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 ongoing 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: 20 Mar 2025 at 20:27 PDT.
Last database update: 20 Mar 2025 at 20:29 PDT

Recently Added Structures:

Apelin receptor (angiotensin II protein J receptor [APJR]), dimeric form: Homo sapiens, 3.25 Å
ATP-dependent translocase ABCB1, SapNP reconstituted: Homo sapiens, 3.80 Å
SLC11A1 natural resistance-associated macrophage protein 1 (NRAMP1) with bound Mn²⁺, towards the inward-open state: Homo sapiens, 3.70 Å
SLC11A2 divalent metal transporter 1 (DMT1) with bound Mn²⁺, occluded state: Homo sapiens, 3.60 Å
Cholinephosphotransferase-1 (CPT1) with bound diacylglycerol: Saccharomyces cerevisiae, 3.20 Å
heterodimeric IrtAB ABC transporter, inward-facing state in nanodisc: Mycolicibacterium thermoresistibile, 3.60 Å

Unique proteins in database = 1814

Coördinate files in database = 8585

Published reports of membrane protein structures in database = 3645

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.

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Links to the Protein Data Bank Site

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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) and Nastou et. al. (2020)
Cyclooxygenases
*Ram Prostaglandin H2 synthase-1 (cyclooxygenase-1 or COX-1): Ovis aries* E Eukaryota, 3.5 Å**	1PRH	Data File Jmol Viewer 1PRH 1PRH 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 1PTH 1PTH	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 1CQE 1CQE	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 1EQG 1HT5 1EQH 1HT8 1EQG 1HT5 1EQH 1HT8	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 1EBV 1EBV	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 1Q4G 1Q4G	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 2AYL 2AYL	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 3N8V 3N8Y 3N8Z 3N8W 3N8X 3N8V 3N8Y 3N8Z 3N8W 3N8X	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 7JXT 7JXT	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 6Y3C 6Y3C	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 1CX2 1CX2 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 6BL4 6BL3 6BL4 6BL3	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 4HHS 4HHR 4HHS 4HHR	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 2SBL 2SBL	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 1YGE 1YGE	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 1LNH 1LNH	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 2FNQ 2FNQ	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 3FG4 3FG4	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 1LOX 1LOX	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 3O8Y 3O8Y	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 4NRE 4NRE	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 2SQC 3SQC 2SQC 3SQC 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 1GOS 1GOS 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 1OJA 1OJC 1OJB 1OJD 1OJ9 1OJA 1OJC 1OJB 1OJD 1OJ9	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 1O5W 1O5W	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 2BXR 2BXS 2BYB 2BXR 2BXS 2BYB	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 2Z5X 2Z5Y 2Z5X 2Z5Y	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 3VV9 3VVA 3W54 3VV9 3VVA 3W54	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 1MT5 1MT5 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 5B49 5B4C 5B4B 5B4D 5B4A 5B49 5B4C 5B4B 5B4D 5B4A	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 4GGM 4GGI 4GGM 4GGI	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 4EHW 4EHX 4EHY 4EHW 4EHX 4EHY	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 4QN9 4QN9	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 2YOC 2YOC	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 6IEJ 6IEJ	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 6I8W 6I8W	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 8EMX 8EMW 8EMV 8EMX 8EMW 8EMV	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 6A2E 5YKA 5YW0 5YVZ 6A2E 5YKA 5YW0 5YVZ	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 5KN7 5KNK 5KN7 5KNK	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 7OJT 7OJT	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 6QGS 6QGO 6QGQ 6QGN 6QGS 6QGO 6QGQ 6QGN	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 6IG4 6IG2 6IG4 6IG2	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 3HYW 3HYV 3HYX 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.
*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 6MO6 6MP5 6MO6 6MP5	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 2GMH 2GMJ 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.
*mitochondrial trifunctional protein: Homo sapiens* E Eukaryota (expressed in E. coli), 3.6 Å**	6DV2	Data File Jmol Viewer 6DV2 6DV2	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 7KOE 7KOE	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 2QCU 2R4E 2R4J 2R45 2R46 2QCU 2R4E 2R4J 2R45 2R46	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 4NM9 4NMC 4NMD 4NMA 4NME 4NMB 4NMF 4NM9 4NMC 4NMD 4NMA 4NME 4NMB 4NMF	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 4G9K 4GAP 4GAV 4G9K 4GAP 4GAV	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 4G6G 4G74 4G6H 4G73 4G6G 4G74 4G6H 4G73	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 4NWZ 4NWZ	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 6BFG 6BFG	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 6L06 6L07 6L06 6L07	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 7CNW 7CNZ 7CNY 7CNX 7CNW 7CNZ 7CNY 7CNX	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 2OLV 2OLU 2OLV 2OLU	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 2OQO 2OQO	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 3VMA 3FWL 3VMA 3FWL	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 7LQ6 7LQ6	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 2XCI 2XCU 2XCI 2XCU	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 3VMT 3VMR 3VMS 3VMQ 3VMT 3VMR 3VMS 3VMQ	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 6EJI 6EJK 6EJJ 6EJI 6EJK 6EJJ	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 6RY0 6RY5 6RY2 6RY1 6RY6 6RY7 6RY0 6RY5 6RY2 6RY1 6RY6 6RY7	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 5W7L 5W7L	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 1B12 1B12	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 1KN9 1KN9	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 1T7D 1T7D	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 4WVG 4WVI 4WVH 4WVJ 4WVG 4WVI 4WVH 4WVJ	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 3BF0 3BEZ 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 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 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.
*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 4GWM 4GWN 4GWM 4GWN	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 4LXJ 5EQB 4LXJ 5EQB	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 1J79 1J79	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 1XGE 1XGE	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 1UUM 1UUO 1UUM 1UUO	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 2PRM 2PRH 2PRL 2PRM 2PRH 2PRL	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 3I65 3I6R 3I68 3I65 3I6R 3I68	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.
*Dihydroorotate Dehydrogenase with bound Inhibitor DSM679: Plasmodium falciparum* E Eukaryota (expressed in E. coli), 2.41 Å** x-ray structure with bound Inhibitor DSM681, 2.10 Å: 9DIK with bound Inhibitor DSM959, 3.10 Å: 9DIZ with bound Inhibitor DSM1153, 3.15 Å: 9DKQ with bound Inhibitor DSM1174, 3.30 Å: 9DKY with bound Inhibitor DSM1398, 2.90 Å: 9DLK with bound Inhibitor DSM1211, 3.10 Å: 9DLY	9DI6	Data File Jmol Viewer 9DI6 9DIK 9DIZ 9DKQ 9DLY 9DLK 9DKY 9DI6 9DIK 9DIZ 9DKQ 9DLY 9DLK 9DKY	Nie et al. (2024). Nie Z, Bonnert R, Tsien J, Deng X, Higgs C, El Mazouni F, Zhang X, Li R, Ho N, Feher V, Paulsen J, Shackleford DM, Katneni K, Chen G, Ng ACF, McInerney M, Wang W, Saunders J, Collins D, Yan D, Li P, Campbell M, Patil R, Ghoshal A, Mondal P, Kundu A, Chittimalla R, Mahadeva M, Kokkonda S, White J, Das R, Mukherjee P, Angulo-Barturen I, Jiménez-Díaz MB, Malmstrom R, Lawrenz M, Rodriguez-Granillo A, Rathod PK, Tomchick DR, Palmer MJ, Laleu B, Qin T, Charman SA, & Phillips MA (2024). Structure-Based Discovery and Development of Highly Potent Dihydroorotate Dehydrogenase Inhibitors for Malaria Chemoprevention. J Med Chem . PubMed Id: 39710971. doi:10.1021/acs.jmedchem.4c02394.
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 3L7I 3L7L 3L7K 3L7M 3L7J 3L7I 3L7L 3L7K 3L7M 3L7J	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 2K5U 2K5U	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 2KSQ 2KSQ	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.
*ADP-ribosylation factor (ARF1)/AP-1 complex, with HIV1-Nef and MHC-I lipopeptide, narrow membrane tubes: Homo sapiens* E Eukaryota (expressed in E.Coli), 9.60 Å** cryo-EM structure ARF1/beta AP-1 dimeric, narrow tubes, 9.30 Å: 8D4C ARF1/gamma AP-1 dimeric, narrow tubes, 9.60 Å: 8D4D wide tubes, 9.20 Å: 8D4E ARF1/beta AP-1 dimeric, wide tubes, 9.80 Å: 8D4F ARF1/gamma AP-1 dimeric, wide tubes, 11.6 Å: 8D4G gamma AP-1 centered, wide tubes, 20.0 Å: 8D9R beta AP-1 centered, wide tubes, 20.0 Å: 8D9S gamma AP-1 centered, narrow membrane, 20.0 Å: 8D9T beta AP-1 centered, narrow membrane tubes, 20.0 Å: 8D9U ARF1/gamma AP-1 homodimeric, narrow membrane tubes, 9.40 Å: 8D9V	7UX3	Data File Jmol Viewer 7UX3 8D9V 8D4E 8D4D 8D9U 8D4C 8D4G 8D9R 8D4F 8D9S 8D9T 7UX3 8D9V 8D4E 8D4D 8D9U 8D4C 8D4G 8D9R 8D4F 8D9S 8D9T	Hooy et al. (2022). Hooy RM, Iwamoto Y, Tudorica DA, Ren X, & Hurley JH (2022). Self-assembly and structure of a clathrin-independent AP-1:Arf1 tubular membrane coat. Sci Adv 8 42:eadd3914. PubMed Id: 36269825. doi:10.1126/sciadv.add3914.
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 3FSN 3FSN	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 4F3D 4F2Z 4F30 4F3A 4F3D 4F2Z 4F30 4F3A	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 4PLA 4PLA	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 7APJ 7APJ	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 3JC1 3JC1	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 6TZ9 6TZA 6TZ4 6TZ5 6TZ9 6TZA 6TZ4 6TZ5	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 7ZCG 7ZCH 7ZCG 7ZCH	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 5FD7 5FD9 5FD7 5FD9	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 5J45 5J45	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 6H7W 5W8M 6H7W 5W8M	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 6MLU 6MLU	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 7RSL 7RSL	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 6QL4 6RZV 6RZT 6RZU 6RZW 6QL4 6RZV 6RZT 6RZU 6RZW	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 6Q0X 6Q0X	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 7D6D 7D6E 7D6D 7D6E	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 8AFZ 8A1G 8ABQ 8AFZ 8A1G 8ABQ	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 6XU5 6STS 4A1H 6XUW 6XVS 6XU9 6XUA 6XVQ 4A8Z 6XW9 6XVY 6XVR 4A1Y 6XU5 6STS 4A1H 6XUW 6XVS 6XU9 6XUA 6XVQ 4A8Z 6XW9 6XVY 6XVR 4A1Y	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 6UP6 6UPN 6UP6 6UPN	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 6ZG5 6ZGA 6ZG6 6ZL0 6ZG5 6ZGA 6ZG6 6ZL0	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 7BLN 7BLP 7BLO 7BLQ 7BLR 7BLN 7BLP 7BLO 7BLQ 7BLR	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 6XJN 6XJO 6XJN 6XJO	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 7SC0 7SC0	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 7SOX 7SOX	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 6VNW 6VOA 6VNW 6VOA	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 5UV6 5UV6	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 6YRK 6RUT 6S3U 6YRK 6RUT 6S3U	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 6NZD 6NZD	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 6ULG 6ULG	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 4Y7I 4Y7I	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 6TZY 6TZZ 6TZY 6TZZ	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 6KOI 6KOJ 6KOK 6KOI 6KOJ 6KOK	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 6UXM 6UXO 6UXN 6UXP 6UXQ 6UXR 6UXM 6UXO 6UXN 6UXP 6UXQ 6UXR	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 6L8V 6L8V	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 7OFM 7OFO 7OFM 7OFO	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 1VSG 1VSG	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 2VSG 2VSG	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 5LY9 5M4T 5LY9 5M4T	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 6ELC 6ELC	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 6Z7A 6Z7E 6Z7C 6Z8H 6Z8G 6Z7B 6Z7D 6Z79 6Z7A 6Z7E 6Z7C 6Z8H 6Z8G 6Z7B 6Z7D 6Z79	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 7AHL 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 3M4D 3M3R 3M2L 3M4E 3M4D 3M3R 3M2L 3M4E 3M4D 3M3R	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 3ANZ 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 6U4P 6U3T 6U49 6U4P 6U3T 6U49 6U4P 6U3T	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 8JBQ 8JC7 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 3B07 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 4P1Y 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 1LKF 2LKF 3LKF 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 4P1X 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 4TW1 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 6RHV 6RHW 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 6U33 6U2S 6U3F 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 7P8S 7P8X 7P8U 7P93 7P8T 7P8S 7P8X 7P8U 7P93 7P8T 7P8S 7P8X 7P8U 7P93	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 6U3Y 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 4H56 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 1M3J 1M3I 1PFO 1M3J 1M3I 1PFO 1M3J 1M3I	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 3KWV 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 3J9C 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 6VRA 6WJJ 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 7KXR 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 3NSJ 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 7PAG 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 6U2L 6U2W 6U2K 6U2J 6U23 6U2L 6U2W 6U2K 6U2J 6U23 6U2L 6U2W 6U2K 6U2J	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 8A1D 8A1S 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 3O44 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 1XEZ 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 4HSC 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 3C0N 3C0O 3C0M 3C0N 3C0O 3C0M 3C0N 3C0O	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 4MKO 4MKQ 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 5FMW 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 6DLW 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 6H03 6H04 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 7NYC 7NYD 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.
*MAC precursor C5b8 in complex with CD59 (C5b8-CD59): Homo sapiens* E Eukaryota, 3.00 Å** cryo-EM structure C5b9-CD59 with 3C9, 3.30 Å: 8B0G C5b9-CD59 with 2C9, 3.30 Å: 8B0H	8B0F	Data File Jmol Viewer 8B0F 8B0G 8B0H 8B0F 8B0G 8B0H 8B0F 8B0G 8B0H	Couves et al. (2023). Couves EC, Gardner S, Voisin TB, Bickel JK, Stansfeld PJ, Tate EW, & Bubeck D (2023). Structural basis for membrane attack complex inhibition by CD59. Nat Commun 14 1:890. PubMed Id: 36797260. doi:10.1038/s41467-023-36441-z.
