1S3A

NMR Solution Structure of Subunit B8 from Human NADH-Ubiquinone Oxidoreductase Complex I (CI-B8)

1S3A の概要

• エントリーDOI: 10.2210/pdb1s3a/pdb
• 分子名称: NADH-ubiquinone oxidoreductase B8 subunit (1 entity in total)
• 機能のキーワード: ci-b8, ndufa2, complex i, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side: O43678
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11194.87

構造登録者

Brockmann, C.,Diehl, A.,Rehbein, K.,Kuhne, R.,Oschkinat, H. (登録日: 2004-01-13, 公開日: 2005-01-25, 最終更新日: 2024-10-30)

主引用文献

Brockmann, C.,Diehl, A.,Rehbein, K.,Strauss, H.,Schmieder, P.,Korn, B.,Kuhne, R.,Oschkinat, H.
The oxidized subunit B8 from human complex I adopts a thioredoxin fold.
Structure, 12:1645-1654, 2004

PubMed Abstract: Subunit B8 from ubiquinone oxidoreductase (complex I) (CI-B8) is one of several nuclear-encoded supernumerary subunits that are not present in bacterial complex I. Its solution structure shows a thioredoxin fold with highest similarities to the human thioredoxin mutant C73S and thioredoxin 2 from Anabeana sp. Interestingly, these proteins contain active sites in the same area, where the disulfide bond of oxidized CI-B8 is located. The redox potential of this disulfide bond is -251.6 mV, comparing well to that of disulfides in other thioredoxin-like proteins. Analysis of the structure reveals a surface area that is exclusively composed of highly conserved residues and thus most likely a subunit interaction site within complex I.

PubMed: 15341729
DOI: 10.1016/j.str.2004.06.021

実験手法

SOLUTION NMR