8OVC
Respiratory supercomplex (III2-IV2) from Mycobacterium smegmatis
8OVC の概要
| エントリーDOI | 10.2210/pdb8ovc/pdb |
| EMDBエントリー | 17210 |
| 分子名称 | Cytochrome bc1 complex cytochrome c subunit, Uncharacterized protein MSMEG_4692/MSMEI_4575, LpqE protein, ... (29 entities in total) |
| 機能のキーワード | respiratory supercomplex, membrane protein, actinobacteria, electron transport |
| 由来する生物種 | Mycolicibacterium smegmatis 詳細 |
| タンパク質・核酸の鎖数 | 28 |
| 化学式量合計 | 766827.18 |
| 構造登録者 | Kovalova, T.,Krol, S.,Sjostrand, D.,Riepl, D.,Gamiz-Hernandez, A.,Brzezinski, P.,Kaila, V.,Hogbom, M. (登録日: 2023-04-25, 公開日: 2024-07-17, 最終更新日: 2025-10-01) |
| 主引用文献 | Riepl, D.,Gamiz-Hernandez, A.P.,Kovalova, T.,Krol, S.M.,Mader, S.L.,Sjostrand, D.,Hogbom, M.,Brzezinski, P.,Kaila, V.R.I. Long-range charge transfer mechanism of the III 2 IV 2 mycobacterial supercomplex. Nat Commun, 15:5276-5276, 2024 Cited by PubMed Abstract: Aerobic life is powered by membrane-bound redox enzymes that shuttle electrons to oxygen and transfer protons across a biological membrane. Structural studies suggest that these energy-transducing enzymes operate as higher-order supercomplexes, but their functional role remains poorly understood and highly debated. Here we resolve the functional dynamics of the 0.7 MDa IIIIV obligate supercomplex from Mycobacterium smegmatis, a close relative of M. tuberculosis, the causative agent of tuberculosis. By combining computational, biochemical, and high-resolution (2.3 Å) cryo-electron microscopy experiments, we show how the mycobacterial supercomplex catalyses long-range charge transport from its menaquinol oxidation site to the binuclear active site for oxygen reduction. Our data reveal proton and electron pathways responsible for the charge transfer reactions, mechanistic principles of the quinone catalysis, and how unique molecular adaptations, water molecules, and lipid interactions enable the proton-coupled electron transfer (PCET) reactions. Our combined findings provide a mechanistic blueprint of mycobacterial supercomplexes and a basis for developing drugs against pathogenic bacteria. PubMed: 38902248DOI: 10.1038/s41467-024-49628-9 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.8 Å) |
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