*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 6CXO 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 5GAQ 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 5IMW 5IMT 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 5IMY 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 5LY6 5AOF 5AOE 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 6RB9 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 6KLX 6KLW 6KLO 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 6UWR 6UWI 6UWT 6UWO 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 7VNJ 7YVQ 7YVS 7VNN 7VNJ 7YVQ 7YVS 7VNN 7VNJ 7YVQ 7YVS	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 6X1K 6X9Z 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 2POR 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 1PRN 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 7PRN 2PRN 3PRN 8PRN 5PRN 1BH3 6PRN 7PRN 2PRN 3PRN 8PRN 5PRN 1BH3 6PRN 7PRN 2PRN 3PRN 8PRN 5PRN	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 1H6S 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 1OSM 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 6RD3 6RCK 6RCP 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 8PYZ 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 1E54 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 2FGR 2FGQ 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 2OMF 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 1MPF 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 1OPF 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 1GFO 1GFP 1GFQ 1GFN 1GFM 1GFO 1GFP 1GFQ 1GFN 1GFM 1GFO 1GFP 1GFQ 1GFN	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 1BT9 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 1HXX 1HXT 1HXU 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 2ZFG 2ZLD 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 3FYX 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 3O0E 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 3HW9 3HWB 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 3K19 3K1B 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 3POU 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 4D5U 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 6WTZ 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 7NSU 7NST 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 5O78 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 3NSG 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 6ENE 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 5O77 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 2J1N 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 2XG6 2XE2 2XE5 2XE3 2XE1 2XG6 2XE2 2XE5 2XE3 2XE1 2XG6 2XE2 2XE5 2XE3	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 7JZ3 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.
*OmpC-MlaA: Escherichia coli* B Bacteria (expressed in E.coli), 2.93 Å** cryo-EM structure OmpC-MlaA-MlaC, 3.25 Å: 8I8X	8I8R	Data File Jmol Viewer 8I8R 8I8X 8I8R 8I8X 8I8R 8I8X	Yeow et al. (2023). Yeow J, Luo M, & Chng SS (2023). Molecular mechanism of phospholipid transport at the bacterial outer membrane interface. Nat Commun 14 1:8285. PubMed Id: 38092770. doi:10.1038/s41467-023-44144-8.
*OmpK36 (OmpC): Klebsiella pneumoniae* B Bacteria (expressed in E. coli), 1.65 Å**	5O79	Data File Jmol Viewer 5O79 5O79 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 5O9C 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 5FVN 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 2F1C 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 2IWV 2IWW 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 2X9K 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 2JQY 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 5MWV 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 6OQH 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 6EHE 6EHD 6EHF 5OYK 6EHE 6EHD 6EHF 5OYK 6EHE 6EHD 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 5ONU 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 6EHB 6EHC 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 1PHO 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 2MPR 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 1MAL 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 1MPN 1MPO 1MPM 1MPN 1MPO 1MPM 1MPN 1MPO	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 1AF6 1MPQ 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 1A0T 1A0S 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 1UUN 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 4GEY 4GF4 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 4RJW 4RJX 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 2O4V 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 3VZW 3A2S 3VZU 3VZT 3VZW 3A2S 3VZU 3VZT 3VZW 3A2S 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 3WI4 3WI5 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 7DE8 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 4AUI 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 4FQE 4PR7 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 4D5D 4D51 4D5B 4V3G 4V3H 4D5D 4D51 4D5B 4V3G 4V3H 4D5D 4D51 4D5B	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 4RL8 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 2N6L 2N6P 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 5LDV 5LDT 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 5NXU 5NXR 5NXN 4D65 5N9H 5N9I 4D64 5NXU 5NXR 5NXN 4D65 5N9H 5N9I 4D64 5NXU 5NXR 5NXN 4D65 5N9H 5N9I	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 5MDR 5MDQ 5MDS 5MDO 5MDP 5MDR 5MDQ 5MDS 5MDO 5MDP 5MDR 5MDQ 5MDS	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 5O67 5O68 5O65 5O67 5O68 5O65 5O67 5O68	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 6EUS 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 6R2Q 6QYC 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 2ODJ 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 3SY7 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 3SY9 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 3SYB 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 2QTK 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 3SYS 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 3SZD 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 3SZV 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 3T0S 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 3T20 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 3T24 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 3JTY 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 5DL5 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 5DL6 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 5DL7 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 5DL8 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 1EK9 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 1TQQ 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 2VDE 2VDD 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 6WXH 6WXI 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 7NG9 7NNA 7NG8 7NG9 7NNA 7NG8 7NG9 7NNA	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 4MT4 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 1YC9 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 1WP1 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 3D5K 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 5AZO 5AZP 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 5AZS 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 5BUN 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 3PIK 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 4K34 4K7K 4K7R 4K34 4K7K 4K7R 4K34 4K7K	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 1NQF 1NQH 1NQG 1NQE 1NQF 1NQH 1NQG 1NQE 1NQF 1NQH 1NQG 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 1UJW 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 2GUF 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 2GSK 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 2YSU 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 3M8B 3M8D 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 2HDI 2HDF 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 1BXW 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 1QJP 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 1G90 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 2GE4 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 2JMM 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 2K0L 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 1I78 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 2X55 2X56 2X4M 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 2F1V 2F1T 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 2MHL 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 6QWR 6QAM 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 4RL9 4RLB 4FUV 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 4RLC 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 2X27 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 2LHF 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 1QJ8 1QJ9 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 1ORM 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 1Q9F 1Q9G 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 2M06 2M07 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 3QRA 3QRC 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 2N2M 2N2L 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 5VJ8 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 3DZM 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 1QD5 1QD6 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 1FW2 1FW3 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 1ILZ 1ILD 1IM0 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 1K24 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 2VDF 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 1P4T 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 2WJR 2WJQ 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 2ERV 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 3FID 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 1MM4 1MM5 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 1THQ 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 3GP6 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 1T16 1T1L 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 2R4L 2R88 2R4P 2R4N 2R4O 3DWN 2R4L 2R88 2R4P 2R4N 2R4O 3DWN 2R4L 2R88 2R4P 2R4N 2R4O	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 2R89 3PGU 3PGS 3PF1 3PGR 2R89 3PGU 3PGS 3PF1 3PGR 2R89 3PGU 3PGS 3PF1	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 3DWO 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 6KZ3 6KZ4 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 3EFM 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 3BS0 3BRZ 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 3BRY 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 1TLZ 1TLW 1TLY 1TLZ 1TLW 1TLY 1TLZ 1TLW	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 1BY3 1BY5 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 2FCP 1FCP 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 1QFG 1QFF 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 1QKC 1QJQ 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 1FI1 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 2GRX 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 4CU4 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 8A60 8A8C 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 4EPI 4EPF 4EPA 4EXM 4EPI 4EPF 4EPA 4EXM 4EPI 4EPF	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 1FEP 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 6BPN 6BPM 6BPO 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 1KMO 1KMP 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 1PNZ 1PO0 1PO3 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 2D1U 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 5FOK 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 5NEC 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 5FP1 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 5FP2 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 5FR8 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 3DDR 3CSN 3CSL 3DDR 3CSN 3CSL 3DDR 3CSN	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 3FHH 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 1XKW 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 3QLB 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 1XKH 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 2O5P 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 2IAH 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 3RBH 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 4B61 4AZL 4AFK 4B61 4AZL 4AFK 4B61 4AZL	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 4XNL 4XNK 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 8PZ4 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 8RQP 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 7ULA 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 2VQI 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 3FIP 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 3RFZ 3OHN 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 4J3O 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 6E14 6E15 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 7LHI 7LHH 7LHG 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 3SKP 3V89 3V83 3V8U 3V8X 3SKP 3V89 3V83 3V8U 3V8X 3SKP 3V89 3V83 3V8U	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 2YNK 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 2MLH 2MAF 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.
Opa₆₀ for receptor-mediated engulfment, proton-detected magic-angle spinning nuclear magnetic resonance (MAS NMR) used: Neisseria gonorrhoeae B Bacteria (expressed in E. coli), NMR structure	8QWQ	Data File Jmol Viewer 8QWQ 8QWQ 8QWQ	Forster et al. (2024). Forster MC, Tekwani Movellan K, Najbauer EE, Becker S, & Andreas LB (2024). Magic-angle spinning NMR structure of Opa60 in lipid bilayers. J Struct Biol X 9 :100098. PubMed Id: 39010882. doi:10.1016/j.yjsbx.2024.100098.
*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 4UV3 4UV2 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 4Q79 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 6LQJ 7BRM 6LQH 6LQJ 7BRM 6LQH 6LQJ 7BRM	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 6L7A 6L7C 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 6SI7 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 4ZGV 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 6GIE 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 4B7O 4AIQ 4AIP 4B7O 4AIQ 4AIP 4B7O 4AIQ	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 6E4V 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 6V81 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 5NC4 5OUT 6Q5E 6I2J 5NR2 6R1F 5MZS 5M9B 5NC4 5OUT 6Q5E 6I2J 5NR2 6R1F 5MZS 5M9B 5NC4 5OUT 6Q5E 6I2J 5NR2 6R1F 5MZS	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 7OBW 6Y47 6Z33 6YY5 6Z2N 5NC3 7OBW 6Y47 6Z33 6YY5 6Z2N 5NC3 7OBW 6Y47 6Z33 6YY5 6Z2N	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 6TZK 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.
*BcsC cellulose synthase outer membrane channel: Escherichia coli* B Bacteria, 3.40 Å** cryo-EM structure with bound cellotetraose, 3.80 Å: 9B8H	9B8A	Data File Jmol Viewer 9B8A 9B8H 9B8A 9B8H 9B8A 9B8H	Verma et al. (2024). Verma P, Ho R, Chambers SA, Cegelski L, & Zimmer J (2024). Insights into phosphoethanolamine cellulose synthesis and secretion across the Gram-negative cell envelope. Nat Commun 15 1:7798. PubMed Id: 39242554. doi:10.1038/s41467-024-51838-0.
*ZnuD zinc transporter: Neisseria meningitidis* B Bacteria (expressed in E. coli), 3.20 Å**	4RDT	Data File Jmol Viewer 4RDT 4RDT 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 4MT0 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 6V0I 6VCI 6V0D 6V0F 6V0J 6V0E 6V0G 6V0H 6V0C 6V0I 6VCI 6V0D 6V0F 6V0J 6V0E 6V0G 6V0H 6V0C 6V0I 6VCI 6V0D 6V0F 6V0J 6V0E 6V0G 6V0H	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 7PGE 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 porin OmpW: Klebsiella pneumoniae* B Bacteria (expressed in E. coli), 3.20 Å** X-ray structure	8QXP	Data File Jmol Viewer 8QXP 8QXP 8QXP	Seddon et al. (2024). Seddon C, Frankel G, & Beis K (2024). Structure of the outer membrane porin OmpW from the pervasive pathogen Klebsiella pneumoniae. Acta Crystallogr F Struct Biol Commun 80 :22-27. PubMed Id: 38206593. doi:10.1107/S2053230X23010579.
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 1UYN 1UYO 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 2GR8 2GR7 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 2QOM 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 3SLO 3SLT 3SLJ 3SLO 3SLT 3SLJ 3SLO 3SLT	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 3SZE 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 4MEE 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 3AEH 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 1WXR 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 3KVN 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 3ML3 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 4E1S 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 1F02 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 4E1T 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 1CWV 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 2LME 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 4C00 4BZA 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 4RAP 4RB4 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 3QQ2 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 6WIL 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 6WIM 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 7O23 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 4QKY 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 3NJT 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 2X8X 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 3MC9 3MC8 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 4N75 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 7P1C 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 7R1V 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 4K3B 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 4K3C 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 2QCZ 2QDF 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 3EFC 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 2V9H 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 3OG5 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 3Q6B 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 4C4V 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 6FSU 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 6QGX 6QGY 6QGW 6QGX 6QGY 6QGW 6QGX 6QGY	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 3PRW 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 3P1L 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 3Q7M 3Q7O 3Q7N 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 2YH3 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 3Q54 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 4XGA 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 2YH6 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 2YH5 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 2LAF 2LAE 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 3SNS 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 3QKY 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 2YHC 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 3Q5M 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 5WAQ 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 2KM7 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 2YH9 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 5WAM 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 3TGO 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 5EKQ 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 6AIT 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 5EFR 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 5D0O 5D0Q 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 5AYW 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 5LGO 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 6V05 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 6T1W 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 6SN5 6SN2 6SN8 6SN4 6SOB 6SOC 6SN7 6SOG 6SOJ 6SN3 6SN9 6SOH 6SMX 6SN5 6SN2 6SN8 6SN4 6SOB 6SOC 6SN7 6SOG 6SOJ 6SN3 6SN9 6SOH 6SMX 6SN5 6SN2 6SN8 6SN4 6SOB 6SOC 6SN7 6SOG 6SOJ 6SN3 6SN9 6SOH	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 7NCS 7NBX 7ND0 7BNQ 7NCS 7NBX 7ND0 7BNQ 7NCS 7NBX 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 6LYQ 6LYR 6LYU 6LYS 6LYQ 6LYR 6LYU 6LYS 6LYQ 6LYR 6LYU	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 7NRF 7NRE 7NRI 7NRF 7NRE 7NRI 7NRF 7NRE	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 7RI5 7RI8 7RI4 7RI6 7RI9 7RJ5 7RI7 7RI5 7RI8 7RI4 7RI6 7RI9 7RJ5 7RI7 7RI5 7RI8 7RI4 7RI6 7RI9 7RJ5	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 7TT5 7TT4 7TSZ 7TT6 7TT7 7TT2 7TT1 7TT0 7TT3 7TTC 7TT5 7TT4 7TSZ 7TT6 7TT7 7TT2 7TT1 7TT0 7TT3 7TTC 7TT5 7TT4 7TSZ 7TT6 7TT7 7TT2 7TT1 7TT0 7TT3	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 8ADG 8ADi 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 8BWC 8BVQ 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 8BNZ 7YE6 8BO2 7YE4 8BNZ 7YE6 8BO2 7YE4 8BNZ 7YE6 8BO2	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 7R1W 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 2K4T 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 2JK4 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 6TIQ 6TIQ 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 7QI2 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 3EMN 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 4C69 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 7KUH 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 4BUM 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 5O8O 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 8B4I 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 6JNF 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 6UCU 6UCV 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 7E4H 7E4I 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 7CK6 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 7CP9 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 7VD2 7VDD 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 6WUJ 6WUL 6WUN 6WUM 6WUT 6WUH 6WUJ 6WUL 6WUN 6WUM 6WUT 6WUH 6WUJ 6WUL 6WUN 6WUM 6WUT	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 4N4R 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 4Q35 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 4NHR 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 4Y25 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 5IXM 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 5IV8 5IV9 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 5IVA 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 7OMM 7OMT 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 5T3R 5QF7 5FQ4 5QF3 5LX8 5T4Y 5FQ6 5FQ8 5T3R 5QF7 5FQ4 5QF3 5LX8 5T4Y 5FQ6 5FQ8 5T3R 5QF7 5FQ4 5QF3 5LX8 5T4Y 5FQ6	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 6ZM1 6Z9A 6ZLU 6ZLT 6Z8I 6ZAZ 6ZM1 6Z9A 6ZLU 6ZLT 6Z8I 6ZAZ 6ZM1 6Z9A 6ZLU 6ZLT 6Z8I	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.
