4jjg | pdb_00004jjg

Crystal structure of FE-hydrogenase from methanothermobacter marburgensis in complex with toluenesulfonylmethylisocyanide

spinqualitylabelsall models 4jjg, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4jjg is a 2 chain structure with sequence from Methanothermobacter marburgensis str. Marburg. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: IC9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HMD_METTM Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT. Publication Abstract from PubMed Inhibition mechanism: Isocyanides strongly inhibit [Fe]-hydrogenase. X-ray crystallography and X-ray absorption spectroscopy revealed that the isocyanide binds to the trans position, versus the acyl carbon of the Fe center, and is covalently bound to the pyridinol hydroxy oxygen. These results also indicated that the hydroxy group is essential for H2 activation. Crystal Structures of [Fe]-Hydrogenase in Complex with Inhibitory Isocyanides: Implications for the H -Activation Site.,Tamura H, Salomone-Stagni M, Fujishiro T, Warkentin E, Meyer-Klaucke W, Ermler U, Shima S Angew Chem Int Ed Engl. 2013 Jul 22. doi: 10.1002/anie.201305089. PMID:23873755 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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