1yew: Difference between revisions

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[[Image:1yew.gif|left|200px]]
{{Seed}}
[[Image:1yew.png|left|200px]]


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{{STRUCTURE_1yew|  PDB=1yew  |  SCENE=  }}  
{{STRUCTURE_1yew|  PDB=1yew  |  SCENE=  }}  


'''Crystal structure of particulate methane monooxygenase'''
===Crystal structure of particulate methane monooxygenase===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_15674245}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_15674245}}


==About this Structure==
==About this Structure==
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[[Category: Methane]]
[[Category: Methane]]
[[Category: Zinc]]
[[Category: Zinc]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:14:05 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:49:01 2008''

Revision as of 05:49, 29 July 2008

File:1yew.png

Template:STRUCTURE 1yew

Crystal structure of particulate methane monooxygenase

Template:ABSTRACT PUBMED 15674245

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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