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PDBsum entry 4pi2
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Oxidoreductase
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PDB id
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4pi2
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Contents |
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19 a.a.
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20 a.a.
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244 a.a.
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390 a.a.
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25 a.a.
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228 a.a.
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PDB id:
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| Name: |
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Oxidoreductase
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Title:
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Crystal structure of particulate methane monooxygenase from methylocystis sp. Atcc 49242 (rockwell) soaked in zinc
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Structure:
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Unknown peptide. Chain: d, h, n. Particulate methane monooxygenase subunit a. Chain: f, j, b. Synonym: pmoa. Particulate methane monooxygenase subunit b. Chain: e, a, i. Synonym: pmob. Particulate methane monooxygenase subunit c.
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Source:
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Methylocystis sp. Atcc 49242. Organism_taxid: 622637. Organism_taxid: 622637
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Resolution:
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3.33Å
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R-factor:
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0.228
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R-free:
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0.282
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Authors:
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S.Sirajuddin,A.C.Rosenzweig
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Key ref:
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S.Sirajuddin
et al.
(2014).
Effects of zinc on particulate methane monooxygenase activity and structure.
J Biol Chem,
289,
21782-21794.
PubMed id:
DOI:
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Date:
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07-May-14
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Release date:
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25-Jun-14
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PROCHECK
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Headers
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References
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No UniProt id for this chain
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No UniProt id for this chain
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No UniProt id for this chain
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No UniProt id for this chain
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Enzyme class:
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Chains F, E, A, I, J, B:
E.C.1.14.18.3
- methane monooxygenase (particulate).
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Reaction:
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methane + a quinol + O2 = methanol + a quinone + H2O
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methane
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+
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quinol
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+
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O2
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=
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methanol
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+
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quinone
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+
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H2O
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Cofactor:
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Cu cation
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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J Biol Chem
289:21782-21794
(2014)
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PubMed id:
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Effects of zinc on particulate methane monooxygenase activity and structure.
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S.Sirajuddin,
D.Barupala,
S.Helling,
K.Marcus,
T.L.Stemmler,
A.C.Rosenzweig.
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ABSTRACT
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Particulate methane monooxygenase (pMMO) is a membrane-bound metalloenzyme that
oxidizes methane to methanol in methanotrophic bacteria. Zinc is a known
inhibitor of pMMO, but the details of zinc binding and the mechanism of
inhibition are not understood. Metal binding and activity assays on
membrane-bound pMMO from Methylococcus capsulatus (Bath) reveal that zinc
inhibits pMMO at two sites that are distinct from the copper active site. The
2.6 Å resolution crystal structure of Methylocystis species strain Rockwell
pMMO reveals two previously undetected bound lipids, and metal soaking
experiments identify likely locations for the two zinc inhibition sites. The
first is the crystallographic zinc site in the pmoC subunit, and zinc binding
here leads to the ordering of 10 previously unobserved residues. A second zinc
site is present on the cytoplasmic side of the pmoC subunit. Parallels between
these results and zinc inhibition studies of several respiratory complexes
suggest that zinc might inhibit proton transfer in pMMO.
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