1hbn
From Proteopedia
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Revision as of 13:29, 30 October 2007
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METHYL-COENZYME M REDUCTASE
Overview
Methyl-coenzyme M reductase (MCR) catalyzes the final reaction of the, energy conserving pathway of methanogenic archaea in which methylcoenzyme, M and coenzyme B are converted to methane and the heterodisulfide, CoM-S-S-CoB. It operates under strictly anaerobic conditions and contains, the nickel porphinoid F430 which is present in the nickel (I) oxidation, state in the active enzyme. The known crystal structures of the inactive, nickel (II) enzyme in complex with coenzyme M and coenzyme B, (MCR-ox1-silent) and in complex with the heterodisulfide CoM-S-S-CoB, (MCR-silent) were now refined at 1.16 A and 1.8 A resolution, respectively. The atomic resolution structure of MCR-ox1-silent describes, the exact geometry of the cofactor F430, of the active site residues and, of the modified amino ... [(full description)]
About this Structure
1HBN is a [Protein complex] structure of sequences from [Methanothermobacter thermautotrophicus] with ZN, MG, NA, CL, F43, TP7, COM and GOL as [ligands]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5 and AC6. Full crystallographic information is available from [OCA].
Reference
On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding., Grabarse W, Mahlert F, Duin EC, Goubeaud M, Shima S, Thauer RK, Lamzin V, Ermler U, J Mol Biol. 2001 May 25;309(1):315-30. PMID:11491299
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Categories: Methanothermobacter thermautotrophicus | Protein complex | Ermler, U. | Grabarse, W. | CL | COM | F43 | GOL | MG | NA | TP7 | ZN | Biological methanogenesis | Methanogenesis | Ni-enzyme | Oxidoreductase
