8IAQ

Respiratory complex Membrane domain of CI, focused map of type I, Wild type mouse under thermoneutral temperature

8IAQ の概要

• エントリーDOI: 10.2210/pdb8iaq/pdb
• EMDBエントリー: 35315
• 分子名称: NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11, NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial, ... (29 entities in total)
• 機能のキーワード: respiratory complex, respiratory supercomplex, electron transport
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 569800.71

構造登録者

Shin, Y.-C.,Liao, M. (登録日: 2023-02-09, 公開日: 2024-09-18, 最終更新日: 2024-10-30)

主引用文献

Shin, Y.C.,Latorre-Muro, P.,Djurabekova, A.,Zdorevskyi, O.,Bennett, C.F.,Burger, N.,Song, K.,Xu, C.,Paulo, J.A.,Gygi, S.P.,Sharma, V.,Liao, M.,Puigserver, P.
Structural basis of respiratory complex adaptation to cold temperatures.
Cell, 2024

PubMed Abstract: In response to cold, mammals activate brown fat for respiratory-dependent thermogenesis reliant on the electron transport chain. Yet, the structural basis of respiratory complex adaptation upon cold exposure remains elusive. Herein, we combined thermoregulatory physiology and cryoelectron microscopy (cryo-EM) to study endogenous respiratory supercomplexes from mice exposed to different temperatures. A cold-induced conformation of CI:III (termed type 2) supercomplex was identified with a ∼25° rotation of CIII around its inter-dimer axis, shortening inter-complex Q exchange space, and exhibiting catalytic states that favor electron transfer. Large-scale supercomplex simulations in mitochondrial membranes reveal how lipid-protein arrangements stabilize type 2 complexes to enhance catalytic activity. Together, our cryo-EM studies, multiscale simulations, and biochemical analyses unveil the thermoregulatory mechanisms and dynamics of increased respiratory capacity in brown fat at the structural and energetic level.

PubMed: 39395414
DOI: 10.1016/j.cell.2024.09.029

実験手法

ELECTRON MICROSCOPY (3.4 Å)