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8UEM

The CryoEM structure of the high affinity Carbon monoxide dehydrogenase from Mycobacterium smegmatis

8UEM の概要
エントリーDOI10.2210/pdb8uem/pdb
関連するPDBエントリー8UDS
EMDBエントリー42164
分子名称Carbon monoxide dehydrogenase (Large chain), CoxL, Carbon monoxide dehydrogenase medium chain, [2Fe-2S] binding domain protein, ... (8 entities in total)
機能のキーワードcarbon monoxide dehydrogenase, mocu, mycobacterium smegmatis, high affinity, trace gas scavenging, oxidoreductase
由来する生物種Mycolicibacterium smegmatis MC2 155
詳細
タンパク質・核酸の鎖数6
化学式量合計273749.43
構造登録者
Grinter, R.,Venugopal, H.,Greening, C.,Gillett, D. (登録日: 2023-10-02, 公開日: 2024-10-16, 最終更新日: 2025-07-09)
主引用文献Kropp, A.,Gillett, D.L.,Venugopal, H.,Gonzalvez, M.A.,Lingford, J.P.,Jain, S.,Barlow, C.K.,Zhang, J.,Greening, C.,Grinter, R.
Quinone extraction drives atmospheric carbon monoxide oxidation in bacteria.
Nat.Chem.Biol., 21:1058-1068, 2025
Cited by
PubMed Abstract: Diverse bacteria and archaea use atmospheric CO as an energy source for long-term survival. Bacteria use [MoCu]-CO dehydrogenases (Mo-CODH) to convert atmospheric CO to carbon dioxide, transferring the obtained electrons to the aerobic respiratory chain. However, it is unknown how these enzymes oxidize CO at low concentrations and interact with the respiratory chain. Here, we use cryo-electron microscopy and structural modeling to show how Mo-CODH (CoxSML) from Mycobacterium smegmatis interacts with its partner, the membrane-bound menaquinone-binding protein CoxG. We provide electrochemical, biochemical and genetic evidence that Mo-CODH transfers CO-derived electrons to the aerobic respiratory chain through CoxG. Lastly, we show that Mo-CODH and CoxG genetically and structurally associate in diverse bacteria and archaea. These findings reveal the basis of the biogeochemically and ecologically important process of atmospheric CO oxidation, while demonstrating that long-range quinone transport is a general mechanism of energy conservation, which convergently evolved on multiple occasions.
PubMed: 39881213
DOI: 10.1038/s41589-025-01836-0
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (1.85 Å)
構造検証レポート
Validation report summary of 8uem
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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