*SusCD fructo-oligosaccharide (FOS) transporter with bound FOS DP 8-12: Bacteroides thetaiotaomicron* B Bacteria, 2.90 Å** cryo-EM structure with bound FOS DP15-25, inactive state, 2.70 Å: 8AA3 BT1760-1761 complex with bound FOS DP 8-12, 3.20 Å: 8AA0 BT1760-1761 complex with bound FOS DP 15-25, inactive state, 3.10 Å: 8AA2 SusC-BT1760-1761 complex, 3.50 Å: 8A9Y SusC only, 3.10 Å: 8AA4	8AA1	Data File Jmol Viewer 8AA1 8AA3 8A9Y 8AA2 8AA4 8AA0 8AA1 8AA3 8A9Y 8AA2 8AA4 8AA0 8AA1 8AA3 8A9Y 8AA2 8AA4 8AA0	White et al. (2023). White JBR, Silale A, Feasey M, Heunis T, Zhu Y, Zheng H, Gajbhiye A, Firbank S, Baslé A, Trost M, Bolam DN, van den Berg B, & Ranson NA (2023). Outer membrane utilisomes mediate glycan uptake in gut Bacteroidetes. Nature 618 7965:583-589. PubMed Id: 37286596. doi:10.1038/s41586-023-06146-w.
*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 6SLN 6SLI 6SLJ 6SLN 6SLI 6SLJ 6SLN 6SLI	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 5WQ7 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 5WQ8 5WQ9 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 6HCG 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 7OFH 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 5TCP 5TCQ 5TCR 5TCP 5TCQ 5TCR 5TCP 5TCQ	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 6SD2 6TRE 6SD4 6SD5 6SD1 6SD3 6SCN 6SD2 6TRE 6SD4 6SD5 6SD1 6SD3 6SCN 6SD2 6TRE 6SD4 6SD5 6SD1 6SD3	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 6XFK 6XFL 6XFJ 6XFK 6XFL 6XFJ 6XFK 6XFL	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 7AH9 7AHI 7AGX 7AH9 7AHI 7AGX 7AH9 7AHI	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 7FEB 7FEC 7FED 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 6F2D 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 6DV3 6DV6 6DWB 6DUZ 6DV3 6DV6 6DWB 6DUZ 6DV3 6DV6 6DWB	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 6PEE 6Q16 6PEM 6PEP 6Q14 6Q15 6PEE 6Q16 6PEM 6PEP 6Q14 6Q15 6PEE 6Q16 6PEM 6PEP 6Q14	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 6RWK 6RWY 6RWX 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 8AXL 8AXN 8AXK 8AXL 8AXN 8AXK 8AXL 8AXN	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 6S3S 6S3L 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 6S3R 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 7KHW 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 7K7K 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 7QIJ 7QIH 7QII 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 3JQO 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 6ODI 6OEH 6OEF 6OEG 6OEE 6ODJ 6ODI 6OEH 6OEF 6OEG 6OEE 6ODJ 6ODI 6OEH 6OEF 6OEG 6OEE	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 8DOL 6JHO 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 6W6M 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 6X62 6X66 6X64 6X65 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 6VE2 6VE3 6VE4 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 7OKN 7OKO 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 7SPC 7SPK 7SPJ 7SPI 7SPB 7SPC 7SPK 7SPJ 7SPI 7SPB 7SPC 7SPK 7SPJ 7SPI	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 6N38 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 6SK0 6SKI 6SJL 6SK0 6SKI 6SJL 6SK0 6SKI	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 8GI1 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 6H3I 6H3J 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 5WC3 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 6CB8 5B5R 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 6VFE 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 8ET2 8EFP 8ET1 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 8GTN 8GTJ 8GTK 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 2WCD 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 6H2E 6H2D 6GRK 6H2F 6R1J 6GRJ 6H2E 6H2D 6GRK 6H2F 6R1J 6GRJ 6H2E 6H2D 6GRK 6H2F 6R1J	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 7A27 6ZZH 6ZZ5 7A26 7A0G 7A27 6ZZH 6ZZ5 7A26 7A0G 7A27 6ZZH 6ZZ5 7A26	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 5KUD 5KUC 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 3LIM 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 4TSO 3VWI 4TSP 4TSQ 3W9P 4TSL 4TSN 4TSY 4TSO 3VWI 4TSP 4TSQ 3W9P 4TSL 4TSN 4TSY 4TSO 3VWI 4TSP 4TSQ 3W9P 4TSL 4TSN	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 2YMK 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 4O9Y 4O9X 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 5LKH 5LKI 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 6SUF 6SUE 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 4CDB 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 6GY6 6GY7 6GY8 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 6NYG 6NYN 6NYJ 6NYM 6NYL 6NYF 6NYG 6NYN 6NYJ 6NYM 6NYL 6NYF 6NYG 6NYN 6NYJ 6NYM 6NYL	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 6ODY 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 7KIY 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 6YRF 7NTX 6YRG 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 4P6L 4P6K 2MUZ 4P6J 4P6L 4P6K 2MUZ 4P6J 4P6L 4P6K 2MUZ	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 6B87 6B85 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 1ZLL 6MQ2 6MCT 6MPW 6MQU 1ZLL 6MQ2 6MCT 6MPW 6MQU 1ZLL 6MQ2 6MCT 6MPW 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 6TJ1 6O35 6TMS 6M6Z 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 5G1J 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 6LEO 6LEP 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 7P5C 7PJ5 7P5M 7P54 7P5C 7PJ5 7P5M 7P54 7P5C 7PJ5 7P5M	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 7RTW 7RTV 7RTU 7RTT 7RTW 7RTV 7RTU 7RTT 7RTW 7RTV 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 7N0K 7N0L 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 7N7P 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 7F3T 7F3U 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 7F6V 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 7MYZ 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 7FH1 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 6WVD 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 7T6D 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 7WJT 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.
*TMEM87A (or Elkin1, also known as Golgi-pH-regulating cation channel (GolpHCat)): Homo sapiens* E Eukaryota (expressed in sf9 cells), 4.74 Å** cryo-EM structure	8CTJ	Data File Jmol Viewer 8CTJ 8CTJ 8CTJ	Hoel et al. (2022). Hoel CM, Zhang L, & Brohawn SG (2022). Structure of the GOLD-domain seven-transmembrane helix protein family member TMEM87A. Elife 11 :e81704. PubMed Id: 36373655. doi:10.7554/eLife.81704.
*TMEM87A (or Elkin1, also known as Golgi-pH-regulating cation channel (GolpHCat)), wild-type: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.10 Å** cryo-EM structure wild-type, with bound gluconate, 3.60 Å: 8HTT A308M mutant, 3.10 Å: 8KB4	8HSI	Data File Jmol Viewer 8HSI 8HTT 8KB4 8HSI 8HTT 8KB4 8HSI 8HTT 8KB4	Kang et al. (2024). Kang H, Han AR, Zhang A, Jeong H, Koh W, Lee JM, Lee H, Jo HY, Maria-Solano MA, Bhalla M, Kwon J, Roh WS, Yang J, An HJ, Choi S, Kim HM, & Lee CJ (2024). GolpHCat (TMEM87A), a unique voltage-dependent cation channel in Golgi apparatus, contributes to Golgi-pH maintenance and hippocampus-dependent memory. Nat Commun 15 1:5830. PubMed Id: 38992057. doi:10.1038/s41467-024-49297-8.
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 5UW2 5UWB 5UWA 5UVN 5UW8 5UW2 5UWB 5UWA 5UVN 5UW8 5UW2 5UWB 5UWA 5UVN	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 6XGY 6XGZ 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 6XBD 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 6ZY4 6ZY3 6ZY9 6ZY2 6ZY4 6ZY3 6ZY9 6ZY2 6ZY4 6ZY3 6ZY9	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 7CH0 7CGN 7CGE 7CH0 7CGN 7CGE 7CH0 7CGN	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 7D09 7D08 7D06 7D0A 7D09 7D08 7D06 7D0A 7D09 7D08	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 7CH8 7CH7 7CHA 7CH6 7CH9 7CH8 7CH7 7CHA 7CH6 7CH9 7CH8 7CH7 7CHA 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 8FEF 8FEE 8FED 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 2J58 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 2VQG 2VQH 2VQK 2VQL 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 5NUQ 5NUP 5NUR 5NUO 5NUQ 5NUP 5NUR 5NUO 5NUQ 5NUP 5NUR	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.
*KpsMT-KspE translocon complex for capsular polysaccharides, apo form, state 1: Caldimonas thermodepolymerans* B Bacteria (expressed in E. coli), 3.10 Å** cryo-EM structure KpsMT(E151Q mutant)-KpsE complex, with bound ATP, 3.10 Å: 8TSH with bound ADP and AlF4^-, 4.40 Å: 8TSI KpsMT-KspE-KspE complex, apo form, state 2, 3.40 Å: 8TSL KpsMT-KspE-KspE complex, in glycolipid, state 1, 3.40 Å: 8TUN KpsMT-KspE-KspE complex, in glycolipid, state 2, 3.40 Å: 8TT3	8TSW	Data File Jmol Viewer 8TSW 8TSI 8TSL 8TT3 8TUN 8TSH 8TSW 8TSI 8TSL 8TT3 8TUN 8TSH 8TSW 8TSI 8TSL 8TT3 8TUN 8TSH	Kuklewicz & Zimmer (2024). Kuklewicz J, & Zimmer J (2024). Molecular insights into capsular polysaccharide secretion. Nature 628 8009:901-909. PubMed Id: 38570679. doi:10.1038/s41586-024-07248-9.
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 2MMU 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 8HHF 8HHH 8HHG 8HHF 8HHH 8HHG 8HHF 8HHH	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.
*FtsE-FtsX complex: Mycobacterium tuberculosis* B Bacteria (expressed in expressed in E. coli), 3.90 Å** cryo-EM structure FtsE-FtsX complex belongs to the type VII subfamily of ABC transporters. with bound RipC, 3.90 Å: 8IDC with bound RipC and ATP, complex type 1, 4.00 Å: 8IDD with bound RipC and ADP, complex type 2, 5.70 Å: 8IGQ FtsE(E165Q)-FtsX with bound RipC and ATP, 3.90 Å: 8JIA	8IDB	Data File Jmol Viewer 8IDB 8IGQ 8IDC 8IDD 8JIA 8IDB 8IGQ 8IDC 8IDD 8JIA 8IDB 8IGQ 8IDC 8IDD 8JIA	Li et al. (2023). Li J, Xu X, Shi J, Hermoso JA, Sham LT, & Luo M (2023). Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis. Nat Commun 14 1:7999. PubMed Id: 38044344. doi:10.1038/s41467-023-43770-6.
*FtsE-FtsX complex: Pseudomonas aeruginosa* B Bacteria (expressed in expressed in E. coli), 4.23 Å** cryo-EM structure with bound metallopeptidase EnvC and ATP, 3.80 Å: 8I6O FtsE(E165Q)-FtsX complex with bound ATP, 4.00 Å: 8I6R FtsE(E165Q)-FtsX complex with bound EnvC and ATP, 4.40 Å: 8I6S	8I6Q	Data File Jmol Viewer 8I6Q 8I6R 8I6O 8I6S 8I6Q 8I6R 8I6O 8I6S 8I6Q 8I6R 8I6O 8I6S	Xu et al. (2023). Xu X, Li J, Chua WZ, Pages MA, Shi J, Hermoso JA, Bernhardt T, Sham LT, & Luo M (2023). Mechanistic insights into the regulation of cell wall hydrolysis by FtsEX and EnvC at the bacterial division site. Proc Natl Acad Sci U S A 120 21:e2301897120. PubMed Id: 37186861. doi:10.1073/pnas.2301897120.
*FtsE-FtsX complex: Vibrio cholerae* B Bacteria (expressed in expressed in E. coli), 3.51 Å** cryo-EM structure with bound EnvC (short form) and Mg-ADP, 3.55 Å: 8TZK with bound EnvC (long form) and Mg-ADP, 3.55 Å: 8TZL	8TZJ	Data File Jmol Viewer 8TZJ 8TZL 8TZK 8TZJ 8TZL 8TZK 8TZJ 8TZL 8TZK	Hao et al. (2024). Hao A, Suo Y, & Lee SY (2024). Structural insights into the FtsEX-EnvC complex regulation on septal peptidoglycan hydrolysis in Vibrio cholerae. Structure 32 2:188-199.e5. PubMed Id: 38070498. doi:10.1016/j.str.2023.11.007.
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 6S1K 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 7NB6 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 7OT9 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 6WVG 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 5TCX 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 7JIC 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 6K4J 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.
*Perioherin-2 (PRPH2)-Rod out segment membrane protein 1 (ROM1) hetero-dimer: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.70 Å** cryo-EM structure	7ZW1	Data File Jmol Viewer 7ZW1 7ZW1 7ZW1	El Mazouni & Gros (2022). El Mazouni D, & Gros P (2022). Cryo-EM structures of peripherin-2 and ROM1 suggest multiple roles in photoreceptor membrane morphogenesis. Sci Adv 8 45:eadd3677. PubMed Id: 36351012. doi:10.1126/sciadv.add3677.
