6T7J
As-isolated Ni-free crystal structure of carbon monoxide dehydrogenase from Thermococcus sp. AM4 produced without CooC maturase
Summary for 6T7J
| Entry DOI | 10.2210/pdb6t7j/pdb |
| Descriptor | Carbon monoxide dehydrogenase, IRON/SULFUR CLUSTER, FE2/S2 (INORGANIC) CLUSTER, ... (9 entities in total) |
| Functional Keywords | ni-free cluster c, co dehydrogenase, oxidoreductase |
| Biological source | Thermococcus sp. AM4 |
| Total number of polymer chains | 3 |
| Total formula weight | 208091.01 |
| Authors | Dobbek, H.,Jeoung, J.-H. (deposition date: 2019-10-22, release date: 2020-11-18, Last modification date: 2024-01-24) |
| Primary citation | Benvenuti, M.,Meneghello, M.,Guendon, C.,Jacq-Bailly, A.,Jeoung, J.H.,Dobbek, H.,Leger, C.,Fourmond, V.,Dementin, S. The two CO-dehydrogenases of Thermococcus sp. AM4. Biochim Biophys Acta Bioenerg, 1861:148188-148188, 2020 Cited by PubMed Abstract: Ni-containing CO-dehydrogenases (CODHs) allow some microorganisms to couple ATP synthesis to CO oxidation, or to use either CO or CO 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 O. 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 (K) are in the microM range for CO and in the mM range (CODH 1) or above (CODH 2) for CO. Product inhibition is observed only for CO reduction, consistent with CO binding being much weaker than CO binding. The two enzymes are rather O sensitive (similarly to CODH II from Carboxydothermus hydrogenoformans), and react more slowly with O than any other CODH for which these data are available. PubMed: 32209322DOI: 10.1016/j.bbabio.2020.148188 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.43 Å) |
Structure validation
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