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PDBsum entry 5odc
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Oxidoreductase
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PDB id
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5odc
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Contents |
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653 a.a.
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291 a.a.
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184 a.a.
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138 a.a.
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298 a.a.
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447 a.a.
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173 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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Methanogenic heterodisulfide reductase (hdrabc-Mvhagd) uses two noncubane [4fe-4s] clusters for reduction.
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Authors
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T.Wagner,
J.Koch,
U.Ermler,
S.Shima.
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Ref.
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Science, 2017,
357,
699-703.
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PubMed id
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Abstract
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In methanogenic archaea, the carbon dioxide (CO2) fixation and
methane-forming steps are linked through the heterodisulfide reductase
(HdrABC)-[NiFe]-hydrogenase (MvhAGD) complex that uses flavin-based electron
bifurcation to reduce ferredoxin and the heterodisulfide of coenzymes M and B.
Here, we present the structure of the native heterododecameric HdrABC-MvhAGD
complex at 2.15-angstrom resolution. HdrB contains two noncubane [4Fe-4S]
clusters composed of fused [3Fe-4S]-[2Fe-2S] units sharing 1 iron (Fe) and 1
sulfur (S), which were coordinated at the CCG motifs. Soaking experiments showed
that the heterodisulfide is clamped between the two noncubane [4Fe-4S] clusters
and homolytically cleaved, forming coenzyme M and B bound to each iron.
Coenzymes are consecutively released upon one-by-one electron transfer. The
HdrABC-MvhAGD atomic model serves as a structural template for numerous HdrABC
homologs involved in diverse microbial metabolic pathways.
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