4PI2
Crystal structure of particulate methane monooxygenase from Methylocystis sp. ATCC 49242 (Rockwell) soaked in zinc
Summary for 4PI2
| Entry DOI | 10.2210/pdb4pi2/pdb |
| Related | 4PHZ 4PI0 |
| Descriptor | unknown peptide, Particulate methane monooxygenase subunit A, Particulate methane monooxygenase subunit B, ... (7 entities in total) |
| Functional Keywords | bacterial proteins, binding sites, copper, zinc, methylocystaceae, oxygenases, protein binding, oxidoreductase |
| Biological source | Methylocystis sp. ATCC 49242 More |
| Total number of polymer chains | 12 |
| Total formula weight | 317688.90 |
| Authors | Sirajuddin, S.,Rosenzweig, A.C. (deposition date: 2014-05-07, release date: 2014-06-25, Last modification date: 2024-10-23) |
| Primary citation | Sirajuddin, S.,Barupala, D.,Helling, S.,Marcus, K.,Stemmler, T.L.,Rosenzweig, A.C. Effects of zinc on particulate methane monooxygenase activity and structure. J.Biol.Chem., 289:21782-21794, 2014 Cited by PubMed Abstract: Particulate methane monooxygenase (pMMO) is a membrane-bound metalloenzyme that oxidizes methane to methanol in methanotrophic bacteria. Zinc is a known inhibitor of pMMO, but the details of zinc binding and the mechanism of inhibition are not understood. Metal binding and activity assays on membrane-bound pMMO from Methylococcus capsulatus (Bath) reveal that zinc inhibits pMMO at two sites that are distinct from the copper active site. The 2.6 Å resolution crystal structure of Methylocystis species strain Rockwell pMMO reveals two previously undetected bound lipids, and metal soaking experiments identify likely locations for the two zinc inhibition sites. The first is the crystallographic zinc site in the pmoC subunit, and zinc binding here leads to the ordering of 10 previously unobserved residues. A second zinc site is present on the cytoplasmic side of the pmoC subunit. Parallels between these results and zinc inhibition studies of several respiratory complexes suggest that zinc might inhibit proton transfer in pMMO. PubMed: 24942740DOI: 10.1074/jbc.M114.581363 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.33 Å) |
Structure validation
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