1mhz
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1MHZ is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Methylosinus_trichosporium Methylosinus trichosporium]] with FE as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1MHZ is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Methylosinus_trichosporium Methylosinus trichosporium]] with FE as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Methane_monooxygenase Methane monooxygenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25]]. Structure known Active Site: FE2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MHZ OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9070438 9070438] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9070438 9070438] | ||
| + | [[Category: Methane monooxygenase]] | ||
[[Category: Methylosinus trichosporium]] | [[Category: Methylosinus trichosporium]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:49:14 2007'' |
Revision as of 08:44, 30 October 2007
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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
1MHZ 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
Page seeded by OCA on Tue Oct 30 10:49:14 2007
