9SW3

Structure of the MvhAGD-HdrABC dimer of M. marburgensis under state 2 substate b (composite structure)

Summary for 9SW3

• Entry DOI: 10.2210/pdb9sw3/pdb
• EMDB information: 55296
• Descriptor: H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit A, FE2/S2 (INORGANIC) CLUSTER, CARBONMONOXIDE-(DICYANO) IRON, ... (12 entities in total)
• Functional Keywords: oxidoreductase, hydrogenase, dehydrogenase, polyferredoxin
• Biological source: Methanothermobacter marburgensis; More
• Total number of polymer chains: 6
• Total formula weight: 234683.41

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

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: 42748252
DOI: 10.1126/sciadv.aed3711

Experimental method

ELECTRON MICROSCOPY (3.25 Å)