Monoamine Oxidase Structures Updated
New Structure:
Prokaryotic pentameric ligand-gated ion channel
Unique proteins* in database = 157.
Number of coördinate files in database = 368.
*Includes 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.
| Protein | PDB Code | Get File | Get Image |
Reference (links are to PubMed) |
|---|---|---|---|---|
| MONOTOPIC MEMBRANE PROTEINS | ||||
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Prostaglandin H2 synthase-1: Ram (Ovine) seminal vesicle, 3.5 Å
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Cyclooxygenase-2: Mus Musculus, 3.0Å
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Squalene-hopene cyclase: Alicyclobacillus acidocaldarius, 2.0 Å
2SQC is space group P43212. 3SQC, 2.8 Å is P3221. |
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Monoamine Oxidase B: Human mitochondrial outer membrane (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 outside of the membrane. |
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Monoamine Oxidase B with bound Isatin: Human mitochondrial outer membrane (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 |
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Monoamine Oxidase A with bound Harmine: Human mitochondrial outer membrane (expressed in S. cerevisiae),
2.20 Å
G110A mutant with bound Harmine, 2.17 Å: 2Z5Y |
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Monoamine Oxidase A: Rat mitochondrial outer membrane (expressed in S. cerevisiae), 3.20 Å
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Fatty acid amide hydrolase: Rattus norvegicus, 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. |
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Flavoprotein-ubiquinone oxidoreductase (ETF-QO) with bound UQ: Sus scrofa, 2.5 Å
UQ-free structure, 2.6 Å: 2GMJ |
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Peptidoglycan Glycosyltransferase: Staphylococccus aureus, 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. |
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Signal Peptide Peptidase (SppA), native protein: Eschericia coli, 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. Also listed under Intramembrane Proteases. |
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Glycerol-3-phosphate dehydrogenase (GlpD, native):
Escherichia coli, 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 Also listed under Respiratory Proteins. |
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| TRANSMEMBRANE PROTEINS: BETA-BARREL | ||||
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Beta-Barrel Membrane Proteins: Multimeric
(Porins and Relatives) |
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Porin: Rhodobacter capsulatus, 1.8 Å
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Porin: Rhodopeudomonas blastica, 1.96 Å
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OmpK36 osmoporin: Klebsiella pneumoniae, 3.2 Å
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Omp32 anion-selective porin: Comamonas acidovorans, 2.1 Å
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Omp32 anion-selective porin: Delftia acidovorans, 1.5 Å
With bound malate, 1.45 Å: 2FGQ |
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OmpF Matrix Porin: Escherichia coli, 2.4 Å
Note: Also see BtuB with bound colicin E3 R-domain, below. |
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OmpC Osmoporin: Escherichia coli, 2.0 Å
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OmpG *monomeric* porin: Escherichia coli, 2.3 Å
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OmpG *monomeric* porin in open state: Escherichia coli, 2.3 Å
OmpG in closed state, 2.73 Å: 2IWW |
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OmpG *monomeric* porin: Escherichia coli, NMR Structure (DPC micelles)
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PhoE: Escherihia coli, 3.0 Å
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Maltoporin: Salmonella typhimurium, 2.4 Å
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Maltoporin: Escherichia coli, 3.1 Å
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ScrY sucrose-specific porin: Salmonella typhimurium, 2.4 Å
Complexed Form, 1AOT. Uncomplexed form, 1A0S. |
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MspA mycobacterial porin: Mycobacterium smegmatis, 2.5 Å
Homooctamer |
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OprP phosphate-specific transporter: Pseudomonas aeruginosa, 1.9 Å
Contains a novel nine-residue arginine ladder |
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OprD basic amino acid uptake channel: Pseudomonas aeruginosa, 2.9 Å
Like OprP, contains a basic ladder |
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| Beta-Barrel Membrane Proteins: Monomeric/Dimeric | ||||
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TolC outer membrane protein: Escherichia coli, 2.1 Å
NOTE: Functional protein is a homotrimer. Each monomer contributes 4 strands to a single barrel. |
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VceC outer membrane protein: Vibrio cholerae, 1.8 Å
NOTE: Functional protein is a homotrimer. Each monomer contributes 4 strands to a single barrel. |
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OprM drug discharge outer membrane protein: Pseudomonas aeruginosa, 2.56 Å
NOTE: Functional protein is a homotrimer. Each monomer contributes 4 strands to a single barrel. |
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apo BtuB by in meso crystallization: Escherichia coli, 1.95 Å
NOTE: Crystals were prepared from cubic phase lipids. This is the first β-barrel protein prepared by this method. |
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BtuB with bound colicin E3 R-domain: Escherichia coli, 2.75 Å
NOTE: The 135-residue coiled-coil R-domain is believed to deliver the colicin to OmpF (above). |
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BtuB with bound colicin E2 R-domain: Escherichia coli, 3.50 Å
NOTE: The 135-residue coiled-coil R-domain is believed to deliver the colicin to OmpF or OmpC (above). |
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BtuB in complex with TonB: Escherichia coli, 2.1 Å
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Colicin I receptor Cir in complex with Colicin Ia binding domain: Escherichia coli, 2.5 Å
Cir Colicin I receptor alone, 2.65 Å: 2HDF |
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OmpA: Escherichia coli, x-ray diffraction, 2.5 Å
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OmpA: Escherichia coli, NMR (in DPC micelles)
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OmpA with four shortened loops: Escherichia coli, NMR (in DHPC micelles)
Called β-barrel platform (BBP) |
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OmpT outer membrane protease: Escherichia coli, 2.6 Å
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OmpW outer membrane protein: Escherichia coli, 2.7 Å
2F1V is orthorhomibic form. Trigonal form, 3.0 Å: 2F1T |
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OmpX: Escherichia coli, 1.9 Å
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OmpX: Escherichia coli, NMR (DPC micelles, with H-bond constraints)
For structure without H-bond constraints, see 1Q9G |
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OmpLA outer membrane phospholipase A monomer: Escherichia coli, 2.17 Å
Dimer, 2.10 Å: 1QD6
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OpcA adhesin protein: Neisseria meningitidis, 2.0 Å
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NspA surface protein: Neisseria meningitidis, 2.55 Å
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NalP autotransporter translocator domain: Neisseria meningitidis, 2.60 Å
p6122 space group. See also 1UYO, C2221 space group, 3.2 Å resolution. |
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Hia1022-1098 trimeric autotransporter: Haemophilus influenzae, 2.0 Å
Hia992-1098, 2.3 Å: 2GR7 |
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EspP autotransporter, postcleavage state: Escherichia coli, 2.7 Å
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PagP outer membrane palimitoyl transferease: Escherichia coli, NMR
1MM4 is Structure in DPC micelles. Structure in OG micelles: 1MM5 |
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PagP outer membrane palimitoyl transferease: Escherichia coli, x-ray, 1.9 Å
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FadL long-chain fatty acid transporter: Escherichia coli, 2.6 Å
1T16 is from Monoclinic crystals. From hexagonal crystals, 2.8 Å: 1T1L |
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FhuA, Ferrichrome-iron receptor without ligand: Escherichia coli, 2.7 Å
With ligand: 1BY5 | ||||