Structural highlights
6tga is a 8 chain structure with sequence from "rhodonostoc_capsulatum"_molisch_1907 "rhodonostoc capsulatum" molisch 1907. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , , |
| Gene: | U715_16550 ("Rhodonostoc capsulatum" Molisch 1907), U715_16555 ("Rhodonostoc capsulatum" Molisch 1907), U715_16560 ("Rhodonostoc capsulatum" Molisch 1907), U715_16540 ("Rhodonostoc capsulatum" Molisch 1907) |
| Activity: | Formate dehydrogenase, with EC number 1.2.1.2 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
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.
Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase.,Radon C, Mittelstadt G, Duffus BR, Burger J, Hartmann T, Mielke T, Teutloff C, Leimkuhler S, Wendler P Nat Commun. 2020 Apr 20;11(1):1912. doi: 10.1038/s41467-020-15614-0. PMID:32313256[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Radon C, Mittelstadt G, Duffus BR, 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. 2020 Apr 20;11(1):1912. doi: 10.1038/s41467-020-15614-0. PMID:32313256 doi:http://dx.doi.org/10.1038/s41467-020-15614-0
