7ZMG

CryoEM structure of mitochondrial complex I from Chaetomium thermophilum (state 1)

7ZMG の概要

• エントリーDOI: 10.2210/pdb7zmg/pdb
• 関連するPDBエントリー: 7ZM7 7ZM8 7ZMB 7ZME 7ZMH
• EMDBエントリー: 14797
• 分子名称: NADH-ubiquinone oxidoreductase chain 1, NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial, NADH-ubiquinone oxidoreductase 49 kDa subunit-like protein, ... (53 entities in total)
• 機能のキーワード: proton transporter, mitochondrial membrane protein, complex, oxidoreductase
• 由来する生物種: Chaetomium thermophilum var. thermophilum DSM 1495; 詳細
• タンパク質・核酸の鎖数: 43
• 化学式量合計: 1219033.60

構造登録者

Laube, E.,Kuehlbrandt, W. (登録日: 2022-04-19, 公開日: 2022-11-30, 最終更新日: 2024-10-23)

主引用文献

Laube, E.,Meier-Credo, J.,Langer, J.D.,Kuhlbrandt, W.
Conformational changes in mitochondrial complex I of the thermophilic eukaryote Chaetomium thermophilum.
Sci Adv, 8:eadc9952-eadc9952, 2022

PubMed Abstract: Mitochondrial complex I is a redox-driven proton pump that generates proton-motive force across the inner mitochondrial membrane, powering oxidative phosphorylation and ATP synthesis in eukaryotes. We report the structure of complex I from the thermophilic fungus , determined by cryoEM up to 2.4-Å resolution. We show that the complex undergoes a transition between two conformations, which we refer to as state 1 and state 2. The conformational switch is manifest in a twisting movement of the peripheral arm relative to the membrane arm, but most notably in substantial rearrangements of the Q-binding cavity and the E-channel, resulting in a continuous aqueous passage from the E-channel to subunit ND5 at the far end of the membrane arm. The conformational changes in the complex interior resemble those reported for mammalian complex I, suggesting a highly conserved, universal mechanism of coupling electron transport to proton pumping.

PubMed: 36427319
DOI: 10.1126/sciadv.adc9952

実験手法

ELECTRON MICROSCOPY (2.44 Å)