7DEG

Cryo-EM structure of a heme-copper terminal oxidase dimer provides insights into its catalytic mechanism

7DEG の概要

• エントリーDOI: 10.2210/pdb7deg/pdb
• EMDBエントリー: 30657
• 分子名称: Cytochrome c oxidase subunit I, DINUCLEAR COPPER ION, Cytochrome oxidase subunit IIa, ... (10 entities in total)
• 機能のキーワード: electron cryo-microscopy, heme-copper oxidase, cytochrome c oxidase dimer, aquifex aeolicus, naphthoquinone, oxidoreductase
• 由来する生物種: Aquifex aeolicus (strain VF5); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 183295.85

構造登録者

Fei, S.,Hartmut, M.,Yun, Z.,Guoliang, Z.,Shuangbo, Z. (登録日: 2020-11-04, 公開日: 2021-08-04, 最終更新日: 2025-09-17)

主引用文献

Zhu, G.,Zeng, H.,Zhang, S.,Juli, J.,Tai, L.,Zhang, D.,Pang, X.,Zhang, Y.,Lam, S.M.,Zhu, Y.,Peng, G.,Michel, H.,Sun, F.
The Unusual Homodimer of a Heme-Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors.
Angew.Chem.Int.Ed.Engl., 60:13323-13330, 2021

PubMed Abstract: The heme-copper oxidase superfamily comprises cytochrome c and ubiquinol oxidases. These enzymes catalyze the transfer of electrons from different electron donors onto molecular oxygen. A B-family cytochrome c oxidase from the hyperthermophilic bacterium Aquifex aeolicus was discovered previously to be able to use both cytochrome c and naphthoquinol as electron donors. Its molecular mechanism as well as the evolutionary significance are yet unknown. Here we solved its 3.4 Å resolution electron cryo-microscopic structure and discovered a novel dimeric structure mediated by subunit I (CoxA2) that would be essential for naphthoquinol binding and oxidation. The unique structural features in both proton and oxygen pathways suggest an evolutionary adaptation of this oxidase to its hyperthermophilic environment. Our results add a new conceptual understanding of structural variation of cytochrome c oxidases in different species.

PubMed: 33665933
DOI: 10.1002/anie.202016785

実験手法

ELECTRON MICROSCOPY (3.4 Å)