3M9C

Crystal structure of the membrane domain of respiratory complex I from Escherichia coli

3M9C の概要

• エントリーDOI: 10.2210/pdb3m9c/pdb
• 関連するPDBエントリー: 3M9S
• 分子名称: NADH-quinone oxidoreductase subunit NuoL, NADH-quinone oxidoreductase subunit NuoM, NADH-quinone oxidoreductase subunit NuoN, ... (4 entities in total)
• 機能のキーワード: membrane protein, complex i, oxidoreductase, electron transport, respiratory chain
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 129771.64

構造登録者

Efremov, R.G.,Baradaran, R.,Sazanov, L.A. (登録日: 2010-03-22, 公開日: 2010-05-26, 最終更新日: 2024-02-21)

主引用文献

Efremov, R.G.,Baradaran, R.,Sazanov, L.A.
The architecture of respiratory complex I
Nature, 465:441-445, 2010

PubMed Abstract: Complex I is the first enzyme of the respiratory chain and has a central role in cellular energy production, coupling electron transfer between NADH and quinone to proton translocation by an unknown mechanism. Dysfunction of complex I has been implicated in many human neurodegenerative diseases. We have determined the structure of its hydrophilic domain previously. Here, we report the alpha-helical structure of the membrane domain of complex I from Escherichia coli at 3.9 A resolution. The antiporter-like subunits NuoL/M/N each contain 14 conserved transmembrane (TM) helices. Two of them are discontinuous, as in some transporters. Unexpectedly, subunit NuoL also contains a 110-A long amphipathic alpha-helix, spanning almost the entire length of the domain. Furthermore, we have determined the structure of the entire complex I from Thermus thermophilus at 4.5 A resolution. The L-shaped assembly consists of the alpha-helical model for the membrane domain, with 63 TM helices, and the known structure of the hydrophilic domain. The architecture of the complex provides strong clues about the coupling mechanism: the conformational changes at the interface of the two main domains may drive the long amphipathic alpha-helix of NuoL in a piston-like motion, tilting nearby discontinuous TM helices, resulting in proton translocation.

PubMed: 20505720
DOI: 10.1038/nature09066

実験手法

X-RAY DIFFRACTION (3.9 Å)