Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7EV9

cryoEM structure of particulate methane monooxygenase associated with Cu(I)

7EV9 の概要
エントリーDOI10.2210/pdb7ev9/pdb
EMDBエントリー31325
分子名称Particulate methane monooxygenase alpha subunit, Particulate methane monooxygenase beta subunit, Ammonia monooxygenase/methane monooxygenase, subunit C family protein, ... (4 entities in total)
機能のキーワードparticulate methane monooxygenase, copper contained, oxidoreductase
由来する生物種Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
詳細
タンパク質・核酸の鎖数9
化学式量合計314767.56
構造登録者
Chang, W.H.,Lin, H.H.,Tsai, I.K.,Huang, S.H.,Chung, S.C.,Tu, I.P.,Yu, S.F.,Chan, S.I. (登録日: 2021-05-20, 公開日: 2021-07-21, 最終更新日: 2024-06-05)
主引用文献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: 34170126
DOI: 10.1021/jacs.1c04082
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.6 Å)
構造検証レポート
Validation report summary of 7ev9
検証レポート(詳細版)ダウンロードをダウンロード

247035

件を2026-01-07に公開中

PDB statisticsPDBj update infoContact PDBjnumon