5LC5

Structure of mammalian respiratory Complex I, class2

5LC5 の概要

• エントリーDOI: 10.2210/pdb5lc5/pdb
• EMDBエントリー: 4032
• 分子名称: NADH-ubiquinone oxidoreductase chain 3, NADH-ubiquinone oxidoreductase chain 6, NADH-ubiquinone oxidoreductase chain 4L, ... (50 entities in total)
• 機能のキーワード: nadh:ubiquinone oxidoreductase, multienzyme complexes, complex i, mitochondria, oxidoreductase
• 由来する生物種: Bos taurus (Bovine); 詳細
• タンパク質・核酸の鎖数: 45
• 化学式量合計: 885284.98

構造登録者

Vinothkumar, K.R.,Zhu, J.,Hirst, J. (登録日: 2016-06-19, 公開日: 2016-09-07, 最終更新日: 2024-10-23)

主引用文献

Zhu, J.,Vinothkumar, K.R.,Hirst, J.
Structure of mammalian respiratory complex I.
Nature, 536:354-358, 2016

PubMed Abstract: Complex I (NADH:ubiquinone oxidoreductase), one of the largest membrane-bound enzymes in the cell, powers ATP synthesis in mammalian mitochondria by using the reducing potential of NADH to drive protons across the inner mitochondrial membrane. Mammalian complex I (ref. 1) contains 45 subunits, comprising 14 core subunits that house the catalytic machinery (and are conserved from bacteria to humans) and a mammalian-specific cohort of 31 supernumerary subunits. Knowledge of the structures and functions of the supernumerary subunits is fragmentary. Here we describe a 4.2-Å resolution single-particle electron cryomicroscopy structure of complex I from Bos taurus. We have located and modelled all 45 subunits, including the 31 supernumerary subunits, to provide the entire structure of the mammalian complex. Computational sorting of the particles identified different structural classes, related by subtle domain movements, which reveal conformationally dynamic regions and match biochemical descriptions of the 'active-to-de-active' enzyme transition that occurs during hypoxia. Our structures therefore provide a foundation for understanding complex I assembly and the effects of mutations that cause clinically relevant complex I dysfunctions, give insights into the structural and functional roles of the supernumerary subunits and reveal new information on the mechanism and regulation of catalysis.

PubMed: 27509854
DOI: 10.1038/nature19095

実験手法

ELECTRON MICROSCOPY (4.35 Å)