30GJ

W-formate dehydrogenase from Nitratidesulfovibrio vulgaris (Desulfovibrio vulgaris) - Ambient temperature, Serial crystallography

Summary for 30GJ

• Entry DOI: 10.2210/pdb30gj/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, ... (7 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: 139532.13

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

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: 42572941
DOI: 10.1107/S2059798326006923

Experimental method

X-RAY DIFFRACTION (1.93 Å)