6G2J

Mouse mitochondrial complex I in the active state

6G2J の概要

• エントリーDOI: 10.2210/pdb6g2j/pdb
• EMDBエントリー: 4345
• 分子名称: NADH-ubiquinone oxidoreductase chain 3, NADH-ubiquinone oxidoreductase chain 6, NADH-ubiquinone oxidoreductase chain 4L, ... (54 entities in total)
• 機能のキーワード: complex i, mitochondria, proton pump, membrane protein, oxidoreductase
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 45
• 化学式量合計: 1065953.11

構造登録者

Agip, A.N.A.,Blaza, J.N.,Bridges, H.R.,Viscomi, C.,Rawson, S.,Muench, S.P.,Hirst, J. (登録日: 2018-03-23, 公開日: 2018-06-06, 最終更新日: 2025-04-09)

主引用文献

Agip, A.A.,Blaza, J.N.,Bridges, H.R.,Viscomi, C.,Rawson, S.,Muench, S.P.,Hirst, J.
Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states.
Nat. Struct. Mol. Biol., 25:548-556, 2018

PubMed Abstract: Complex I (NADH:ubiquinone oxidoreductase) uses the reducing potential of NADH to drive protons across the energy-transducing inner membrane and power oxidative phosphorylation in mammalian mitochondria. Recent cryo-EM analyses have produced near-complete models of all 45 subunits in the bovine, ovine and porcine complexes and have identified two states relevant to complex I in ischemia-reperfusion injury. Here, we describe the 3.3-Å structure of complex I from mouse heart mitochondria, a biomedically relevant model system, in the 'active' state. We reveal a nucleotide bound in subunit NDUFA10, a nucleoside kinase homolog, and define mechanistically critical elements in the mammalian enzyme. By comparisons with a 3.9-Å structure of the 'deactive' state and with known bacterial structures, we identify differences in helical geometry in the membrane domain that occur upon activation or that alter the positions of catalytically important charged residues. Our results demonstrate the capability of cryo-EM analyses to challenge and develop mechanistic models for mammalian complex I.

PubMed: 29915388
DOI: 10.1038/s41594-018-0073-1

実験手法

ELECTRON MICROSCOPY (3.3 Å)