3E9J

Structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB

3E9J の概要

• エントリーDOI: 10.2210/pdb3e9j/pdb
• 分子名称: Thiol/disulfide oxidoreductase DsbA, Thiol/disulfide oxidoreductase DsbB, UBIQUINONE-1 (3 entities in total)
• 機能のキーワード: membrane protein complex, mechanism of disulfide bond formation, oxidative protein folding in escherichia coli periplasm, x-ray crystal structure, charge transfer reaction intermediate, four helix bundle, periplasm, redox-active center, cell inner membrane, cell membrane, chaperone, electron transport, membrane, oxidoreductase, transmembrane, transport
• 由来する生物種: Escherichia coli K12; 詳細
• 細胞内の位置: Periplasm: P0AEG4; Cell inner membrane; Multi-pass membrane protein: P0A6M2
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 84650.35

構造登録者

Malojcic, G.,Owen, R.L.,Glockshuber, R. (登録日: 2008-08-22, 公開日: 2008-11-25, 最終更新日: 2024-10-30)

主引用文献

Malojcic, G.,Owen, R.L.,Grimshaw, J.P.,Glockshuber, R.
Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB.
Febs Lett., 582:3301-3307, 2008

PubMed Abstract: Disulfide bond formation is a critical step in the folding of many secretory proteins. In bacteria, disulfide bonds are introduced by the periplasmic dithiol oxidase DsbA, which transfers its catalytic disulfide bond to folding polypeptides. Reduced DsbA is reoxidized by ubiquinone Q8, catalyzed by inner membrane quinone reductase DsbB. Here, we report the preparation of a kinetically stable ternary complex between wild-type DsbB, containing all essential cysteines, Q8 and DsbA covalently bound to DsbB. The crystal structure of this trapped DsbB reaction intermediate exhibits a charge-transfer interaction between Q8 and the Cys44 in the DsbB reaction center providing experimental evidence for the mechanism of de novo disulfide bond generation in DsbB.

PubMed: 18775700
DOI: 10.1016/j.febslet.2008.07.063

実験手法

X-RAY DIFFRACTION (3.7 Å)