6t7j

As-isolated Ni-free crystal structure of carbon monoxide dehydrogenase from Thermococcus sp. AM4 produced without CooC maturase

spinqualitylabelsall models 6t7j, resolution 2.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6t7j is a 3 chain structure with sequence from Thermococcus sp. AM4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.43Å Ligands: BU3, CIT, FES, MSK, PEG, PO4, SF4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7R5K0_9EURY CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).[ARBA:ARBA00002452] Publication Abstract from PubMed Ni-containing CO-dehydrogenases (CODHs) allow some microorganisms to couple ATP synthesis to CO oxidation, or to use either CO or CO2 as a source of carbon. The recent detailed characterizations of some of them have evidenced a great diversity in terms of catalytic properties and resistance to O2. In an effort to increase the number of available CODHs, we have heterologously produced in Desulfovibrio fructosovorans, purified and characterized the two CooS-type CODHs (CooS1 and CooS2) from the hyperthermophilic archaeon Thermococcus sp. AM4 (Tc). We have also crystallized CooS2, which is coupled in vivo to a hydrogenase. CooS1 and CooS2 are homodimers, and harbour five metalloclusters: two [Ni4Fe-4S] C clusters, two [4Fe-4S] B clusters and one interfacial [4Fe-4S] D cluster. We show that both are dependent on a maturase, CooC1 or CooC2, which is interchangeable. The homologous protein CooC3 does not allow Ni insertion in either CooS. The two CODHs from Tc have similar properties: they can both oxidize and produce CO. The Michaelis constants (Km) are in the microM range for CO and in the mM range (CODH 1) or above (CODH 2) for CO2. Product inhibition is observed only for CO2 reduction, consistent with CO2 binding being much weaker than CO binding. The two enzymes are rather O2 sensitive (similarly to CODH II from Carboxydothermus hydrogenoformans), and react more slowly with O2 than any other CODH for which these data are available. The two CO-dehydrogenases of Thermococcus sp. AM4.,Benvenuti M, Meneghello M, Guendon C, Jacq-Bailly A, Jeoung JH, Dobbek H, Leger C, Fourmond V, Dementin S Biochim Biophys Acta Bioenerg. 2020 Jul 1;1861(7):148188. doi:, 10.1016/j.bbabio.2020.148188. Epub 2020 Mar 21. PMID:32209322 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Carbon monoxide dehydrogenase 3D structures

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