5ODH
Heterodisulfide reductase / [NiFe]-hydrogenase complex from Methanothermococcus thermolithotrophicus soaked with heterodisulfide for 3.5 minutes
Summary for 5ODH
Entry DOI | 10.2210/pdb5odh/pdb |
Descriptor | Heterodisulfide reductase, subunit A, FLAVIN-ADENINE DINUCLEOTIDE, Non-cubane [4Fe-4S]-cluster, ... (19 entities in total) |
Functional Keywords | heterodisulfide reductase, [nife]-hydrogenase, fes cluster, ferredoxin, ccg motif, methanogenesis, flavoprotein, flavin-based electron bifurcation, [2fe-2s] cluster, macromolecular complex, anaerobic, thioredoxin, metabolism, oxidoreductase |
Biological source | Methanothermococcus thermolithotrophicus DSM 2095 More |
Total number of polymer chains | 12 |
Total formula weight | 467281.96 |
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 citation | Wagner, 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: 28818947DOI: 10.1126/science.aan0425 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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