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 6VJA 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 1YGM 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 2CPB 2CPS 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 1PJF 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 2KSJ 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 1MZT 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 1FDM 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 5JYN 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 1AFO 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 2KPF 2KPE 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 5EH4 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 6HKG 6HJQ 6HJN 6HJR 6HKG 6HJQ 6HJN 6HJR 6HKG 6HJQ 6HJN	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 6Y5H 6Y5L 6Y5I 6Y5K 6Y5J 6Y5G 6Y5H 6Y5L 6Y5I 6Y5K 6Y5J 6Y5G 6Y5H 6Y5L 6Y5I 6Y5K 6Y5J	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 5KTF 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 2MIC 2MJO 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 7K7A 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 7RFP 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 7WSO 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 7XT6 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 7XQ8 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 2MFR 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 7YQ5 8GUY 7QY4 7YQ3 7YQ6 7YQ5 8GUY 7QY4 7YQ3 7YQ6 7YQ5 8GUY 7QY4 7YQ3	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 2JWA 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 2N2A 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 2KS1 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 5LV6 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 2L9U 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 2LCX 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 2K1L 2K1K 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 2K9Y 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 2LZL 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 2M59 2MET 2MEU 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 2KNC 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 7KN0 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 8T2V 8T2U 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 8TCG 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 8TCF 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 3WXV 3WXW 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 5LX9 5LWY 5LXG 5LXA 5LX9 5LWY 5LXG 5LXA 5LX9 5LWY	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 6KRZ 6KS0 6KS1 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 6YXD 6YXG 6YXF 6YX9 6YXD 6YXG 6YXF 6YX9 6YXD 6YXG 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 6HG9 6HGU 6HGO 6HGA 6HG4 6HG9 6HGU 6HGO 6HGA 6HG4 6HG9 6HGU 6HGO 6HGA	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 7UWN 7UWK 7UWM 7UWJ 7UWL 7UWN 7UWK 7UWM 7UWJ 7UWL 7UWN 7UWK 7UWM	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 8DHA 8DH9 8DH8 8DHA 8DH9 8DH8 8DHA 8DH9	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.
*IL-7R intramembrane subunit in complex with ILR gamma chain: Mus musculus,* E Eukaryota (expressed in E. coli), NMR structure**	8DDC	Data File Jmol Viewer 8DDC 8DDC 8DDC	Cai et al. (2023). Cai T, Lenoir Capello R, Pi X, Wu H, & Chou JJ (2023). Structural basis of γ chain family receptor sharing at the membrane level. Science 381 6657:569-576. PubMed Id: 37535730. doi:10.1126/science.add1219.
*IL-9R intramembrane subunit in complex with ILR gamma chain: Mus musculus* E Eukaryota (expressed in E. coli), NMR structure**	8DDD	Data File Jmol Viewer 8DDD 8DDD 8DDD	Cai et al. (2023). Cai T, Lenoir Capello R, Pi X, Wu H, & Chou JJ (2023). Structural basis of γ chain family receptor sharing at the membrane level. Science 381 6657:569-576. PubMed Id: 37535730. doi:10.1126/science.add1219.
Toll-Like Receptors (TLR) and TLR Signalling Regulators
*Toll-like receptor TLR2, transmembrane and cytoplasmic juxtamembrane regions: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure**	8AR0	Data File Jmol Viewer 8AR0 8AR0 8AR0	Kornilov et al. (2023). Kornilov FD, Shabalkina AV, Lin C, Volynsky PE, Kot EF, Kayushin AL, Lushpa VA, Goncharuk MV, Arseniev AS, Goncharuk SA, Wang X, & Mineev KS (2023). The architecture of transmembrane and cytoplasmic juxtamembrane regions of Toll-like receptors. Nat Commun 14 1:1503. PubMed Id: 36932058. doi:10.1038/s41467-023-37042-6.
*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 7C76 7CYN 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, transmembrane and cytoplasmic juxtamembrane regions: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure**	8AT1	Data File Jmol Viewer 8AT1 8AT1 8AT1	Kornilov et al. (2023). Kornilov FD, Shabalkina AV, Lin C, Volynsky PE, Kot EF, Kayushin AL, Lushpa VA, Goncharuk MV, Arseniev AS, Goncharuk SA, Wang X, & Mineev KS (2023). The architecture of transmembrane and cytoplasmic juxtamembrane regions of Toll-like receptors. Nat Commun 14 1:1503. PubMed Id: 36932058. doi:10.1038/s41467-023-37042-6.
*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 7C77 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.
*Toll-like receptor TLR5, transmembrane and cytoplasmic juxtamembrane regions: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure**	8AR2	Data File Jmol Viewer 8AR2 8AR2 8AR2	Kornilov et al. (2023). Kornilov FD, Shabalkina AV, Lin C, Volynsky PE, Kot EF, Kayushin AL, Lushpa VA, Goncharuk MV, Arseniev AS, Goncharuk SA, Wang X, & Mineev KS (2023). The architecture of transmembrane and cytoplasmic juxtamembrane regions of Toll-like receptors. Nat Commun 14 1:1503. PubMed Id: 36932058. doi:10.1038/s41467-023-37042-6.
*Toll-like receptor TLR9, transmembrane and cytoplasmic juxtamembrane regions: Homo sapiens* E Eukaryota (expressed in E. coli), NMR structure**	8AR3	Data File Jmol Viewer 8AR3 8AR3 8AR3	Kornilov et al. (2023). Kornilov FD, Shabalkina AV, Lin C, Volynsky PE, Kot EF, Kayushin AL, Lushpa VA, Goncharuk MV, Arseniev AS, Goncharuk SA, Wang X, & Mineev KS (2023). The architecture of transmembrane and cytoplasmic juxtamembrane regions of Toll-like receptors. Nat Commun 14 1:1503. PubMed Id: 36932058. doi:10.1038/s41467-023-37042-6.
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 5HK1 5HK2 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 7W2D 7W2G 7W2C 7W2E 7W2F 7W2H 7W2B 7W2D 7W2G 7W2C 7W2E 7W2F 7W2H 7W2B 7W2D 7W2G 7W2C 7W2E 7W2F 7W2H	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-1 (σ1) receptor complexed with progesterone by co-crstayllization, I432 space group: Xenopus laevis* E Eukaryota (expressed in Komagataella pastoris), 2.15 Å** X-ray structure by soaking, 2.68 Å: 8W4C in the absence of known ligands, 2.17 Å: 8W4D complexed with DHEAS by soaking, 2.50 Å: 8WWB complexed with DHEAS by soaking, C2 space group. 3.09 Å: 8WUE side-open, C2 space group, 2.81 Å: 8W4E side-open all protomers, C2 space group, 3.12 Å: 8YBB	8W4B	Data File Jmol Viewer 8W4B 8W4E 8W4C 8W4D 8WUE 8WWB 8YBB 8W4B 8W4E 8W4C 8W4D 8WUE 8WWB 8YBB 8W4B 8W4E 8W4C 8W4D 8WUE 8WWB 8YBB	Fu et al. (2024). Fu C, Xiao Y, Zhou X, & Sun Z (2024). Insight into binding of endogenous neurosteroid ligands to the sigma-1 receptor. Nat Commun 15 1:5619. PubMed Id: 38965213. doi:10.1038/s41467-024-49894-7.
*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 7M94 7M96 7M95 7MFI 7M93 7M94 7M96 7M95 7MFI 7M93 7M94 7M96 7M95 7MFI	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 5SY1 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 2BRD 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 1AT9 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 1AP9 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 1BRR 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 1BRX 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 1R84 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 1QKP 1QKO 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 1M0K 1M0L 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 1KG8 1KG9 1KGB 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 1QHJ 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 1C3W 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 1C8R 1C8S 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 3NS0 3NSB 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 3T45 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 4FPD 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 4X31 4X32 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 5B35 5B34 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 5H2M 5H2L 5H2I 5B6Z 5B6W 5B6Y 5H2H 5H2J 5B6X 5H2K 5H2O 5H2P 5H2N 5B6V 5H2M 5H2L 5H2I 5B6Z 5B6W 5B6Y 5H2H 5H2J 5B6X 5H2K 5H2O 5H2P 5H2N 5B6V 5H2M 5H2L 5H2I 5B6Z 5B6W 5B6Y 5H2H 5H2J 5B6X 5H2K 5H2O 5H2P 5H2N	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 6G7I 6G7L 6G7J 6G7K 6G7H 6G7I 6G7L 6G7J 6G7K 6G7H 6G7I 6G7L 6G7J 6G7K	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 5ZIL 5ZIN 5ZIM 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 6RNJ 6RPH 6RQO 6RNJ 6RPH 6RQO 6RNJ 6RPH	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 6GAB 6GA9 6GAF 6GA6 6GAA 6GA4 6GAG 6RMK 6GAC 6GAH 6GA7 6GAE 6GA5 6GA8 6GAD 6GA2 6GA3 6AGI 6GA1 6GAB 6GA9 6GAF 6GA6 6GAA 6GA4 6GAG 6RMK 6GAC 6GAH 6GA7 6GAE 6GA5 6GA8 6GAD 6GA2 6GA3 6AGI 6GA1 6GAB 6GA9 6GAF 6GA6 6GAA 6GA4 6GAG 6RMK 6GAC 6GAH 6GA7 6GAE 6GA5 6GA8 6GAD 6GA2 6GA3 6AGI	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 7VSO 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 7Z0D 7Z0E 7Z0C 7Z09 7Z0A 7Z0D 7Z0E 7Z0C 7Z09 7Z0A 7Z0D 7Z0E 7Z0C	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 7XJD 7XJE 7XJC 7XJD 7XJE 7XJC 7XJD 7XJE	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 4QI1 4QID 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 5ITE 5ITC 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 1E12 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 7Q36 7Q37 7Q35 7Q38 7Q36 7Q37 7Q35 7Q38 7Q36 7Q37 7Q35	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 3A7K 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 7ZOY 7ZOV 7ZOW 7ZOU 7ZOY 7ZOV 7ZOW 7ZOU 7ZOY 7ZOV 7ZOW	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 6K6I 6K6K 6K6J 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 1XIO 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 2M3G 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 1JGJ 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 1H68 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 1H2S 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 2KSY 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 3QDC 3QAP 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 1UAZ 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 1VGO 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 2EI4 2Z55 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 3WQJ 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 6GUX 6S6C 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 6GUZ 6S63 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 3DDL 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 3AM6 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 3UG9 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 4YZI 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 7E70 7E6Y 7E6Z 7E71 7E6X 7C86 7E70 7E6Y 7E6Z 7E71 7E6X 7C86 7E70 7E6Y 7E6Z 7E71 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 6CSN 6CSO 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 6EID 6EIG 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 6CSM 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 6EDQ 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 7L1E 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 5ZIH 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 2L6X 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 7B03 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 4HYJ 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 4JQ6 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 4KLY 4KNF 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 4L35 4JR8 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 3X3B 3X3C 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 6RF0 6RF5 6RF4 6REW 6RFA 6RF3 6RF7 6RFB 6RF6 6REZ 6RF1 6RFC 6REX 6RF0 6RF5 6RF4 6REW 6RFA 6RF3 6RF7 6RFB 6RF6 6REZ 6RF1 6RFC 6REX 6RF0 6RF5 6RF4 6REW 6RFA 6RF3 6RF7 6RFB 6RF6 6REZ 6RF1 6RFC	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 6YC0 6YC1 6YBY 6YC2 6YC4 6YBZ 6YC3 6XYT 6YC0 6YC1 6YBY 6YC2 6YC4 6YBZ 6YC3 6XYT 6YC0 6YC1 6YBY 6YC2 6YC4 6YBZ 6YC3	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 4XTL 4XTN 4XTL 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 6TK3 6TK6 6TK2 6TK4 6TK5 6TK1 6TK7 6TK3 6TK6 6TK2 6TK4 6TK5 6TK1 6TK7 6TK3 6TK6 6TK2 6TK4 6TK5 6TK1	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 5AZD 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 6IS6 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 7U55 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 6SU3 6SU4 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 6SQG 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 5G2C 5G54 5G2A 5G28 5G2D 5G2C 5G54 5G2A 5G28 5G2D 5G2C 5G54 5G2A	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 7CRT 7CRY 7CRK 7CRX 7CRS 7CRJ 7CRI 7CRT 7CRY 7CRK 7CRX 7CRS 7CRJ 7CRI 7CRT 7CRY 7CRK 7CRX 7CRS	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 6JY6 6JYA 6JYB 6JYD 6JY7 6JYC 6JYF 6JY8 6JY9 6JYE 6JY6 6JYA 6JYB 6JYD 6JY7 6JYC 6JYF 6JY8 6JY9 6JYE 6JY6 6JYA 6JYB 6JYD 6JY7 6JYC 6JYF 6JY8 6JY9	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 7VGU 7VGV 7VGT 7VGU 7VGV 7VGT 7VGU 7VGV	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 7O8O 7O8M 7O8Z 7O8G 7O8R 7O8S 7O8L 7O8Y 7O8H 7O8P 7O8U 7O8Q 7O8V 7O8N 7O8J 7O8I 7O8K 7O8F 7O8O 7O8M 7O8Z 7O8G 7O8R 7O8S 7O8L 7O8Y 7O8H 7O8P 7O8U 7O8Q 7O8V 7O8N 7O8J 7O8I 7O8K 7O8F 7O8O 7O8M 7O8Z 7O8G 7O8R 7O8S 7O8L 7O8Y 7O8H 7O8P 7O8U 7O8Q 7O8V 7O8N 7O8J 7O8I 7O8K	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 7CJ3 7D7Q 7D7P 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 6LM0 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 6LM1 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 7AKX 7AKW 7AKY 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 7BMH 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 7PL9 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 7W74 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 7E4G 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 6GYH 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 6NWD 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 6XL3 6WP8 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 7SFK 7SHS 7SFJ 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 7W9W 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.
*kalium channelrhodopsin 1 (KCR1) embedded in peptidisc: Hyphochytrium catenoides* E Eukaryota (expressed in Komagataella pastoris), 2.88 Å** cryo-EM structure	8GI8	Data File Jmol Viewer 8GI8 8GI8 8GI8	Morizumi et al. (2023). Morizumi T, Kim K, Li H, Govorunova EG, Sineshchekov OA, Wang Y, Zheng L, Bertalan É, Bondar AN, Askari A, Brown LS, Spudich JL, & Ernst OP (2023). Structures of channelrhodopsin paralogs in peptidiscs explain their contrasting K+ and Na+ selectivities. Nat Commun 14 1:4365. PubMed Id: 37474513. doi:10.1038/s41467-023-40041-2.
