1mhz
From Proteopedia
(New page: 200px<br /> <applet load="1mhz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mhz, resolution 2.7Å" /> '''METHANE MONOOXYGENAS...) |
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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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MHZ OCA]]. | + | 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/Oxidoreductase Oxidoreductase]], 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== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:48:14 2007'' |
Revision as of 06:43, 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 [Oxidoreductase], 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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