianson BM, Negami T, Zou B, Terada T, Canniffe DP, Shirouzu M, Li M, & Liu LN (2022). Structural basis for the assembly and quinone transport mechanisms of the dimeric photosynthetic RC-LH1 supercomplex. Nat Commun 13 1:1977. PubMed Id: 35418573. doi:10.1038/s41467-022-29563-3.
*Photosynthetic FMO-Reaction Center complex (FMO-RC): Chlorobaculum tepidum* B Bacteria, 2.50 Å** cryo-EM structure	7Z6Q	Data File Jmol Viewer 7Z6Q	Xie et al. (2023). Xie H, Lyratzakis A, Khera R, Koutantou M, Welsch S, Michel H, & Tsiotis G (2023). Cryo-EM structure of the whole photosynthetic reaction center apparatus from the green sulfur bacterium Chlorobaculum tepidum. Proc Natl Acad Sci U S A 120 5:e2216734120. PubMed Id: 36693097. doi:10.1073/pnas.2216734120.

Description of Table

The table above is initially presented in a collapsed form, and the user can expand different sections of the table, or the entire table, and bookmark different sections of the table, or a fully expanded table version of the page, using the , , , and icons on the left margin of the table section headers.

mpstruc Taxonomic Domain data are derived from the UniProt Knowledgebase, which is based on the NCBI taxonomy database. These taxa can be searched for using 'Text Search of Table', above. The following icons are used in the table, as appropriate:

A : Archaea
B : Bacteria
E : Eukaryota
Vd : Viroids
V : Viruses
O : Other
U : Unclassified

The figure at the top right of the page shows the progress of membrane protein structure determination. The figure may be used freely in seminar presentations provided that the URL and lab information on the image are not removed.

Useful Membrane Protein Structure Resources

Progress of membrane protein structure determination. See also White (2009)

Bilayer Insertion of Membrane Proteins (Structural Bioinformatics and Computational Biochemistry Unit, Oxford)

Protein Data Bank of Transmembrane Proteins (Institute of Enzymology, Budapest)

mpstruc has a new user interface to help accommodate the growing size of the protein data table. The dynamic nature of this new interface is handled by your browser, and so, your particular browser, its configuration, and your hardware configuration all may have an impact on the interface performance.

We've found that, in general, contemporary versions of Firefox, Chrome, and Safari provide the best performance. Internet Explorer performs well, but is a bit awkward when attempting to create a bookmark for this page to open with an expanded table (preparing the proper URL requires a page reload). This may also be an issue for older versions of the previously mentioned browsers.

The Opera browser, while full featured, seems to be the slowest browser of those we've tested. If this is your favorite browser, you may want to bookmark an expanded table version of the page, and avoid using the dynamic features of the table.

Of course, browser providers are providing frequent updates of their products, so these observations may be out of date by the time you read this.

By the way, you can use the icons to bookmark sections of the table. That icon in the table header allows you to create a bookmark for this page with the table fully expanded.

If you discover any issues with this interface, please let us know. We want to make this resource as useful as possible!

from the Stephen White laboratory at UC Irvine