8cm4

W-formate dehydrogenase C872A from Desulfovibrio vulgaris - exposed to oxygen

spinqualitylabelsall models 8cm4, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8cm4 is a 4 chain structure with sequence from Desulfovibrio vulgaris str. Hildenborough. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: GOL, H2S, MGD, NO3, PEG, W Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q72EJ1_NITV2 Publication Abstract from PubMed Metal-dependent formate dehydrogenases reduce CO(2) 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(2) exposure. An allosteric redox switch involved in oxygen protection in a CO(2) reductase.,Oliveira AR, Mota C, Vilela-Alves G, Manuel RR, Pedrosa N, Fourmond V, Klymanska K, Leger C, Guigliarelli B, Romao MJ, Cardoso Pereira IA Nat Chem Biol. 2024 Jan;20(1):111-119. doi: 10.1038/s41589-023-01484-2. Epub 2023 , Nov 20. PMID:37985883 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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