1yew

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[[Image:1yew.gif|left|200px]]<br /><applet load="1yew" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yew.gif|left|200px]]
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caption="1yew, resolution 2.801&Aring;" />
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'''Crystal structure of particulate methane monooxygenase'''<br />
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{{Structure
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|PDB= 1yew |SIZE=350|CAPTION= <scene name='initialview01'>1yew</scene>, resolution 2.801&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=CUA:DINUCLEAR COPPER ION'>CUA</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal structure of particulate methane monooxygenase'''
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==Overview==
==Overview==
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==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 <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].
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1YEW is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YEW OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15674245 15674245]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15674245 15674245]
[[Category: Methylococcus capsulatus]]
[[Category: Methylococcus capsulatus]]
[[Category: Methylococcus capsulatus str. bath]]
[[Category: Methylococcus capsulatus str. bath]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:22:00 2008''

Revision as of 13:22, 20 March 2008


PDB ID 1yew

Drag the structure with the mouse to rotate
, resolution 2.801Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



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. 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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