9CL2
Particulate methane monooxygenase in washed native membranes
This is a non-PDB format compatible entry.
Summary for 9CL2
| Entry DOI | 10.2210/pdb9cl2/pdb |
| EMDB information | 45659 |
| Descriptor | Particulate methane monooxygenase gamma subunit, Particulate methane monooxygenase beta subunit, Particulate methane monooxygenase alpha subunit, ... (6 entities in total) |
| Functional Keywords | membrane protein, metalloenzyme, monooxygenase, oxidoreductase |
| Biological source | Methylococcus capsulatus str. Bath More |
| Total number of polymer chains | 9 |
| Total formula weight | 336625.61 |
| Authors | Tucci, F.J.,Rosenzweig, A.C. (deposition date: 2024-07-10, release date: 2025-01-08, Last modification date: 2025-01-15) |
| Primary citation | Tucci, F.J.,Rosenzweig, A.C. Structures of methane and ammonia monooxygenases in native membranes. Proc.Natl.Acad.Sci.USA, 122:e2417993121-e2417993121, 2025 Cited by PubMed Abstract: Methane- and ammonia-oxidizing bacteria play key roles in the global carbon and nitrogen cycles, respectively. These bacteria use homologous copper membrane monooxygenases to accomplish the defining chemical transformations of their metabolisms: the oxidations of methane to methanol by particulate methane monooxygenase (pMMO) and ammonia to hydroxylamine by ammonia monooxygenase (AMO), enzymes of prime interest for applications in mitigating climate change. However, investigations of these enzymes have been hindered by the need for disruptive detergent solubilization prior to structure determination, confounding studies of pMMO and precluding studies of AMO. Here, we overcome these challenges by using cryoEM to visualize pMMO and AMO directly in their native membrane arrays at 2.4 to 2.8 Å resolution. These structures reveal details of the copper centers, numerous bound lipids, and previously unobserved components, including identifiable and distinct supernumerary helices interacting with pMMO and AMO, suggesting a widespread role for these helices in copper membrane monooxygenases. Comparisons between these structures, their metallocofactors, and their unexpected protein-protein interactions highlight features that may govern activity or the formation of higher-order arrays in native membranes. The ability to obtain molecular insights within the native membrane will enable further understanding of these environmentally important enzymes. PubMed: 39739801DOI: 10.1073/pnas.2417993121 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.42 Å) |
Structure validation
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