*Xenorhodopsin (XeR), ground state, pH 8.2, in the presence of sodium, 100K structure: Bacillus coahuilensis* B Bacteria (expressed in expressed in E. coli), 1.70 Å** X-ray structure M state, pH 8.2, in the presence of sodium,1.70 Å: 7ZN0 L state, pH 8.2, in the presence of sodium,1.60 Å: 7ZN3 ground state, pH 7.0, in the presence of sodium, 2.20 Å: 7ZN8 M state, pH 7.0, in the presence of sodium, 2.30 Å: 7ZN9 ground state, pH 5.2, in the presence of sodium, 1.80 Å: 7ZNA M state, pH 5.2, in the presence of sodium, 1.90 Å: 7ZNB ground state, pH 7.6, 1.70 Å: 7ZNC M state, pH 7.6, 1.70 Å: 7ZND ground state, pH 8.2, room temperature (RT) structure with 7.5 ms-snapshot, 2.10 Å: 7ZNE ground state, pH 8.2, RT structure with 500 μs-snapshot, 2.30 Å: 7ZNG activated state, pH 8.2, RT structure with 250-750 μs-snapshot, 2.30 Å: 7ZNH activated state, pH 8.2, RT structure with 7.5-15 ms-snapshot, 2.20 Å: 7ZNI	7ZMY	Data File Jmol Viewer 7ZMY 7ZNI 7ZNC 7ZN8 7ZN3 7ZNE 7ZN9 7ZNA 7ZND 7ZNB 7ZN0 7ZNG 7ZNH 7ZMY 7ZNI 7ZNC 7ZN8 7ZN3 7ZNE 7ZN9 7ZNA 7ZND 7ZNB 7ZN0 7ZNG 7ZNH 7ZMY 7ZNI 7ZNC 7ZN8 7ZN3 7ZNE 7ZN9 7ZNA 7ZND 7ZNB 7ZN0 7ZNG 7ZNH	Kovalev et al. (2023). Kovalev K, Tsybrov F, Alekseev A, Shevchenko V, Soloviov D, Siletsky S, Bourenkov G, Agthe M, Nikolova M, von Stetten D, Astashkin R, Bukhdruker S, Chizhov I, Royant A, Kuzmin A, Gushchin I, Rosselli R, Rodriguez-Valera F, Ilyinskiy N, Rogachev A, Borshchevskiy V, Schneider TR, Bamberg E, & Gordeliy V (2023). Mechanisms of inward transmembrane proton translocation. Nat Struct Mol Biol 30 7:970-979. PubMed Id: 37386213. doi:10.1038/s41594-023-01020-9.
*Xenorhodopsin (XeR): Candidatus Nanosalina* B Bacteria (expressed in expressed in E. coli), 2.50 Å** X-ray structure	6EYU	Data File Jmol Viewer 6EYU 6EYU 6EYU	Shevchenko et al. (2017). Shevchenko V, Mager T, Kovalev K, Polovinkin V, Alekseev A, Juettner J, Chizhov I, Bamann C, Vavourakis C, Ghai R, Gushchin I, Borshchevskiy V, Rogachev A, Melnikov I, Popov A, Balandin T, Rodriguez-Valera F, Manstein DJ, Bueldt G, Bamberg E, & Gordeliy V (2017). Inward H+ pump xenorhodopsin: Mechanism and alternative optogenetic approach. Sci Adv 3 9:e1603187. PubMed Id: 28948217. doi:10.1126/sciadv.1603187.
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 6R4O 6R4P 6R3Q 6R4O 6R4P 6R3Q 6R4O 6R4P	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.
*Adenylyl cyclase Rv1625c/Cya in C1 symmetry: Mycobacterium tuberculosis* B Bacteria (expressed in E.coli), 3.83 Å** cryo-EM structure in C2 symmetry, 3.57 Å: 7YZK	7YZI	Data File Jmol Viewer 7YZI 7YZK 7YZI 7YZK 7YZI 7YZK	Mehta et al. (2022). Mehta V, Khanppnavar B, Schuster D, Kantarci I, Vercellino I, Kosturanova A, Iype T, Stefanic S, Picotti P, & Korkhov VM (2022). Structure of Mycobacterium tuberculosis Cya, an evolutionary ancestor of the mammalian membrane adenylyl cyclases. Elife 11 :e77032. PubMed Id: 35980026. doi:10.7554/eLife.77032.
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 2KSD 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 2KSE 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 8JWD 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 7X6G 7X6H 7X6F 7X6G 7X6H 7X6F 7X6G 7X6H	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 2KSF 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 5JEQ 5JEF 5IJI 5JEQ 5JEF 5IJI 5JEQ 5JEF	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 6XYN 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 6YUE 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 6JXR 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 2HAC 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 7FJD 7FJF 7FJE 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 2L35 2L34 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 4WOL 4WO1 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 7VU5 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 3HD7 3HD9 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 2KOG 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 2M8R 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 6MTI 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 6XM1 6XJL 6XMD 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 7BV6 7BV4 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 7UDB 7UDC 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 7KP4 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 7TDM 7TDN 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 6OV2 6OV3 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 4P79 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 3X29 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 4WIS 4WIT 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 6QM6 6QMB 6QM5 6QMA 6QM4 6QM9 6QM6 6QMB 6QM5 6QMA 6QM4 6QM9 6QM6 6QMB 6QM5 6QMA 6QM4	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 6OY3 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 5NL2 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 5OYB 5OYG 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 6BGI 6BGJ 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 7B5C 7B5E 7B5D 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 7ZK3 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.
*TMEM16A calcium-activated chloride channel, Ca²⁺ bound, L647V & I733V mutant: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.29 Å** cryo-EM structure	8QZC	Data File Jmol Viewer 8QZC 8QZC 8QZC	Lam & Dutzler (2023). Lam AK, & Dutzler R (2023). Mechanistic basis of ligand efficacy in the calcium-activated chloride channel TMEM16A. EMBO J 42 24:e115030. PubMed Id: 37984335. doi:10.15252/embj.2023115030.
*TMEM16A calcium-activated chloride channel, Ca²⁺ bound, in complex with Tamsulosin: Mus musculus* E Eukaryota (expressed in HEK293 cells), 2.93 Å** cryo-EM structure	8XLR	Data File Jmol Viewer 8XLR 8XLR 8XLR	Chen et al. (2024). Chen H, Xia Z, Dong J, Huang B, Zhang J, Zhou F, Yan R, Shi Y, Gong J, Jiang J, Huang Z, & Jiang D (2024). Structural mechanism of voltage-gated sodium channel slow inactivation. Nat Commun 15 1:3691. PubMed Id: 38693179. doi:10.1038/s41467-024-48125-3.
*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 6E1O 6DZ7 6E0H 6E1O 6DZ7 6E0H 6E1O 6DZ7	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 6QPI 6QP6 6QPB 6QPC 6QPI 6QP6 6QPB 6QPC 6QPI 6QP6 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 6P49 6P48 6P46 6P47 6P49 6P48 6P46 6P47 6P49 6P48	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 8B8M 8BC0 8B8Q 8BC1 8B8K 8B8J 8B8G 8B8M 8BC0 8B8Q 8BC1 8B8K 8B8J 8B8G 8B8M 8BC0 8B8Q 8BC1 8B8K 8B8J	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 8TAL 8SUR 8TAG 8SUN 8TAI 8TAL 8SUR 8TAG 8SUN 8TAI 8TAL 8SUR	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 6R7Z 6R7Y 5OC9 6R65 6R7X 6R7Z 6R7Y 5OC9 6R65 6R7X 6R7Z 6R7Y 5OC9 6R65	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 7P14 7P16 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 7DCE 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 1RHZ 1RH5 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 2YXR 2YXQ 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 3MP7 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 3DIN 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 5EUL 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 6ITC 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 7XHA 7XHB 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 6R7L 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 2ZJS 2ZQP 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 5AWW 5CH4 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 3JC2 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 6Z3T 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 6W6L 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 8DO0 8DO2 8DNY 8DO3 8DNW 8DO1 8DNX 8DNZ 8DNV 8DO0 8DO2 8DNY 8DO3 8DNW 8DO1 8DNX 8DNZ 8DNV 8DO0 8DO2 8DNY 8DO3 8DNW 8DO1 8DNX 8DNZ	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 7TM3 7TUT 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 6N3Q 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 6ND1 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 7AFT 6ZZZ 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 7KAP 7KAT 7KB5 7KAU 7KAR 7KAO 7KAJ 7KAI 7KAQ 7KAH 7KAP 7KAT 7KB5 7KAU 7KAR 7KAO 7KAJ 7KAI 7KAQ 7KAH 7KAP 7KAT 7KB5 7KAU 7KAR 7KAO 7KAJ 7KAI 7KAQ	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 7KAN 7KAM 7KAL 7KAK 7KAN 7KAM 7KAL 7KAK 7KAN 7KAM 7KAL	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 3WO6 3WO7 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 3WVF 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 6AL2 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 5Y83 5Y82 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 6Y86 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 6SO5 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 8CR1 8CR2 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 8CQZ 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 8ODU 8ODV 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 5C8J 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 3AQP 3AQO 2RRN 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 5YHF 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 5AXP 5XAN 5XAM 5AXP 5XAN 5XAM 5AXP 5XAN	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 2L16 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 2LZS 2LZR 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 4B4A 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 4HTS 4HTT 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 5V6P 5V7V 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 6VJY 6VJZ 6VK3 6VK1 6VK0 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 7CZB 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 6E10 6E11 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 6WQZ 6WR4 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 7JLO 7JLQ 7JLP 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 7D0I 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 6Z3W 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 6WW7 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 7ADP 7ADO 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 8EOI 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 6WB9 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 7KTX 7KRA 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 6LO8 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 7CGP 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.
*TIM23 complex (Tim17–Tim23–Tim44) from mitochondrial inner membrane: Saccharomyces cerevisiae* E Eukaryota (expressed in yeast), 2.70 Å** cryo-EM structure endogenous TIM23 complex extracted from S. cerevisiae, 2.90 Å: 8E1M	8SCX	Data File Jmol Viewer 8SCX 8E1M 8SCX 8E1M 8SCX 8E1M	Sim et al. (2023). Sim SI, Chen Y, Lynch DL, Gumbart JC, & Park E (2023). Structural basis of mitochondrial protein import by the TIM23 complex. Nature 621 7979:620-626. PubMed Id: 37344598. doi:10.1038/s41586-023-06239-6.
Channels: Mechanosensitive
*MscL Mechanosensitive channel: Mycobacterium tuberculosis* B Bacteria, 3.5 Å** This structure supersedes 1MSL.	2OAR	Data File Jmol Viewer 2OAR 2OAR 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 3HZQ 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 4Y7K 4Y7J 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 2OAU 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 2VV5 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 5AJI 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 6RLD 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 6PWN 6PWO 6PWP 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 6UZH 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 6VYL 6VYM 6VYK 6VYL 6VYM 6VYK 6VYL 6VYM	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 7OO6 7OO0 7OOA 7OO8 7ONJ 7ONL 7OO6 7OO0 7OOA 7OO8 7ONJ 7ONL 7OO6 7OO0 7OOA 7OO8 7ONJ	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 6VXP 6VXN 6VXM 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 6LYP 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.
*MSL10 MscS voltage-modulated mechanosensitive channel homolog in GDN: Arabidopsis thaliana* E Eukaryota (expressed in K. pastoris), 3.70 Å** cryo-EM structure G556V mutant, 3.50 Å: 8TDK K539E mutant, 3.70 Å: 8TDM in saposin, 3.60 Å: 8TDL	8TDJ	Data File Jmol Viewer 8TDJ 8TDM 8TDK 8TDL 8TDJ 8TDM 8TDK 8TDL 8TDJ 8TDM 8TDK 8TDL	Zhang et al. (2023). Zhang J, Maksaev G, & Yuan P (2023). Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10. Nat Commun 14 1:6284. PubMed Id: 37805510. doi:10.1038/s41467-023-42117-5.
*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 3JAC 4RAX 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 6B3R 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 6BPZ 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 5Z10 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 6LQI 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 7WLT 7WLU 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 8IMZ 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 6KG7 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 6JPF 5Z1F 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 8GRN 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 6MGV 6MGW 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 8T56 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 8XNG 8XS4 8XW2 8XS5 8XVX 8XW1 8XW3 8XAJ 8XNG 8XS4 8XW2 8XS5 8XVX 8XW1 8XW3 8XAJ 8XNG 8XS4 8XW2 8XS5 8XVX 8XW1 8XW3	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 6OCE 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 8T57 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 8GRO 8GSO 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 8XVY 8XVZ 8XW0 8XRY 8XS0 8XVY 8XVZ 8XW0 8XRY 8XS0 8XVY 8XVZ 8XW0	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 3.1 in nanodiscs: Arabidopsis thaliana* E Eukaryota (expressed in HEK293 cells), 2.60 Å** cryo-EM structure	8U53	Data File Jmol Viewer 8U53 8U53 8U53	Jojoa-Cruz et al. (2024). Jojoa-Cruz S, Dubin AE, Lee WH, & Ward AB (2024). Structure-guided mutagenesis of OSCAs reveals differential activation to mechanical stimuli. Elife 12 . PubMed Id: 38592763. doi:10.7554/eLife.93147.
*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 8GRS 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 TMEM63A in nanodisc: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.80 Å** cryo-EM structure	8EHW	Data File Jmol Viewer 8EHW 8EHW 8EHW	Zheng et al. (2023). Zheng W, Rawson S, Shen Z, Tamilselvan E, Smith HE, Halford J, Shen C, Murthy SE, Ulbrich MH, Sotomayor M, Fu TM, & Holt JR (2023). TMEM63 proteins function as monomeric high-threshold mechanosensitive ion channels. Neuron 111 20:3195-3210.e7. PubMed Id: 37543036. doi:10.1016/j.neuron.2023.07.006.
*Hypo-osmolality-gated calcium-permeable channel TMEM63B in LMNG: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.60 Å** cryo-EM structure	8EHX	Data File Jmol Viewer 8EHX 8EHX 8EHX	Zheng et al. (2023). Zheng W, Rawson S, Shen Z, Tamilselvan E, Smith HE, Halford J, Shen C, Murthy SE, Ulbrich MH, Sotomayor M, Fu TM, & Holt JR (2023). TMEM63 proteins function as monomeric high-threshold mechanosensitive ion channels. Neuron 111 20:3195-3210.e7. PubMed Id: 37543036. doi:10.1016/j.neuron.2023.07.006.
