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5ODH

Heterodisulfide reductase / [NiFe]-hydrogenase complex from Methanothermococcus thermolithotrophicus soaked with heterodisulfide for 3.5 minutes

Summary for 5ODH
Entry DOI10.2210/pdb5odh/pdb
DescriptorHeterodisulfide reductase, subunit A, FLAVIN-ADENINE DINUCLEOTIDE, Non-cubane [4Fe-4S]-cluster, ... (19 entities in total)
Functional Keywordsheterodisulfide reductase, [nife]-hydrogenase, fes cluster, ferredoxin, ccg motif, methanogenesis, flavoprotein, flavin-based electron bifurcation, [2fe-2s] cluster, macromolecular complex, anaerobic, thioredoxin, metabolism, oxidoreductase
Biological sourceMethanothermococcus thermolithotrophicus DSM 2095
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Total number of polymer chains12
Total formula weight467281.96
Authors
Wagner, T.,Koch, J.,Ermler, U.,Shima, S. (deposition date: 2017-07-05, release date: 2017-08-30, Last modification date: 2024-10-23)
Primary citationWagner, T.,Koch, J.,Ermler, U.,Shima, S.
Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction.
Science, 357:699-703, 2017
Cited by
PubMed Abstract: In methanogenic archaea, the carbon dioxide (CO) 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.
PubMed: 28818947
DOI: 10.1126/science.aan0425
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

237735

數據於2025-06-18公開中

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