7AWT

E. coli NADH quinone oxidoreductase hydrophilic arm

7AWT の概要

• エントリーDOI: 10.2210/pdb7awt/pdb
• EMDBエントリー: 11930
• 分子名称: NADH-quinone oxidoreductase subunit B, FLAVIN MONONUCLEOTIDE, NADH-quinone oxidoreductase subunit C/D, ... (11 entities in total)
• 機能のキーワード: e. coli, respiratory complex i, electron transport
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 285816.02

構造登録者

Schimpf, J.,Grishkovskaya, I.,Haselbach, D.,Friedrich, T. (登録日: 2020-11-09, 公開日: 2021-09-15, 最終更新日: 2024-07-10)

主引用文献

Schimpf, J.,Oppermann, S.,Gerasimova, T.,Santos Seica, A.F.,Hellwig, P.,Grishkovskaya, I.,Wohlwend, D.,Haselbach, D.,Friedrich, T.
Structure of the peripheral arm of a minimalistic respiratory complex I.
Structure, 30:80-, 2022

PubMed Abstract: Respiratory complex I drives proton translocation across energy-transducing membranes by NADH oxidation coupled with (ubi)quinone reduction. In humans, its dysfunction is associated with neurodegenerative diseases. The Escherichia coli complex represents the structural minimal form of an energy-converting NADH:ubiquinone oxidoreductase. Here, we report the structure of the peripheral arm of the E. coli complex I consisting of six subunits, the FMN cofactor, and nine iron-sulfur clusters at 2.7 Å resolution obtained by cryo electron microscopy. While the cofactors are in equivalent positions as in the complex from other species, individual subunits are adapted to the absence of supernumerary proteins to guarantee structural stability. The catalytically important subunits NuoC and D are fused resulting in a specific architecture of functional importance. Striking features of the E. coli complex are scrutinized by mutagenesis and biochemical characterization of the variants. Moreover, the arrangement of the subunits sheds light on the unknown assembly of the complex.

PubMed: 34562374
DOI: 10.1016/j.str.2021.09.005

実験手法

ELECTRON MICROSCOPY (2.73 Å)