6Q9C

Crystal structure of Aquifex aeolicus NADH-quinone oxidoreductase subunits NuoE and NuoF bound to NADH under anaerobic conditions

6Q9C の概要

• エントリーDOI: 10.2210/pdb6q9c/pdb
• 分子名称: NADH-quinone oxidoreductase subunit E, NADH-quinone oxidoreductase subunit F, FE2/S2 (INORGANIC) CLUSTER, ... (10 entities in total)
• 機能のキーワード: respiratory chain, complex i, nadh ubiquinone oxidoreductase, fe-s clusters, oxidoreductase
• 由来する生物種: Aquifex aeolicus (strain VF5); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 133700.45

構造登録者

Wohlwend, D.,Gerhardt, S.,Gnandt, E.,Friedrich, T. (登録日: 2018-12-17, 公開日: 2019-06-26, 最終更新日: 2024-05-15)

主引用文献

Schulte, M.,Frick, K.,Gnandt, E.,Jurkovic, S.,Burschel, S.,Labatzke, R.,Aierstock, K.,Fiegen, D.,Wohlwend, D.,Gerhardt, S.,Einsle, O.,Friedrich, T.
A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I.
Nat Commun, 10:2551-2551, 2019

PubMed Abstract: Respiratory complex I plays a central role in cellular energy metabolism coupling NADH oxidation to proton translocation. In humans its dysfunction is associated with degenerative diseases. Here we report the structure of the electron input part of Aquifex aeolicus complex I at up to 1.8 Å resolution with bound substrates in the reduced and oxidized states. The redox states differ by the flip of a peptide bond close to the NADH binding site. The orientation of this peptide bond is determined by the reduction state of the nearby [Fe-S] cluster N1a. Fixation of the peptide bond by site-directed mutagenesis led to an inactivation of electron transfer and a decreased reactive oxygen species (ROS) production. We suggest the redox-gated peptide flip to represent a previously unrecognized molecular switch synchronizing NADH oxidation in response to the redox state of the complex as part of an intramolecular feed-back mechanism to prevent ROS production.

PubMed: 31186428
DOI: 10.1038/s41467-019-10429-0

実験手法

X-RAY DIFFRACTION (1.78 Å)