9SW6
Structure of the Mvh-Hdr-Fmd complex of Methanothermobacter marburgensis (composite structure)
Summary for 9SW6
| Entry DOI | 10.2210/pdb9sw6/pdb |
| EMDB information | 55299 |
| Descriptor | H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit A, Molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C, Polyferredoxin protein MvhB, ... (24 entities in total) |
| Functional Keywords | oxidoreductase, hydrogenase, dehydrogenase, polyferredoxin |
| Biological source | Methanothermobacter marburgensis More |
| Total number of polymer chains | 17 |
| Total formula weight | 697997.84 |
| Authors | San Segundo-Acosta, P.,Murphy, B.J. (deposition date: 2025-10-04, release date: 2026-04-29, Last modification date: 2026-09-30) |
| Primary citation | Segundo-Acosta, P.S.,Nomura, S.,Fernandes-Queiroz, J.P.,Protasov, E.,Kahnt, J.,Kaneko, M.,Hochberg, G.,Shima, S.,Murphy, B.J. Diversity of electron-bifurcating CO 2 -fixing supercomplexes in methanogens. Sci Adv, 12:eaed3711-eaed3711, 2026 Cited by PubMed Abstract: In the hydrogenotrophic methanogenic pathway, formylmethanofuran dehydrogenase (Fmd) reduces and fixes CO, driven by low-potential electrons provided by electron-bifurcating heterodisulfide reductase (Hdr) complexed with electron-donating proteins such as Mvh hydrogenase. Here, we report the structure of a C2-symmetric (Mvh-Hdr)-Fmd supercomplex from a Class I methanogen, , which is architecturally different from the previously reported ring-shaped D3-symmetric supercomplex of a methanogen belonging to phylogenetically distinct Class II methanogens. In this C2-symmetric form, the redox active sites of Hdr and Fmd are connected by two MvhB polyferredoxins, whose branching electron paths appear to be available for electron transfer to/from other partners. The ancestral form was likely C2 symmetric, whereas D3-symmetric supercomplexes were acquired by horizontal gene transfer, a transition probably helpful for growth in substrate-poor environments. PubMed: 42748252DOI: 10.1126/sciadv.aed3711 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
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