8BQG
W-formate dehydrogenase from Desulfovibrio vulgaris - Soaking with Formate 1 min
Summary for 8BQG
| Entry DOI | 10.2210/pdb8bqg/pdb |
| Descriptor | Formate dehydrogenase, alpha subunit, selenocysteine-containing, FORMIC ACID, Formate dehydrogenase, beta subunit, putative, ... (11 entities in total) |
| Functional Keywords | formate, co2, molybdenum and tungsten enzymes, dmso reductase family, oxidoreductase |
| Biological source | Desulfovibrio vulgaris str. Hildenborough More |
| Total number of polymer chains | 2 |
| Total formula weight | 142576.67 |
| Authors | Vilela-Alves, G.,Mota, C.,Oliveira, A.R.,Manuel, R.R.,Pereira, I.C.,Romao, M.J. (deposition date: 2022-11-21, release date: 2023-01-18, Last modification date: 2024-10-16) |
| Primary citation | Vilela-Alves, G.,Manuel, R.R.,Oliveira, A.R.,Pereira, I.C.,Romao, M.J.,Mota, C. Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation. Int J Mol Sci, 24:-, 2022 Cited by PubMed Abstract: Metal-dependent formate dehydrogenases (Fdh) catalyze the reversible conversion of CO 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 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 FdhAB in crystals was confirmed by reduction and reoxidation structural studies. PubMed: 36613918DOI: 10.3390/ijms24010476 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.946 Å) |
Structure validation
Download full validation report
