1yew

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(New page: 200px<br /><applet load="1yew" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yew, resolution 2.801&Aring;" /> '''Crystal structure o...)
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[[Image:1yew.gif|left|200px]]<br /><applet load="1yew" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1yew, resolution 2.801&Aring;" />
caption="1yew, resolution 2.801&Aring;" />
'''Crystal structure of particulate methane monooxygenase'''<br />
'''Crystal structure of particulate methane monooxygenase'''<br />
==Overview==
==Overview==
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Particulate methane monooxygenase (pMMO) is an integral membrane, metalloenzyme that catalyses the conversion of methane to methanol., Knowledge of how pMMO performs this extremely challenging chemistry may, have an impact on the use of methane as an alternative energy source by, facilitating the development of new synthetic catalysts. We have, determined the structure of pMMO from the methanotroph Methylococcus, capsulatus (Bath) to a resolution of 2.8 A. The enzyme is a trimer with an, alpha3beta3gamma3 polypeptide arrangement. Two metal centres, modelled as, mononuclear copper and dinuclear copper, are located in soluble regions of, each pmoB subunit, which resembles cytochrome c oxidase subunit II. A, third metal centre, occupied by zinc in the crystal, is located within the, membrane. The structure provides new insight into the molecular details of, biological methane oxidation.
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Particulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme that catalyses the conversion of methane to methanol. Knowledge of how pMMO performs this extremely challenging chemistry may have an impact on the use of methane as an alternative energy source by facilitating the development of new synthetic catalysts. We have determined the structure of pMMO from the methanotroph Methylococcus capsulatus (Bath) to a resolution of 2.8 A. The enzyme is a trimer with an alpha3beta3gamma3 polypeptide arrangement. Two metal centres, modelled as mononuclear copper and dinuclear copper, are located in soluble regions of each pmoB subunit, which resembles cytochrome c oxidase subunit II. A third metal centre, occupied by zinc in the crystal, is located within the membrane. The structure provides new insight into the molecular details of biological methane oxidation.
==About this Structure==
==About this Structure==
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1YEW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus] and [http://en.wikipedia.org/wiki/Methylococcus_capsulatus_str._bath Methylococcus capsulatus str. bath] with ZN, CU and CUA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YEW OCA].
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1YEW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus] and [http://en.wikipedia.org/wiki/Methylococcus_capsulatus_str._bath Methylococcus capsulatus str. bath] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=CUA:'>CUA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YEW OCA].
==Reference==
==Reference==
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[[Category: Methylococcus capsulatus str. bath]]
[[Category: Methylococcus capsulatus str. bath]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Lieberman, R.L.]]
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[[Category: Lieberman, R L.]]
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[[Category: Rosenzweig, A.C.]]
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[[Category: Rosenzweig, A C.]]
[[Category: CU]]
[[Category: CU]]
[[Category: CUA]]
[[Category: CUA]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:03:11 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:39 2008''

Revision as of 14:04, 21 February 2008


1yew, resolution 2.801Å

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Crystal structure of particulate methane monooxygenase

Overview

Particulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme that catalyses the conversion of methane to methanol. Knowledge of how pMMO performs this extremely challenging chemistry may have an impact on the use of methane as an alternative energy source by facilitating the development of new synthetic catalysts. We have determined the structure of pMMO from the methanotroph Methylococcus capsulatus (Bath) to a resolution of 2.8 A. The enzyme is a trimer with an alpha3beta3gamma3 polypeptide arrangement. Two metal centres, modelled as mononuclear copper and dinuclear copper, are located in soluble regions of each pmoB subunit, which resembles cytochrome c oxidase subunit II. A third metal centre, occupied by zinc in the crystal, is located within the membrane. The structure provides new insight into the molecular details of biological methane oxidation.

About this Structure

1YEW is a Protein complex structure of sequences from Methylococcus capsulatus and Methylococcus capsulatus str. bath with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane., Lieberman RL, Rosenzweig AC, Nature. 2005 Mar 10;434(7030):177-82. Epub 2005 Jan 26. PMID:15674245

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