1mhy

From Proteopedia

Revision as of 13:38, 30 October 2007

METHANE MONOOXYGENASE HYDROXYLASE

Overview

Methane monooxygenase (MMO), found in aerobic methanotrophic bacteria, catalyzes the O2-dependent conversion of methane to methanol. The soluble, form of the enzyme (sMMO) consists of three components: a reductase, a, regulatory "B" component (MMOB), and a hydroxylase component (MMOH), which, contains a hydroxo-bridged dinuclear iron cluster. Two genera of, methanotrophs, termed Type X and Type II, which differ markedly in, cellular and metabolic characteristics, are known to produce the sMMO. The, structure of MMOH from the Type X methanotroph Methylococcus capsulatus, Bath (MMO Bath) has been reported recently. Two different structures were, found for the essential diiron cluster, depending upon the temperature at, which the diffraction data were collected. In order to extend the, ... [(full description)]

About this Structure

1MHY is a [Protein complex] structure of sequences from [Methylosinus trichosporium] with FE as [ligand]. Active as [Methane monooxygenase], with EC number [1.14.13.25]. Structure known Active Site: FE2. Full crystallographic information is available from [OCA].

Reference

Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b., Elango N, Radhakrishnan R, Froland WA, Wallar BJ, Earhart CA, Lipscomb JD, Ohlendorf DH, Protein Sci. 1997 Mar;6(3):556-68. PMID:9070438

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