8QQK

Cryo-EM structure of E. coli cytochrome bo3 quinol oxidase assembled in peptidiscs

8QQK の概要

• エントリーDOI: 10.2210/pdb8qqk/pdb
• EMDBエントリー: 18594
• 分子名称: Cytochrome bo(3) ubiquinol oxidase subunit 1, Cytochrome bo(3) ubiquinol oxidase subunit 2, Cytochrome bo(3) ubiquinol oxidase subunit 3, ... (9 entities in total)
• 機能のキーワード: e. coli, membrane protein, ni-nta resin, cytochrome bo3 quinol oxidase; ubiquinone-8 release; peptidisc; single particle analysis; cryo-em
• 由来する生物種: Escherichia coli BL21(DE3); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 150094.95

構造登録者

Gao, Y.,Zhang, Y.,Hakke, S.,Peters, P.J.,Ravelli, R.B.G. (登録日: 2023-10-05, 公開日: 2024-04-24, 最終更新日: 2024-05-01)

主引用文献

Gao, Y.,Zhang, Y.,Hakke, S.,Mohren, R.,Sijbers, L.J.P.M.,Peters, P.J.,Ravelli, R.B.G.
Cryo-EM structure of cytochrome bo 3 quinol oxidase assembled in peptidiscs reveals an "open" conformation for potential ubiquinone-8 release.
Biochim Biophys Acta Bioenerg, 1865:149045-149045, 2024

PubMed Abstract: Cytochrome bo quinol oxidase belongs to the heme‑copper-oxidoreductase (HCO) superfamily, which is part of the respiratory chain and essential for cell survival. While the reaction mechanism of cyt bo has been studied extensively over the last decades, specific details about its substrate binding and product release have remained unelucidated due to the lack of structural information. Here, we report a 2.8 Å cryo-electron microscopy structure of cyt bo from Escherichia coli assembled in peptidiscs. Our structural model shows a conformation for amino acids 1-41 of subunit I different from all previously published structures while the remaining parts of this enzyme are similar. Our new conformation shows a "U-shape" assembly in contrast to the transmembrane helix, named "TM0", in other reported structural models. However, TM0 blocks ubiquinone-8 (reaction product) release, suggesting that other cyt bo conformations should exist. Our structural model presents experimental evidence for an "open" conformation to facilitate substrate/product exchange. This work helps further understand the reaction cycle of this oxidase, which could be a benefit for potential drug/antibiotic design for health science.

PubMed: 38614453
DOI: 10.1016/j.bbabio.2024.149045

実験手法

ELECTRON MICROSCOPY (2.8 Å)