8RCG
W-formate dehydrogenase M405S from Desulfovibrio vulgaris
Summary for 8RCG
| Entry DOI | 10.2210/pdb8rcg/pdb |
| Descriptor | Formate dehydrogenase, alpha subunit, selenocysteine-containing, Formate dehydrogenase, beta subunit, putative, 2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE, ... (10 entities in total) |
| Functional Keywords | formate, co2, molybdenum and tungsten enzymes, dmso reductase family, electron transport, oxidoreductase |
| Biological source | Nitratidesulfovibrio vulgaris str. Hildenborough More |
| Total number of polymer chains | 2 |
| Total formula weight | 140024.57 |
| Authors | Vilela-Alves, G.,Manuel, R.R.,Pereira, I.C.,Romao, M.J.,Mota, C. (deposition date: 2023-12-06, release date: 2024-05-08, Last modification date: 2024-11-20) |
| Primary citation | Vilela-Alves, G.,Rebelo Manuel, R.,Pedrosa, N.,Cardoso Pereira, I.A.,Romao, M.J.,Mota, C. Structural and biochemical characterization of the M405S variant of Desulfovibrio vulgaris formate dehydrogenase. Acta Crystallogr.,Sect.F, 80:98-106, 2024 Cited by PubMed Abstract: Molybdenum- or tungsten-dependent formate dehydrogenases have emerged as significant catalysts for the chemical reduction of CO 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 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 reduction, together with an increased sensitivity to oxygen inactivation. PubMed: 38699971DOI: 10.1107/S2053230X24003911 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.005 Å) |
Structure validation
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