8CM4
W-formate dehydrogenase C872A from Desulfovibrio vulgaris - exposed to oxygen
Summary for 8CM4
| Entry DOI | 10.2210/pdb8cm4/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 | Desulfovibrio vulgaris str. Hildenborough More |
| Total number of polymer chains | 4 |
| Total formula weight | 279536.63 |
| Authors | Vilela-Alves, G.,Mota, C.,Klymanska, K.,Oliveira, A.R.,Manuel, R.R.,Pereira, I.C.,Romao, M.J. (deposition date: 2023-02-17, release date: 2023-09-27, Last modification date: 2024-01-03) |
| Primary citation | Oliveira, A.R.,Mota, C.,Vilela-Alves, G.,Manuel, R.R.,Pedrosa, N.,Fourmond, V.,Klymanska, K.,Leger, C.,Guigliarelli, B.,Romao, M.J.,Cardoso Pereira, I.A. An allosteric redox switch involved in oxygen protection in a CO 2 reductase. Nat.Chem.Biol., 20:111-119, 2024 Cited by PubMed Abstract: Metal-dependent formate dehydrogenases reduce CO with high efficiency and selectivity, but are usually very oxygen sensitive. An exception is Desulfovibrio vulgaris W/Sec-FdhAB, which can be handled aerobically, but the basis for this oxygen tolerance was unknown. Here we show that FdhAB activity is controlled by a redox switch based on an allosteric disulfide bond. When this bond is closed, the enzyme is in an oxygen-tolerant resting state presenting almost no catalytic activity and very low formate affinity. Opening this bond triggers large conformational changes that propagate to the active site, resulting in high activity and high formate affinity, but also higher oxygen sensitivity. We present the structure of activated FdhAB and show that activity loss is associated with partial loss of the metal sulfido ligand. The redox switch mechanism is reversible in vivo and prevents enzyme reduction by physiological formate levels, conferring a fitness advantage during O exposure. PubMed: 37985883DOI: 10.1038/s41589-023-01484-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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