7NYV

Respiratory complex I from Escherichia coli - conformation 3

7NYV の概要

• エントリーDOI: 10.2210/pdb7nyv/pdb
• 関連するPDBエントリー: 7NYH 7NYR 7NYU 7NZ1
• EMDBエントリー: 12652 12653 12654 12655 12661 13291
• 分子名称: NADH-quinone oxidoreductase subunit B, NADH-quinone oxidoreductase subunit H, NADH-quinone oxidoreductase subunit M, ... (17 entities in total)
• 機能のキーワード: nadh:ubiquinone reductase (h+-translocating), oxidative phosphorylation, electron transport
• 由来する生物種: Escherichia coli B; 詳細
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 544313.77

構造登録者

Kolata, P.,Efremov, R.G. (登録日: 2021-03-23, 公開日: 2021-08-25)

主引用文献

Kolata, P.,Efremov, R.G.
Structure of Escherichia coli respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation.
Elife, 10:-, 2021

PubMed Abstract: Respiratory complex I is a multi-subunit membrane protein complex that reversibly couples NADH oxidation and ubiquinone reduction with proton translocation against transmembrane potential. Complex I from is among the best functionally characterized complexes, but its structure remains unknown, hindering further studies to understand the enzyme coupling mechanism. Here, we describe the single particle cryo-electron microscopy (cryo-EM) structure of the entire catalytically active complex I reconstituted into lipid nanodiscs. The structure of this mesophilic bacterial complex I displays highly dynamic connection between the peripheral and membrane domains. The peripheral domain assembly is stabilized by unique terminal extensions and an insertion loop. The membrane domain structure reveals novel dynamic features. Unusual conformation of the conserved interface between the peripheral and membrane domains suggests an uncoupled conformation of the complex. Considering constraints imposed by the structural data, we suggest a new simple hypothetical coupling mechanism for the molecular machine.

PubMed: 34308841
DOI: 10.7554/eLife.68710

実験手法

ELECTRON MICROSCOPY (3.7 Å)