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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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References listed in PDB file
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Key reference
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Title
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Effects of zinc on particulate methane monooxygenase activity and structure.
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Authors
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S.Sirajuddin,
D.Barupala,
S.Helling,
K.Marcus,
T.L.Stemmler,
A.C.Rosenzweig.
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Ref.
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J Biol Chem, 2014,
289,
21782-21794.
[DOI no: ]
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PubMed id
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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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