*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 8XW4 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 8K0B 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 7N5G 7N5E 7N5F 7N5D 7N5G 7N5E 7N5F 7N5D 7N5G 7N5E 7N5F	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 5Y4O 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 7N4T 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 7USY 7USX 7USW 7USY 7USX 7USW 7USY 7USX	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 7UW5 7UX1 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 1BL8 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 1K4C 1K4D 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 1F6G 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 2BOB 2BOC 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 2ITC 2ITD 2NLJ 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 3EFF 3EFD 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 3PJS 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 3IGA 3GB7 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 3F7Y 3F7V 3FB5 3FB6 3F5W 3F7Y 3F7V 3FB5 3FB6 3F5W 3F7Y 3F7V 3FB5 3FB6	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 3HPL 3FB7 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 3OR7 3OR6 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 3STL 3STZ 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 4MSW 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 2JK5 4UUJ 2W0F 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 5EBM 5EBL 5EBW 5EC2 5EC1 5EBM 5EBL 5EBW 5EC2 5EC1 5EBM 5EBL 5EBW 5EC2	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 5VK6 5VKE 5VKH 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 6NFU 6NFV 6PA0 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 6W0E 6W0H 6W0B 6W0C 6W0I 6W0D 6W0F 6W0G 6W0J 6W0A 6W0E 6W0H 6W0B 6W0C 6W0I 6W0D 6W0F 6W0G 6W0J 6W0A 6W0E 6W0H 6W0B 6W0C 6W0I 6W0D 6W0F 6W0G 6W0J	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 7M2J 7M2I 7M2H 7M2J 7M2I 7M2H 7M2J 7M2I	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 7MK6 7MUB 7MJT 7MHR 7MHX 7MK6 7MUB 7MJT 7MHR 7MHX 7MK6 7MUB 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 6BY2 6BY3 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 3UKM 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 7SK0 7SK1 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 6RV2 6RV3 6RV4 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 6WLV 6WM0 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 3UM7 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 4I9W 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 4WFE 4WFH 4WFG 4WFF 4WFE 4WFH 4WFG 4WFF 4WFE 4WFH 4WFG	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 4RUE 4RUF 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 7LJ4 7LJB 7LJA 7LJ5 7LJ4 7LJB 7LJA 7LJ5 7LJ4 7LJB 7LJA	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 6PIS 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 6CQ9 6CQ8 6CQ6 6CQ9 6CQ8 6CQ6 6CQ9 6CQ8	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 6V3I 6V37 6V3C 6V36 6V3I 6V37 6V3C 6V36 6V3I 6V37 6V3C	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 6W88 6W8F 6W87 6W85 6W7C 6W7D 6W82 6W8A 6W7E 6W86 6W84 6W83 6W8C 6W7B 6W88 6W8F 6W87 6W85 6W7C 6W7D 6W82 6W8A 6W7E 6W86 6W84 6W83 6W8C 6W7B 6W88 6W8F 6W87 6W85 6W7C 6W7D 6W82 6W8A 6W7E 6W86 6W84 6W83 6W8C	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 4XDJ 4XDL 4XDK 4BW5 4XDJ 4XDL 4XDK 4BW5 4XDJ 4XDL 4XDK	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 5DQQ 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 5E1J 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 5TUA 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 6E1P 6E1K 6E1N 6E1M 6E1P 6E1K 6E1N 6E1M 6E1P 6E1K 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 7TDD 7TDE 7TBG 7TDF 7TDD 7TDE 7TBG 7TDF 7TDD 7TDE 7TBG	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 7FHL 7FHO 7FHN 7FHK 7FHL 7FHO 7FHN 7FHK 7FHL 7FHO 7FHN	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 6C9A 6C96 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 6NQ0 6NQ2 6NQ1 6NQ0 6NQ2 6NQ1 6NQ0 6NQ2	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 6V1Q 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 1ORQ 1ORS 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 2A0L 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 2KYH 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 6UWM 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 7SIP 7SJ1 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 8TEO 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 2A79 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 3LUT 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 7SIZ 7SIT 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 2R9R 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 3LNM 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 5WIE 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 6EBK 6EBL 6EBM 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.
*Kv2.1 Voltage-gated potassium channel, wild-type: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), HEK293 cells** cryo-EM structure L403A mutant, 3.32 Å: 8SDA	8SD3	Data File Jmol Viewer 8SD3 8SDA 8SD3 8SDA 8SD3 8SDA	Fernández-Mariño et al. (2023). Fernández-Mariño AI, Tan XF, Bae C, Huffer K, Jiang J, & Swartz KJ (2023). Inactivation of the Kv2.1 channel through electromechanical coupling. Nature 622 7982:410-417. PubMed Id: 37758949. doi:10.1038/s41586-023-06582-8.
*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 7EJ1 7EJ2 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 7WF3 7WF4 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 7PHH 7PHK 7PHI 7PHL 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 7PQT 7PQU 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 8QUC 8QUD 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.
*K_V3.1 voltage-gated potassium channel (alternative name: KCNC1), apo form: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.94 Å** cryo-EM structure with bound modulator compound-4, 2.92 Å: 8F1C	8F1D	Data File Jmol Viewer 8F1D 8F1C 8F1D 8F1C 8F1D 8F1C	Chen et al. (2023). Chen YT, Hong MR, Zhang XJ, Kostas J, Li Y, Kraus RL, Santarelli VP, Wang D, Gomez-Llorente Y, Brooun A, Strickland C, Soisson SM, Klein DJ, Ginnetti AT, Marino MJ, Stachel SJ, & Ishchenko A (2023). Identification, structural, and biophysical characterization of a positive modulator of human Kv3.1 channels. Proc Natl Acad Sci U S A 120 42:e2220029120. PubMed Id: 37812700. doi:10.1073/pnas.2220029120.
*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 7F3F 7E8E 7E8B 7E83 7E8H 7E84 7E7Z 7E87 7E89 7E8G 7F0J 7F3F 7E8E 7E8B 7E83 7E8H 7E84 7E7Z 7E87 7E89 7E8G 7F0J 7F3F 7E8E 7E8B 7E83 7E8H 7E84 7E7Z 7E87 7E89 7E8G	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 7UKH 7UKE 7UKG 7UKC 7UKF 7UKD 7UK5 7UKH 7UKE 7UKG 7UKC 7UKF 7UKD 7UK5 7UKH 7UKE 7UKG 7UKC 7UKF 7UKD	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 7W3Y 7W6N 7W6S 7W6T 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 5K7L 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 7YIH 7YIF 7YIG 7YIJ 7YIE 7YID 7YIH 7YIF 7YIG 7YIJ 7YIE 7YID 7YIH 7YIF 7YIG 7YIJ 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 8EP1 8EP0 8EOW 8EP1 8EP0 8EOW 8EP1 8EP0	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 5VA2 5VA1 5VA3 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 7CN0 7CN1 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 4H33 4H37 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 1LNQ 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 3LDC 3LDD 3LDE 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 3RBZ 3RBX 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 4EI2 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 4HYO 4HZ3 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 4L75 4L76 4L74 4L73 4L75 4L76 4L74 4L73 4L75 4L76 4L74	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 6OLY 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 6U5P 6U5N 6UX4 6UXA 6U6E 6UXB 6UWN 6U5R 6UX7 6U68 6U6D 6U5P 6U5N 6UX4 6UXA 6U6E 6UXB 6UWN 6U5R 6UX7 6U68 6U6D 6U5P 6U5N 6UX4 6UXA 6U6E 6UXB 6UWN 6U5R 6UX7 6U68	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 6U9Z 6U9T 6U9P 6U9Y 6U9Z 6U9T 6U9P 6U9Y 6U9Z 6U9T	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.
*MthK Potassium channel, Ca⁺⁺ gated, in nanodisc, closed form, blocker-free: Methanothermobacter thermautotrophicus* A Archaea (expressed in E. coli), 3.10 Å** cryo-EM structure with bound TPeA, 3.50 Å: 5BKJ with bound bbTBA, 3.50 Å: 5BKK A90L mutant, blocker-free, 3.18 Å: 8DJB A88F mutant, with bound TPeA, 2.88 Å: 8FZ7	5BKI	Data File Jmol Viewer 5BKI 5BKJ 5BKK 8FZ7 8DJB 5BKI 5BKJ 5BKK 8FZ7 8DJB 5BKI 5BKJ 5BKK 8FZ7 8DJB	Fan et al. (2024). Fan C, Flood E, Sukomon N, Agarwal S, Allen TW, & Nimigean CM (2024). Calcium-gated potassium channel blockade via membrane-facing fenestrations. Nat Chem Biol 20 1:52-61. PubMed Id: 37653172. doi:10.1038/s41589-023-01406-2.
*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 5TJ6 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 5TJI 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 3MT5 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 3NAF 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 6V35 6V38 6V3G 6V22 6V35 6V38 6V3G 6V22 6V35 6V38 6V3G	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 6V5A 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 8GH9 8GHF 8GHG 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 3U6N 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 7PXF 7PXH 7PXE 7PXF 7PXH 7PXE 7PXF 7PXH	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 5A6E 5A6F 5A6G 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 5U70 5U76 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 8HK6 8HKK 8HKQ 8HKM 8HKF 8HIR 8HK6 8HKK 8HKQ 8HKM 8HKF 8HIR 8HK6 8HKK 8HKQ 8HKM 8HKF	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 4HPF 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 6CNN 6CNO 6CNM 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 4GX0 4GX1 4GX5 4GX2 4GVL 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 7ZDZ 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.
*Kir2.1 Inward-Rectifier Potassium 2.1 Channel, R312H mutant: Homo sapiens* E Eukaryota (expressed in Komagataella pastoris), 6.00 Å** cryo-EM structure	8QQL	Data File Jmol Viewer 8QQL 8QQL 8QQL	Zuniga et al. (2024). Zuniga D, Zoumpoulakis A, Veloso RF, Peverini L, Shi S, Pozza A, Kugler V, Bonneté F, Bouceba T, Wagner R, Corringer PJ, Fernandes CAH, & Vénien-Bryan C (2024). Biochemical, biophysical, and structural investigations of two mutants (C154Y and R312H) of the human Kir2.1 channel involved in the Andersen-Tawil syndrome. FASEB J 38 21:e70146. PubMed Id: 39520289. doi:10.1096/fj.202401567R.
*Kir2.2 Inward-Rectifier Potassium Channel (Complete): Gallus gallus* E Eukaryota (expressed in Pichia pastoris), 3.1 Å**	3JYC	Data File Jmol Viewer 3JYC 3JYC 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 3SPH 3SPJ 3SPC 3SPI 3SPG 3SPH 3SPJ 3SPC 3SPI 3SPG 3SPH 3SPJ 3SPC	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 5KUK 5KUM 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 6M86 6M84 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 1N9P 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 2QKS 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 3K6N 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 3SYQ 3SYC 3SYA 3SYO 3SYP 3SYQ 3SYC 3SYA 3SYO 3SYP 3SYQ 3SYC 3SYA	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 4KFM 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 6XIS 6XIT 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 1P7B 2WLL 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 2X6C 2WLH 1XL4 2X6B 2WLO 2WLI 2X6A 1XL6 2WLK 2WLN 2WLJ 2WLM 2X6C 2WLH 1XL4 2X6B 2WLO 2WLI 2X6A 1XL6 2WLK 2WLN 2WLJ 2WLM 2X6C 2WLH 1XL4 2X6B 2WLO 2WLI 2X6A 1XL6 2WLK 2WLN	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 3ZRS 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 4LP8 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 6O9U 6O9V 6O9T 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 7N9L 7N9K 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 7ADI 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 5TWV 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 6BAA 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 6PZ9 6PZC 6PZI 6PZA 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 7U1E 7U6Y 7TYT 7U1Q 7U2X 7UAA 7U1S 7U7M 7TYS 7U1E 7U6Y 7TYT 7U1Q 7U2X 7UAA 7U1S 7U7M 7TYS 7U1E 7U6Y 7TYT 7U1Q 7U2X 7UAA 7U1S 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 8TI2 8TI1 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 5WUA 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 5YKE 5YKG 5YW7 5YWB 5YWC 5YW9 5YKF 5YWA 5YWD 5YW8 5YKE 5YKG 5YW7 5YWB 5YWC 5YW9 5YKF 5YWA 5YWD 5YW8 5YKE 5YKG 5YW7 5YWB 5YWC 5YW9 5YKF 5YWA 5YWD	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 6JB1 6JB3 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 7W4O 7W4P 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 6C3O 6C3P 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 7S5Y 7S5Z 7S61 7S5V 7S5X 7S60 7S5T 7S5Y 7S5Z 7S61 7S5V 7S5X 7S60 7S5T 7S5Y 7S5Z 7S61 7S5V 7S5X 7S60	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.
*SUR2A ATP-sensitive K⁺ channel with bound Mg-ATP/ADP and P1075: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure	7VLU	Data File Jmol Viewer 7VLU 7VLU 7VLU	Ding et al. (2022). Ding D, Wu JX, Duan X, Ma S, Lai L, & Chen L (2022). Structural identification of vasodilator binding sites on the SUR2 subunit. Nat Commun 13 1:2675. PubMed Id: 35562524. doi:10.1038/s41467-022-30428-y.
*SUR2A with bound Mg-ATP and repaglinide, inward-facing conformation: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure member of ATP-binding cassette sub-family C member 9 (ABCC9) with bound Mg-ATP/ADP and repaglinide, 3.80 Å: 7Y1K	7Y1J	Data File Jmol Viewer 7Y1J 7Y1K 7Y1J 7Y1K 7Y1J 7Y1K	Ding et al. (2023). Ding D, Hou T, Wei M, Wu JX, & Chen L (2023). The inhibition mechanism of the SUR2A-containing KATP channel by a regulatory helix. Nat Commun 14 1:3608. PubMed Id: 37330603. doi:10.1038/s41467-023-39379-4.
*SUR2B/Kir6.1 ATP-sensitive K⁺ channel with bound ATP and glibenclamide, propeller-like conformation 1: Rattus norvegicus* E Eukaryota (expressed in C. aethiops), 3.40 Å** cryo-EM structure propeller-like conformation 2, 4.20 Å: 7MJP quatrefoil-like conformation 1, 4.00 Å: 7MJO quatrefoil-like conformation 2, 4.20 Å: 7MJQ	7MIT	Data File Jmol Viewer 7MIT 7MJQ 7MJP 7MJO 7MIT 7MJQ 7MJP 7MJO 7MIT 7MJQ 7MJP 7MJO	Sung et al. (2021). Sung MW, Yang Z, Driggers CM, Patton BL, Mostofian B, Russo JD, Zuckerman DM, & Shyng SL (2021). Vascular KATP channel structural dynamics reveal regulatory mechanism by Mg-nucleotides. Proc Natl Acad Sci U S A 118 44:e2109441118. PubMed Id: 34711681. doi:10.1073/pnas.2109441118.
