1YEW
Crystal structure of particulate methane monooxygenase
Summary for 1YEW
| Entry DOI | 10.2210/pdb1yew/pdb |
| Descriptor | particulate methane monooxygenase, B subunit, particulate methane monooxygenase, A subunit, particulate methane monooxygenase subunit C2, ... (6 entities in total) |
| Functional Keywords | membrane protein, methane, beta barrel, oxidoreductase |
| Biological source | Methylococcus capsulatus More |
| Cellular location | Membrane ; Multi- pass membrane protein : Q607G3 |
| Total number of polymer chains | 9 |
| Total formula weight | 314571.68 |
| Authors | Lieberman, R.L.,Rosenzweig, A.C. (deposition date: 2004-12-28, release date: 2005-02-08, Last modification date: 2024-02-14) |
| Primary citation | Lieberman, R.L.,Rosenzweig, A.C. Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature, 434:177-182, 2005 Cited by PubMed Abstract: 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. PubMed: 15674245DOI: 10.1038/nature03311 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.801 Å) |
Structure validation
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