30GK
W-formate dehydrogenase from Nitratidesulfovibrio vulgaris (Desulfovibrio vulgaris) - Same Batch SSX 2025/04/01
Summary for 30GK
| Entry DOI | 10.2210/pdb30gk/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 | 140965.69 |
| Authors | Vilela-Alves, G.,Martins, G.,von Stetten, D.,Mehrabi, P.,Pereira, I.C.,Romao, M.J.,Pearson, A.R.,Mota, C. (deposition date: 2026-04-23, release date: 2026-08-19) |
| Primary citation | Vilela-Alves, G.,Martins, G.,von Stetten, D.,Mehrabi, P.,Pereira, I.A.C.,Romao, M.J.,Pearson, A.R.,Mota, C. Room-temperature crystal structure of a metal-dependent W-formate dehydrogenase by serial synchrotron crystallography. Acta Crystallogr D Struct Biol, 2026 Cited by PubMed Abstract: Metal-dependent formate dehydrogenases (Fdhs) are a promising research target in efforts to mitigate climate change by developing active, efficient, selective and safe industrial catalysts for CO reduction. Here, we report the room-temperature (RT) serial synchrotron X-ray crystallography (SSX) structure of Nitratidesulfovibrio vulgaris formate dehydrogenase AB and compare this structure with previously reported cryogenic structures. The comparison reveals structural differences likely arising from the absence of cryoprotectants, differences in data-collection temperature and the much lower radiation dose accumulated by each crystal during the SSX experiments. The RT-SSX structure provides the first step towards time-resolved serial crystallography experiments targeting possible catalytic intermediates in order to fully understand the catalytic mechanism of metal-dependent Fdhs. PubMed: 42572941DOI: 10.1107/S2059798326006923 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.953 Å) |
Structure validation
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