7EV9
cryoEM structure of particulate methane monooxygenase associated with Cu(I)
Summary for 7EV9
| Entry DOI | 10.2210/pdb7ev9/pdb |
| EMDB information | 31325 |
| Descriptor | Particulate methane monooxygenase alpha subunit, Particulate methane monooxygenase beta subunit, Ammonia monooxygenase/methane monooxygenase, subunit C family protein, ... (4 entities in total) |
| Functional Keywords | particulate methane monooxygenase, copper contained, oxidoreductase |
| Biological source | Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) More |
| Total number of polymer chains | 9 |
| Total formula weight | 314767.56 |
| Authors | Chang, W.H.,Lin, H.H.,Tsai, I.K.,Huang, S.H.,Chung, S.C.,Tu, I.P.,Yu, S.F.,Chan, S.I. (deposition date: 2021-05-20, release date: 2021-07-21, Last modification date: 2024-06-05) |
| Primary citation | Chang, W.H.,Lin, H.H.,Tsai, I.K.,Huang, S.H.,Chung, S.C.,Tu, I.P.,Yu, S.S.,Chan, S.I. Copper Centers in the Cryo-EM Structure of Particulate Methane Monooxygenase Reveal the Catalytic Machinery of Methane Oxidation. J.Am.Chem.Soc., 143:9922-9932, 2021 Cited by PubMed Abstract: The particulate methane monooxygenase (pMMO) is the first enzyme in the C1 metabolic pathway in methanotrophic bacteria. As this enzyme converts methane into methanol efficiently near room temperature, it has become the paradigm for developing an understanding of this difficult C1 chemistry. pMMO is a membrane-bound protein with three subunits (PmoB, PmoA, and PmoC) and 12-14 coppers distributed among different sites. X-ray crystal structures that have revealed only three mononuclear coppers at three sites have neither disclosed the location of the active site nor the catalytic mechanism of the enzyme. Here we report a cyro-EM structure of -pMMO from (Bath) at 2.5 Å, and develop quantitative electrostatic-potential profiling to scrutinize the nonprotein densities for signatures of the copper cofactors. Our results confirm a mononuclear Cu at the site, resolve two Cus at the site, and uncover additional Cu clusters at the PmoA/PmoC interface within the membrane ( site) and in the water-exposed -terminal subdomain of the PmoB ( clusters). These findings complete the minimal set of copper factors required for catalytic turnover of pMMO, offering a glimpse of the catalytic machinery for methane oxidation according to the chemical principles underlying the mechanism proposed earlier. PubMed: 34170126DOI: 10.1021/jacs.1c04082 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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