2FUG

Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus

2FUG の概要

• エントリーDOI: 10.2210/pdb2fug/pdb
• 分子名称: NADH-quinone oxidoreductase chain 1, FE2/S2 (INORGANIC) CLUSTER, FLAVIN MONONUCLEOTIDE, ... (11 entities in total)
• 機能のキーワード: oxidoreductase, electron transport, respiratory chain
• 由来する生物種: Thermus thermophilus; 詳細
• 細胞内の位置: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : Q56222 Q56221 Q56223 Q56220 Q56219 Q56218 Q56224
• タンパク質・核酸の鎖数: 32
• 化学式量合計: 1137723.09

構造登録者

Sazanov, L.A.,Hinchliffe, P. (登録日: 2006-01-26, 公開日: 2006-02-14, 最終更新日: 2024-10-09)

主引用文献

Sazanov, L.A.,Hinchliffe, P.
Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus.
Science, 311:1430-1436, 2006

PubMed Abstract: Respiratory complex I plays a central role in cellular energy production in bacteria and mitochondria. Its dysfunction is implicated in many human neurodegenerative diseases, as well as in aging. The crystal structure of the hydrophilic domain (peripheral arm) of complex I from Thermus thermophilus has been solved at 3.3 angstrom resolution. This subcomplex consists of eight subunits and contains all the redox centers of the enzyme, including nine iron-sulfur clusters. The primary electron acceptor, flavin-mononucleotide, is within electron transfer distance of cluster N3, leading to the main redox pathway, and of the distal cluster N1a, a possible antioxidant. The structure reveals new aspects of the mechanism and evolution of the enzyme. The terminal cluster N2 is coordinated, uniquely, by two consecutive cysteines. The novel subunit Nqo15 has a similar fold to the mitochondrial iron chaperone frataxin, and it may be involved in iron-sulfur cluster regeneration in the complex.

PubMed: 16469879
DOI: 10.1126/science.1123809

実験手法

X-RAY DIFFRACTION (3.3 Å)