2K74

Solution NMR structure of DsbB-ubiquinone complex

2K74 の概要

• エントリーDOI: 10.2210/pdb2k74/pdb
• 関連するPDBエントリー: 2HI7 2K73
• 分子名称: Disulfide bond formation protein B, UBIQUINONE-2 (2 entities in total)
• 機能のキーワード: membrane protein, disulfide bond, redox enzyme, dsbb, ubiquinone, oxidative protein folding, chaperone, electron transport, inner membrane, oxidoreductase, redox-active center, transmembrane, transport
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P0A6M2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21267.20

構造登録者

Zhou, Y.,Cierpicki, T.,Flores Jimenez, R.H.,Lukasik, S.M.,Ellena, J.F.,Cafiso, D.S.,Kadokura, H.,Beckwith, J.,Bushweller, J.H. (登録日: 2008-08-01, 公開日: 2008-10-07, 最終更新日: 2021-10-20)

主引用文献

Zhou, Y.,Cierpicki, T.,Jimenez, R.H.,Lukasik, S.M.,Ellena, J.F.,Cafiso, D.S.,Kadokura, H.,Beckwith, J.,Bushweller, J.H.
NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation.
Mol.Cell, 31:896-908, 2008

PubMed Abstract: We describe the NMR structure of DsbB, a polytopic helical membrane protein. DsbB, a bacterial cytoplasmic membrane protein, plays a key role in disulfide bond formation. It reoxidizes DsbA, the periplasmic protein disulfide oxidant, using the oxidizing power of membrane-embedded quinones. We determined the structure of an interloop disulfide bond form of DsbB, an intermediate in catalysis. Analysis of the structure and interactions with substrates DsbA and quinone reveals functionally relevant changes induced by these substrates. Analysis of the structure, dynamics measurements, and NMR chemical shifts around the interloop disulfide bond suggest how electron movement from DsbA to quinone through DsbB is regulated and facilitated. Our results demonstrate the extraordinary utility of NMR for functional characterization of polytopic integral membrane proteins and provide insights into the mechanism of DsbB catalysis.

PubMed: 18922471
DOI: 10.1016/j.molcel.2008.08.028

実験手法

SOLUTION NMR