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5GUP

Cryo-EM structure of mammalian respiratory supercomplex I1III2IV1

これはPDB形式変換不可エントリーです。
5GUP の概要
エントリーDOI10.2210/pdb5gup/pdb
EMDBエントリー9539
分子名称Cytochrome c oxidase subunit 6C, NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12, ... (81 entities in total)
機能のキーワードcryo-em, mammalian, respiratory, supercomplex, electron transport
由来する生物種Sus scrofa (Pig)
詳細
タンパク質・核酸の鎖数80
化学式量合計1818698.72
構造登録者
Gu, J.,Wu, M.,Guo, R.,Yang, M. (登録日: 2016-08-30, 公開日: 2017-03-29, 最終更新日: 2025-04-09)
主引用文献Wu, M.,Gu, J.,Guo, R.,Huang, Y.,Yang, M.
Structure of Mammalian Respiratory Supercomplex I1III2IV1
Cell, 167:1598-1609.e10, 2016
Cited by
PubMed Abstract: The mammalian respiratory chain complexes assemble into supercomplexes (SCs) and reside in the inner mitochondrial membrane to transfer electrons and establish the proton gradient for complex V to synthesize ATP. The precise arrangement of SCs is largely unknown. Here, we report a 4.0-Å cryo-electron microscopy (cryo-EM) structure of the major SC in porcine heart, the 1.7-MDa SCIIIIIV. The complex III (CIII) dimer and complex IV (CIV) bind at the same side of the L-shaped complex I (CI). Several accessory or supernumerary subunits of CI, such as NDUFA11, NDUFB4, NDUFB8, and NDUFB9, directly contribute to the oligomerization of CI, CIII, and CIV. COX7C and COX7A of CIV attach CIV to the concave surface formed by CIII and the distal end of membrane arm of CI. The structure suggests a possible mechanism by which electrons are transferred from NADH to cytochrome c and provides a platform for future functional dissection of respiration.
PubMed: 27912063
DOI: 10.1016/j.cell.2016.11.012
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (4 Å)
構造検証レポート
Validation report summary of 5gup
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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