6TG9
Cryo-EM Structure of NADH reduced form of NAD+-dependent Formate Dehydrogenase from Rhodobacter capsulatus
Summary for 6TG9
| Entry DOI | 10.2210/pdb6tg9/pdb |
| EMDB information | 10495 |
| Descriptor | Formate dehydrogenase subunit alpha, FLAVIN MONONUCLEOTIDE, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, ... (11 entities in total) |
| Functional Keywords | molybdoenzyme, formate oxidation, nad+-dependent, oxidoreductase |
| Biological source | Rhodobacter capsulatus More |
| Total number of polymer chains | 8 |
| Total formula weight | 370358.64 |
| Authors | Wendler, P.,Radon, C.,Mittelstaedt, G. (deposition date: 2019-11-15, release date: 2020-04-22, Last modification date: 2024-05-22) |
| Primary citation | Radon, C.,Mittelstadt, G.,Duffus, B.R.,Burger, J.,Hartmann, T.,Mielke, T.,Teutloff, C.,Leimkuhler, S.,Wendler, P. Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase. Nat Commun, 11:1912-1912, 2020 Cited by PubMed Abstract: Metal-containing formate dehydrogenases (FDH) catalyse the reversible oxidation of formate to carbon dioxide at their molybdenum or tungsten active site. They display a diverse subunit and cofactor composition, but structural information on these enzymes is limited. Here we report the cryo-electron microscopic structures of the soluble Rhodobacter capsulatus FDH (RcFDH) as isolated and in the presence of reduced nicotinamide adenine dinucleotide (NADH). RcFDH assembles into a 360 kDa dimer of heterotetramers revealing a putative interconnection of electron pathway chains. In the presence of NADH, the RcFDH structure shows charging of cofactors, indicative of an increased electron load. PubMed: 32313256DOI: 10.1038/s41467-020-15614-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.24 Å) |
Structure validation
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