*SUR2B ATP-sensitive K⁺ channel with bound Mg-ATP/ADP: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.40 Å** cryo-EM structure with bound Mg-ATP/ADP and P1075, 3.30 Å: 7VLS with bound Mg-ATP/ADP and levcromakalim, 3.10 Å: 7VLT	7VLR	Data File Jmol Viewer 7VLR 7VLS 7VLT 7VLR 7VLS 7VLT 7VLR 7VLS 7VLT	Ding et al. (2022). Ding D, Wu JX, Duan X, Ma S, Lai L, & Chen L (2022). Structural identification of vasodilator binding sites on the SUR2 subunit. Nat Commun 13 1:2675. PubMed Id: 35562524. doi:10.1038/s41467-022-30428-y.
*SUR2B with bound Mg-ATP and repaglinide, inward-facing conformation: Rattus norvegicus* E Eukaryota (expressed in HEK293 cells), 3.73 Å** cryo-EM structure with bound Mg-ATP/ADP and repaglinide, 3.57 Å: 7Y1M with bound Mg-ATP/ADP, and repaglinide in the partially occluded state, 3.61 Å: 7Y1N	7Y1L	Data File Jmol Viewer 7Y1L 7Y1N 7Y1M 7Y1L 7Y1N 7Y1M 7Y1L 7Y1N 7Y1M	Ding et al. (2023). Ding D, Hou T, Wei M, Wu JX, & Chen L (2023). The inhibition mechanism of the SUR2A-containing KATP channel by a regulatory helix. Nat Commun 14 1:3608. PubMed Id: 37330603. doi:10.1038/s41467-023-39379-4.
*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 2AHY 2AHZ 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 2Q67 2Q6A 2Q69 2Q68 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 3E86 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 3K06 3K0G 3K08 3K04 3K0D 3K06 3K0G 3K08 3K04 3K0D 3K06 3K0G 3K08 3K04	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 3OUS 3K03 3OUF 3OUS 3K03 3OUF 3OUS 3K03	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 3TET 3T4Z 3TCU 3T2M 3T4D 3T1C 3TET 3T4Z 3TCU 3T2M 3T4D 3T1C 3TET 3T4Z 3TCU 3T2M 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 6V8Y 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 3VOU 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 3RVY 3RW0 3RVZ 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 4EKW 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 5VB2 5VB8 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 6C1M 6C1P 6C1K 6C1E 6C1M 6C1P 6C1K 6C1E 6C1M 6C1P 6C1K	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 6MWB 6MWD 6MWG 6MWA 6MWB 6MWD 6MWG 6MWA 6MWB 6MWD 6MWG	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 6MVY 6MVW 6MVX 6MVV 6MVY 6MVW 6MVX 6MVV 6MVY 6MVW 6MVX	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 6P6X 6P6Y 6P6W 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 7TJ8 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 6W6O 6VXO 6VWX 6VX3 6W6O 6VXO 6VWX 6VX3 6W6O 6VXO 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 4DXW 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 4F4L 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 3ZJZ 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 4P30 4PA7 4P2Z 4PA4 4PA3 4OXS 4PA6 4PA9 4P9P 4CBC 4P9O 4P30 4PA7 4P2Z 4PA4 4PA3 4OXS 4PA6 4PA9 4P9P 4CBC 4P9O 4P30 4PA7 4P2Z 4PA4 4PA3 4OXS 4PA6 4PA9 4P9P	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 5BZB 4X88 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 5HVX 5HVD 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 6SXE 6SXC 6SXG 6Z8C 6SX7 6SX5 6SXE 6SXC 6SXG 6Z8C 6SX7 6SX5 6SXE 6SXC 6SXG 6Z8C 6SX7	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 5X0M 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 6A90 6A95 6A91 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 6NT3 6NT4 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 7DTD 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 6J8E 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 7W7F 7W77 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 5XSY 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 6AGF 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 6MBA 6MC9 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 6UZ3 6UZ0 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 7K18 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 7FBS 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 7DTC 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 8GZ1 8GZ2 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 8FHD 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 5EK0 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 6N4I 6N4Q 6N4R 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 6J8H 6J8J 6J8I 6J8G 6J8H 6J8J 6J8I 6J8G 6J8H 6J8J 6J8I	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 7K48 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 7XMG 7XMF 7XM9 7XMG 7XMF 7XM9 7XMG 7XMF	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 8G1A 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 8I5X 8J4F 8S9B 8I5Y 8S9C 8I5G 8I5B 8I5X 8J4F 8S9B 8I5Y 8S9C 8I5G 8I5B 8I5X 8J4F 8S9B 8I5Y 8S9C 8I5G	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 8THG 8THH 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_V1.7 (E406K mutant)-β1-β2 complex: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.50 Å** cryo-EM structure in complex with ProTx-II and tetrodotoxin, 3.00 Å: 7W9M in complex with huwentoxin-IV and saxitoxin, S6_IV π conformation, 2.90 Å: 7W9P in complex with huwentoxin-IV and saxitoxin, S6_IV α conformation, 3.00 Å: 7W9T Na_V1.7 (wild type)-β1-β2 complex, 2.20 Å: 7W9K	7W9L	Data File Jmol Viewer 7W9L 7W9M 7W9K 7W9P 7W9T 7W9L 7W9M 7W9K 7W9P 7W9T 7W9L 7W9M 7W9K 7W9P 7W9T	Huang et al. (2022). Huang G, Liu D, Wang W, Wu Q, Chen J, Pan X, Shen H, & Yan N (2022). High-resolution structures of human Nav1.7 reveal gating modulation through α-π helical transition of S6IV. Cell Rep 39 4:110735. PubMed Id: 35476982. doi:10.1016/j.celrep.2022.110735.
*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 7WEL 7WFR 7WFW 7WE4 7WEL 7WFR 7WFW 7WE4 7WEL 7WFR 7WFW	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_V1.8 voltage-gated sodium channel, full-length, apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.12 Å** cryo-EM structure class I, 3.24 Å: 9DBL class II, 3.22 Å: 9DBM with bound peptide Protoxin-I, 2.76 Å: 9DBN	9DBK	Data File Jmol Viewer 9DBK 9DBN 9DBM 9DBL 9DBK 9DBN 9DBM 9DBL 9DBK 9DBN 9DBM 9DBL	Neumann et al. (2025). Neumann B, McCarthy S, & Gonen S (2025). Structural basis of inhibition of human NaV1.8 by the tarantula venom peptide Protoxin-I. Nat Commun 16 1:1459. PubMed Id: 39920100. doi:10.1038/s41467-024-55764-z.
*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 4LTQ 4LTP 4LTR 4LTO 4LTQ 4LTP 4LTR 4LTO 4LTQ 4LTP 4LTR	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 4G80 4G7Y 4G7V 4G80 4G7Y 4G7V 4G80 4G7Y	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 3WKV 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 5OQK 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 5H35 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 5H36 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 5EGI 5EIK 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 5WUD 5WUE 5WUC 5WUD 5WUE 5WUC 5WUD 5WUE	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 5WUF 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 5WTR 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 6IZ0 6IYX 6IZF 6IYZ 6IYU 6IZ1 6IZ0 6IYX 6IZF 6IYZ 6IYU 6IZ1 6IZ0 6IYX 6IZF 6IYZ	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 6IZ3 6IZ6 6IZ4 6IZ5 6IZ3 6IZ6 6IZ4 6IZ5 6IZ3 6IZ6 6IZ4	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 3BEH 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 6EO1 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 6QD4 6QD2 6QD1 6IAX 6CQY 6QD3 6QCZ 6QD0 6I9D 6QD4 6QD2 6QD1 6IAX 6CQY 6QD3 6QCZ 6QD0 6I9D 6QD4 6QD2 6QD1 6IAX 6CQY 6QD3 6QCZ 6QD0	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 5H3O 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 6WEK 6WEL 6WEJ 6WEK 6WEL 6WEJ 6WEK 6WEL	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 7N17 7N16 7N15 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 5V4S 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 7LFX 7LFW 7LFY 7LG1 7LFT 7LFX 7LFW 7LFY 7LG1 7LFT 7LFX 7LFW 7LFY 7LG1	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 7RHG 7RHH 7RHI 7RHJ 7RH9 7RHK 7RHL 7RHG 7RHH 7RHI 7RHJ 7RH9 7RHK 7RHL 7RHG 7RHH 7RHI 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: Bos taurus* E Eukaryota, 3.40 Å** cryo-EM structure	7O4H	Data File Jmol Viewer 7O4H 7O4H 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 8BX7 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 6CJU 6CJT 6CJQ 6CJU 6CJT 6CJQ 6CJU 6CJT	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 7TKT 7TJ6 7TJ5 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 7RU0 7RYR 7RTF 7RYS 7RTJ 7RSH 7RU0 7RYR 7RTF 7RYS 7RTJ 7RSH 7RU0 7RYR 7RTF 7RYS 7RTJ	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.
*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 7T4X 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 7FCV 7XUF 7WSW 7FCV 7XUF 7WSW 7FCV 7XUF	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.
*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 5U6O 5U6P 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 6UQF 6UQG 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.
*HCN3 hyperpolarization-activated channel: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 3.19 Å** cryo-EM structure with bound cAMP, 3.19Å: 8IO0	8INZ	Data File Jmol Viewer 8INZ 8IO0 8INZ 8IO0 8INZ 8IO0	Yu et al. (2024). Yu B, Lu Q, Li J, Cheng X, Hu H, Li Y, Che T, Hua Y, Jiang H, Zhang Y, Xian C, Yang T, Fu Y, Chen Y, Nan W, McCormick PJ, Xiong B, Duan J, Zeng B, Li Y, Fu Y, & Zhang J (2024). Cryo-EM structure of human HCN3 channel and its regulation by cAMP. J Biol Chem 300 6:107288. PubMed Id: 38636662. doi:10.1016/j.jbc.2024.107288.
*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 7NP3 7NP4 7NMN 7NP3 7NP4 7NMN 7NP3 7NP4	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 5VMS 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 7TCP 7TCI 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 6V01 6V00 6UZZ 6V01 6V00 6UZZ 6V01 6V00	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 6MIE 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 7XNN 7XNL 7XNK 7XNI 7XNN 7XNL 7XNK 7XNI 7XNN 7XNL 7XNK	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 8SIN 8SIM 8SIK 8SIN 8SIM 8SIK 8SIN 8SIM	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 7CR2 7CR7 7CR1 7CR3 7CR4 7CR2 7CR7 7CR1 7CR3 7CR4 7CR2 7CR7 7CR1	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.
*KCNQ2 rectifier K⁺ channel in complex with CaM, PIP₂, wild-type, closed state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.70 Å** cryo-EM structure with bound 2 CBDs, closed state 3.00Å: 8J00 with bound 2 CBDs, 1 PIP2, open state 3.10Å: 8J01 with bound 2 HN37, closed state, 2.50Å: 8IZY with bound 2 HN37, 1 PIP2, closed state, 2.70Å: 8J04 with bound 1 HN37, 1 PIP2, open state, 3.30Å: 8W4U F104A mutant, with bound 1 CBD, closed state, 2.70Å: 8J03 F104A mutant, with bound 1 CBD, 1 PIP2, open state, 3.50Å: 8J02	8J05	Data File Jmol Viewer 8J05 8J00 8J04 8IZY 8W4U 8J02 8J03 8J01 8J05 8J00 8J04 8IZY 8W4U 8J02 8J03 8J01 8J05 8J00 8J04 8IZY 8W4U 8J02 8J03 8J01	Ma et al. (2023). Ma D, Zheng Y, Li X, Zhou X, Yang Z, Zhang Y, Wang L, Zhang W, Fang J, Zhao G, Hou P, Nan F, Yang W, Su N, Gao Z, & Guo J (2023). Ligand activation mechanisms of human KCNQ2 channel. Nat Commun 14 1:6632. PubMed Id: 37857637. doi:10.1038/s41467-023-42416-x.
*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 7BYL 7BYM 7BYN 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 7VNR 7VNQ 7VNP 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 5VRE 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 6WCB 6WCC 6WCA 6WC9 6WCB 6WCC 6WCA 6WC9 6WCB 6WCC 6WCA	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 7UNL 7UNM 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 8DHM 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 6HD9 6HDB 6SWR 6HDC 6HDA 6HD8 6HD9 6HDB 6SWR 6HDC 6HDA 6HD8 6HD9 6HDB 6SWR 6HDC 6HDA	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 6C70 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 6V1X 6V1Y 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 7CAL 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 6XIW 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 7CM3 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 7SX3 7SX4 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.
*photoreceptor Cyclic-nucleotide-gated (CNGA3/B3) heterotetrameric channel, apo state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.93 Å** cryo-EM structure	7RHS	Data File Jmol Viewer 7RHS 7RHS 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 (CNGA3/B3) heterotetrameric channel, with bound cGMP, closed-state, in the detergent glycol-diosgenin (GDN): Homo sapiens E Eukaryota (expressed in HEK293 cells), 3.52 Å cryo-EM structure intermediate state 1, 3.62 Å: 8EU3 intermediate state 2, 3.61 Å: 8EUC truncated CNGA3/B3 (A3: residues 152-694, B3: residues 79–809), closed state, in POPG/POPC nanodiscs, 3.11 Å: 8EV8 truncated CNGA3/B3, intermediate state 1, in POPG/POPC nanodiscs, 3.33 Å: 8EV9 truncated CNGA3/B3, intermediate state 2, in POPG/POPC nanodiscs, 3.33 Å: 8EVA truncated CNGA3/B3, pre-open state, in POPG/POPC nanodiscs, 3.60 Å: 8EVB truncated CNGA3/B3, open state, in POPG/POPC nanodiscs, 3.33 Å: 8EVC	8ETP	Data File Jmol Viewer 8ETP 8EV8 8EV9 8EU3 8EVB 8EVA 8EUC 8EVC 8ETP 8EV8 8EV9 8EU3 8EVB 8EVA 8EUC 8EVC 8ETP 8EV8 8EV9 8EU3 8EVB 8EVA 8EUC 8EVC	Hu et al. (2023). Hu Z, Zheng X, & Yang J (2023). Conformational trajectory of allosteric gating of the human cone photoreceptor cyclic nucleotide-gated channel. Nat Commun 14 1:4284. PubMed Id: 37463923. doi:10.1038/s41467-023-39971-8.
*Stelar K⁺ outward rectifying channel (SKOR), wild-type: Arabidopsis thaliana* E Eukaryota (expressed in sf9 cells), 3.10 Å** cryo-EM structure wild-type, different conformation, 3.50 Å: 8JEU L271P & D312N mutant, 3.10 Å: 8JEC	8JET	Data File Jmol Viewer 8JET 8JEU 8JEC 8JET 8JEU 8JEC 8JET 8JEU 8JEC	Li et al. (2023). Li S, Wang Y, Wang C, Zhang Y, Sun D, Zhou P, Tian C, & Liu S (2023). Cryo-EM structure reveals a symmetry reduction of the plant outward-rectifier potassium channel SKOR. Cell Discov 9 1:67. PubMed Id: 37391403. doi:10.1038/s41421-023-00572-w.
