1ST9

Crystal Structure of a Soluble Domain of ResA in the Oxidised Form

1ST9 の概要

• エントリーDOI: 10.2210/pdb1st9/pdb
• 関連するPDBエントリー: 1SU9
• 分子名称: Thiol-disulfide oxidoreductase resA, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: thioredoxin-like domain, alpha-beta protein, soluble domain, membrane protein, oxidoreductase
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cell membrane; Single-pass type II membrane protein: P35160
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32132.53

構造登録者

Crow, A.,Acheson, R.M.,Le Brun, N.E.,Oubrie, A. (登録日: 2004-03-25, 公開日: 2004-05-11, 最終更新日: 2024-11-20)

主引用文献

Crow, A.,Acheson, R.M.,Le Brun, N.E.,Oubrie, A.
Structural Basis of Redox-coupled Protein Substrate Selection by the Cytochrome c Biosynthesis Protein ResA.
J.Biol.Chem., 279:23654-23660, 2004

PubMed Abstract: Post-translational maturation of cytochromes c involves the covalent attachment of heme to the Cys-Xxx-Xxx-Cys-His motif of the apo-cytochrome. For this process, the two cysteines of the motif must be in the reduced state. In bacteria, this is achieved by dedicated, membrane-bound thiol-disulfide oxidoreductases with a high reducing power, which are essential components of cytochrome c maturation systems and are also linked to cellular disulfide-bond formation machineries. Here we report high-resolution structures of oxidized and reduced states of a soluble, functional domain of one such oxidoreductase, ResA, from Bacillus subtilis. The structures elucidate the structural basis of the protein's high reducing power and reveal the largest redox-coupled conformational changes observed to date in any thioredoxin-like protein. These redox-coupled changes alter the protein surface and illustrate how the redox state of ResA predetermines to which substrate it binds. Furthermore, a polar cavity, present only in the reduced state, may confer specificity to recognize apo-cytochrome c. The described features of ResA are likely to be general for bacterial cytochrome c maturation systems.

PubMed: 15047692
DOI: 10.1074/jbc.M402823200

実験手法

X-RAY DIFFRACTION (1.5 Å)