8bql

W-formate dehydrogenase from Desulfovibrio vulgaris - Co-crystallized with Formate and Reoxidized by exposure to air for 12 min

spinqualitylabelsall models 8bql, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8bql 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 1.906Å Ligands: EDO, GOL, H2S, MGD, W Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q72EJ1_NITV2 Publication Abstract from PubMed Metal-dependent formate dehydrogenases (Fdh) catalyze the reversible conversion of CO(2) to formate, with unrivalled efficiency and selectivity. However, the key catalytic aspects of these enzymes remain unknown, preventing us from fully benefiting from their capabilities in terms of biotechnological applications. Here, we report a time-resolved characterization by X-ray crystallography of the Desulfovibrio vulgaris Hildenborough SeCys/W-Fdh during formate oxidation. The results allowed us to model five different intermediate structures and to chronologically map the changes occurring during enzyme reduction. Formate molecules were assigned for the first time to populate the catalytic pocket of a Fdh. Finally, the redox reversibility of DvFdhAB in crystals was confirmed by reduction and reoxidation structural studies. Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation.,Vilela-Alves G, Manuel RR, Oliveira AR, Pereira IC, Romao MJ, Mota C Int J Mol Sci. 2022 Dec 28;24(1):476. doi: 10.3390/ijms24010476. PMID:36613918 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Formate dehydrogenase 3D structures

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