We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
1yew
From Proteopedia
Revision as of 21:28, 29 September 2014 by OCA (Talk | contribs)
1yew is a 9 chain structure with sequence from Methylococcus capsulatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Lieberman RL, Rosenzweig AC. Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature. 2005 Mar 10;434(7030):177-82. Epub 2005 Jan 26. PMID:15674245 doi:http://dx.doi.org/10.1038/nature03311
