8rcg

W-formate dehydrogenase M405S from Desulfovibrio vulgaris

spinqualitylabelsall models 8rcg, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8rcg is a 2 chain structure with sequence from Desulfovibrio vulgaris str. Hildenborough. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.005Å Ligands: EDO, GOL, H2S, MGD, PEG, SF4, W Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Molybdenum- or tungsten-dependent formate dehydrogenases have emerged as significant catalysts for the chemical reduction of CO(2) to formate, with biotechnological applications envisaged in climate-change mitigation. The role of Met405 in the active site of Desulfovibrio vulgaris formate dehydrogenase AB (DvFdhAB) has remained elusive. However, its proximity to the metal site and the conformational change that it undergoes between the resting and active forms suggests a functional role. In this work, the M405S variant was engineered, which allowed the active-site geometry in the absence of methionine S(delta) interactions with the metal site to be revealed and the role of Met405 in catalysis to be probed. This variant displayed reduced activity in both formate oxidation and CO(2) reduction, together with an increased sensitivity to oxygen inactivation. Structural and biochemical characterization of the M405S variant of Desulfovibrio vulgaris formate dehydrogenase.,Vilela-Alves G, Rebelo Manuel R, Pedrosa N, Cardoso Pereira IA, Romao MJ, Mota C Acta Crystallogr F Struct Biol Commun. 2024 May 1;80(Pt 5):98-106. doi: , 10.1107/S2053230X24003911. Epub 2024 May 1. PMID:38699971 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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