*Stelar K⁺ outward rectifying channel (SKOR), wild-type: Arabidopsis thaliana* E Eukaryota (expressed in sf9 cells), 3.10 Å** cryo-EM structure L271P & D312N mutant, 3.40 Å: 8WUI	8WTZ	Data File Jmol Viewer 8WTZ 8WUI 8WTZ 8WUI 8WTZ 8WUI	Gao et al. (2024). Gao X, Xu X, Sun T, Lu Y, Jia Y, Zhou J, Fu P, Zhang Y, & Yang G (2024). Structural changes in the conversion of an Arabidopsis outward-rectifying K+ channel into an inward-rectifying channel. Plant Commun 5 6:100844. PubMed Id: 38341617. doi:10.1016/j.xplc.2024.100844.
*FMRFamide-gated Na⁺ channel (FaNaCs), apo form: Aplysia californica* E Eukaryota (expressed in HEK293 cells), 3.00 Å** cryo-EM structure with bound FMRFamide, 2.90 Å: 7YVB	7YVC	Data File Jmol Viewer 7YVC 7YVB 7YVC 7YVB 7YVC 7YVB	Liu et al. (2023). Liu F, Dang Y, Li L, Feng H, Li J, Wang H, Zhang X, Zhang Z, Ye S, Tian Y, & Chen Q (2023). Structure and mechanism of a neuropeptide-activated channel in the ENaC/DEG superfamily. Nat Chem Biol 19 10:1276-1285. PubMed Id: 37550431. doi:10.1038/s41589-023-01401-7.
*Voltage-gated sodium channel (Na_V), calcium²⁺-bound state: Gephyrocapsa huxleyi* E Eukaryota (expressed in HEK293 cells), 2.60 Å** cryo-EM structure Ca²⁺-unbound state (EGTA), 3.30 Å: 8J7H N-terminal helix removal form, 3.10 Å: 8J7M	8J7F	Data File Jmol Viewer 8J7F 8J7H 8J7M 8J7F 8J7H 8J7M 8J7F 8J7H 8J7M	Chen et al. (2024). Chen H, Xia Z, Dong J, Huang B, Zhang J, Zhou F, Yan R, Shi Y, Gong J, Jiang J, Huang Z, & Jiang D (2024). Structural mechanism of voltage-gated sodium channel slow inactivation. Nat Commun 15 1:3691. PubMed Id: 38693179. doi:10.1038/s41467-024-48125-3.
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 4MW3 4MVZ 4MTG 4MVM 4MTO 4MVU 4MVQ 4MTF 4MVR 4MVO 4MVS 4MW8 4MS2 4MW3 4MVZ 4MTG 4MVM 4MTO 4MVU 4MVQ 4MTF 4MVR 4MVO 4MVS 4MW8 4MS2 4MW3 4MVZ 4MTG 4MVM 4MTO 4MVU 4MVQ 4MTF 4MVR 4MVO 4MVS 4MW8	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 5KLG 5KMH 5KMF 5KLS 5KMD 5KLB 5KLG 5KMH 5KMF 5KLS 5KMD 5KLB 5KLG 5KMH 5KMF 5KLS 5KMD	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 3JBR 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 5GJV 5GJW 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 6JP5 6JPA 6JPB 6JP8 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 7JPK 7JPV 7JPW 7JPX 7JPK 7JPV 7JPW 7JPX 7JPK 7JPV 7JPW	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 8E56 8E57 8E58 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 8WE7 8WE8 8WEA 8WE9 8FHS 8WE6 8WE7 8WE8 8WEA 8WE9 8FHS 8WE6 8WE7 8WE8 8WEA 8WE9 8FHS	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 8EOG 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 8FD7 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 7UHG 7UHF 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 8E59 8E5B 8E5A 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 7MIY 7MIX 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 7VFS 7VFW 7VFU 7VFV 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 8IF4 8IF3 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 8EPL 8EPM 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 7XLQ 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 6KZO 6KZP 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 7WLL 7WLJ 7WLK 7WLI 7WLL 7WLJ 7WLK 7WLI 7WLL 7WLJ 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 4HKR 4HKS 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 6BBH 6BBG 6BBI 6BBF 6BBH 6BBG 6BBI 6BBF 6BBH 6BBG 6BBI	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 6AKI 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 7KR5 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 6YEL 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 4PGU 4PGV 4PGS 4PGW 4PGR 4PGU 4PGV 4PGS 4PGW 4PGR 4PGU 4PGV 4PGS 4PGW	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 6NQ8 6NQ9 6NQ7 6NQ8 6NQ9 6NQ7 6NQ8 6NQ9	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 3J8H 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 3J8E 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 5C30 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 6FOO 6FG3 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 7CF9 6M2W 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 7M6A 7M6L 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 7TDH 7TDI 7K0T 7TDG 7TDJ 7TDH 7TDI 7K0T 7TDG 7TDJ 7TDH 7TDI	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 6WOT 6WOU 6WOV 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 7T64 7T65 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 5GO9 5GOA 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 6JII 6JRS 6JV2 6JIU 6JI0 6JRR 6JIY 6JI8 6JII 6JRS 6JV2 6JIU 6JI0 6JRR 6JIY 6JI8 6JII 6JRS 6JV2 6JIU 6JI0 6JRR 6JIY	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 6JG3 6JGZ 6JH6 6JHN 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 5C33 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 7VMN 7VMM 7VMP 7VMR 7vMS 7VMO 7VMQ 7VML 7VMN 7VMM 7VMP 7VMR 7vMS 7VMO 7VMQ 7VML 7VMN 7VMM 7VMP 7VMR 7vMS 7VMO 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 3JAV 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 7LHE 7LHF 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 8EAR 8EAQ 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 6DRA 6DQN 6DR2 6DQS 6DQV 6DR0 6DRC 6DQJ 6DQZ 6DRA 6DQN 6DR2 6DQS 6DQV 6DR0 6DRC 6DQJ 6DQZ 6DRA 6DQN 6DR2 6DQS 6DQV 6DR0 6DRC	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 6UQK 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 7T3R 7T3T 7T3P 7T3U 7T3Q 7T3R 7T3T 7T3P 7T3U 7T3Q 7T3R 7T3T	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 8TKD 8TKG 8TKH 8TL9 8TKI 8TLA 8TKE 8TKF 8TK8 8TKD 8TKG 8TKH 8TL9 8TKI 8TLA 8TKE 8TKF 8TK8 8TKD 8TKG 8TKH 8TL9 8TKI 8TLA 8TKE 8TKF	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 5ID3 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 6DT0 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 6D7W 6D80 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 6C5W 6C5R 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 6DNF 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 6O58 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 6WDN 6WDO 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 6XJV 6XJX 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 6K7Y 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 7U9Z 7U9T 7UA4 7UA5 7UA9 7U9X 7UA1 7UA3 7U9Q 7U9R 7U9Z 7U9T 7UA4 7UA5 7UA9 7U9X 7UA1 7UA3 7U9Q 7U9R 7U9Z 7U9T 7UA4 7UA5 7UA9 7U9X 7UA1 7UA3	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 6PW5 6PW4 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 3J9P 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 6PQQ 6PQP 6PQO 6PQQ 6PQP 6PQO 6PQQ 6PQP	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 6V9W 6V9X 6V9V 6V9Y 6V9W 6V9X 6V9V 6V9Y 6V9W 6V9X	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 7JUP 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 6CUD 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 7DXD 7DXE 7DXC 7DXB 7DXD 7DXE 7DXC 7DXB 7DXD 7DXE 7DXC	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 6G1K 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 7B05 7B0J 7B1G 7B16 7B0S 7B05 7B0J 7B1G 7B16 7B0S 7B05 7B0J 7B1G 7B16	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 5Z96 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 7D4P 7D4Q 7E4T 7D4P 7D4Q 7E4T 7D4P 7D4Q	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 7WDB 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 7X6I 8GVW 8GVX 7X6C 7X6I 8GVW 8GVX 7X6C 7X6I 8GVW 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 6UZA 6UZ8 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 7DXF 7DXG 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 6CO7 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 6DRK 6DRJ 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 6PKW 6PKX 6D73 6PKV 6PKW 6PKX 6D73 6PKV 6PKW 6PKX 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 6MIZ 6MJ2 6MIX 6MIZ 6MJ2 6MIX 6MIZ 6MJ2	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 6PUO 6PUR 6PUU 6PUS 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 7VQ1 7VQ2 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 7DYS 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 5WP6 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 6BQR 6BQV 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 6BWI 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 6BCO 6BCQ 6BCL 6BCJ 6BCO 6BCQ 6BCL 6BCJ 6BCO 6BCQ 6BCL	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 5ZX5 6BWF 6BWD 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.
*TRPM7 α-kinase and divalent-ion permeable channel, apo state, in MSP2N2 nanodiscs: Mus musculus* E Eukaryota (expressed in HEK293 cells), 2.19 Å** cryo-EM structure with bound naltriben, open state, 2.17 Å: 8SI5 with bound naltriben, closed state, 2.44 Å: 8SI6 in GDN detergent: 2.61 Å: 8Si3 with bound VER155008, in GDN detergent, closed state, 2.59 Å: 8SI7 N1098Q mutant, in GDN detergent, open state, 2.46 Å: 8Si4 N1098Q mutant, with bound VER155008, in GDN detergent, closed state, 2.99 Å: 8SI8 N1098Q mutant, with bound NS8593, in GDN detergent, closed state, 2.91 Å: 8SIA	8SI2	Data File Jmol Viewer 8SI2 8SI8 8SI6 8Si3 8SIA 8SI7 8SI5 8Si4 8SI2 8SI8 8SI6 8Si3 8SIA 8SI7 8SI5 8Si4 8SI2 8SI8 8SI6 8Si3 8SIA 8SI7 8SI5 8Si4	Nadezhdin et al. (2023). Nadezhdin KD, Correia L, Narangoda C, Patel DS, Neuberger A, Gudermann T, Kurnikova MG, Chubanov V, & Sobolevsky AI (2023). Structural mechanisms of TRPM7 activation and inhibition. Nat Commun 14 1:2639. PubMed Id: 37156763. doi:10.1038/s41467-023-38362-3.
*TRPM7 α-kinase and divalent-ion permeable channel with anticancer agent CCT128930 in closed state: Homo sapiens* E Eukaryota (expressed in HEK293 cells), 2.45 Å** cryo-EM structure	8W2L	Data File Jmol Viewer 8W2L 8W2L 8W2L	Nadezhdin et al. (2024). Nadezhdin KD, Correia L, Shalygin A, Aktolun M, Neuberger A, Gudermann T, Kurnikova MG, Chubanov V, & Sobolevsky AI (2024). Structural basis of selective TRPM7 inhibition by the anticancer agent CCT128930. Cell Rep 43 4:114108. PubMed Id: 38615321. doi:10.1016/j.celrep.2024.114108.
*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 6BPQ 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 6NR2 6NR4 6NR3 6NR2 6NR4 6NR3 6NR2 6NR4	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 6O6A 6O72 6O77 6O6R 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 8E4Q 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 8E4N 8E4L 8E4O 8E4M 8E4P 8E4N 8E4L 8E4O 8E4M 8E4P 8E4N 8E4L 8E4O 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.
*TRPM8 cold- & menthol-sensing channel, apo, D-state: Mus musculus* E Eukaryota (expressed in HEK293 cells), 3.30 Å** cryo-EM structure in complex with: TC-I 2014, 2.91 Å: 9B6E AMG2850, 3.42 Å: 9B6F AMTB, 2.81 Å: 9B6G TC-I 2014 and C3, 2.76 Å: 9BGH Ca²⁺ and PIP₂, 3.53 Å: 9B6J Ca²⁺ only, 4.13 Å: 9B6K	9B6D	Data File Jmol Viewer 9B6D 9B6E 9B6F 9B6K 9BGH 9B6G 9B6J 9B6D 9B6E 9B6F 9B6K 9BGH 9B6G 9B6J 9B6D 9B6E 9B6F 9B6K 9BGH 9B6G 9B6J	Yin et al. (2024). Yin Y, Park CG, Zhang F, G Fedor J, Feng S, Suo Y, Im W, & Lee SY (2024). Mechanisms of sensory adaptation and inhibition of the cold and menthol receptor TRPM8. Sci Adv 10 31:eadp2211. PubMed Id: 39093967. doi:10.1126/sciadv.adp2211.
*TRPM8 cold- & menthol-sensing channel, closed state: Homo sapiens* E Eukaryota (expressed in S. frugiperda), 2.65 Å** cryo-EM structure	8BDC	Data File Jmol Viewer 8BDC 8BDC 8BDC	Palchevskyi et al. (2023). Palchevskyi S, Czarnocki-Cieciura M, Vistoli G, Gervasoni S, Nowak E, Beccari AR, Nowotny M, & Talarico C (2023). Structure of human TRPM8 channel. Commun Biol 6 1:1065. PubMed Id: 37857704. doi:10.1038/s42003-023-05425-6.
*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 5WPT 5WPQ 5WPV 5WPT 5WPQ 5WPV 5WPT 5WPQ	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 7SQ8 7SQ7 7SQ9 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 5W3S 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 6AYF 6AYG 6AYE 6AYF 6AYG 6AYE 6AYF 6AYG	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 3J5P 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 3J5Q 3J5R 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 5IRZ 5IRX 5IS0 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 7LPD 7LPC 7LPA 7LPB 7LPE 7LP9 7LPD 7LPC 7LPA 7LPB 7LPE 7LP9 7LPD 7LPC 7LPA 7LPB 7LPE	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 7MZB 7MZ7 7MZA 7MZC 7L2N 7MZ5 7MZ9 7MZ6 7L2I 7L2U 7L2J 7L2W 72LR 7MZE 7L2M 7L2O 7L2T 7L2K 7L2X 7L2H 7L2L 7L2S 7L2V 7MZD 7L2P 7MZB 7MZ7 7MZA 7MZC 7L2N 7MZ5 7MZ9 7MZ6 7L2I 7L2U 7L2J 7L2W 72LR 7MZE 7L2M 7L2O 7L2T 7L2K 7L2X 7L2H 7L2L 7L2S 7L2V 7MZD 7L2P 7MZB <

from the Stephen White laboratory at UC Irvine

and the Bridge Institute at USC

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