6elq

Carbon Monoxide Dehydrogenase IV from Carboxydothermus hydrogenoformans

spinqualitylabelsall models 6elq, resolution 2.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6elq is a 3 chain structure with sequence from Carboxydothermus hydrogenoformans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.52Å Ligands: BF8, SF4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3AE44_CARHZ Publication Abstract from PubMed CO dehydrogenases (CODHs) catalyse the reversible conversion between CO and CO2 . Genomic analysis indicated that the metabolic functions of CODHs vary. The genome of Carboxydothermus hydrogenoformans encodes five CODHs (CODH-I-V), of which CODH-IV is found in a gene cluster near a peroxide-reducing enzyme. Our kinetic and crystallographic experiments reveal that CODH-IV differs from other CODHs in several characteristic properties: it has a very high affinity for CO, oxidizes CO at diffusion-limited rate over a wide range of temperatures, and is more tolerant to oxygen than CODH-II. Thus, our observations support the idea that CODH-IV is a CO scavenger in defence against oxidative stress and highlight that CODHs are more diverse in terms of reactivity than expected. CODH-IV: A High-Efficiency CO-Scavenging CO Dehydrogenase with Resistance to O2.,Domnik L, Merrouch M, Goetzl S, Jeoung JH, Leger C, Dementin S, Fourmond V, Dobbek H Angew Chem Int Ed Engl. 2017 Nov 27;56(48):15466-15469. doi:, 10.1002/anie.201709261. Epub 2017 Nov 2. PMID:29024326 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Carbon monoxide dehydrogenase 3D structures

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