1e6y

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Revision as of 17:29, 29 October 2007

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spinqualitylabelsall models 1e6y, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

METHYL-COENZYME M REDUCTASE FROM METHANOSARCINA BARKERI

Overview

The nickel enzyme methyl-coenzyme M reductase (MCR) catalyzes the terminal, step of methane formation in the energy metabolism of all methanogenic, archaea. In this reaction methyl-coenzyme M and coenzyme B are converted, to methane and the heterodisulfide of coenzyme M and coenzyme B. The, crystal structures of methyl-coenzyme M reductase from Methanosarcina, barkeri (growth temperature optimum, 37 degrees C) and Methanopyrus, kandleri (growth temperature optimum, 98 degrees C) were determined and, compared with the known structure of MCR from Methanobacterium, thermoautotrophicum (growth temperature optimum, 65 degrees C). The active, sites of MCR from M. barkeri and M. kandleri were almost identical to that, of M. thermoautotrophicum and predominantly occupied by coenzyme M and, ... [(full description)]

About this Structure

1E6Y is a [Protein complex] structure of sequences from [Methanosarcina barkeri] with F43, TP7, COM and GOL as [ligands]. Full crystallographic information is available from [OCA].

Reference

Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation., Grabarse W, Mahlert F, Shima S, Thauer RK, Ermler U, J Mol Biol. 2000 Oct 20;303(2):329-44. PMID:11023796

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