NMR Solution Structure of the Integral Membrane Enzyme DsbB: Functional Insights into DsbB-Catalyzed Disulfide Bond Formation

Yunpeng Zhou, Tomasz Cierpicki, Ricardo H.Flores Jimenez, Stephen M. Lukasik, Jeffrey F. Ellena, David S. Cafiso, Hiroshi Kadokura, Jon Beckwith, John H. Bushweller

研究成果: Article査読

144 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)896-908
ページ数13
ジャーナルMolecular Cell
31
6
DOI
出版ステータスPublished - 2008 9 26
外部発表はい

ASJC Scopus subject areas

  • 分子生物学
  • 細胞生物学

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