Protein disulfide bond generation in Escherichia coli DsbB-DsbA

Kenji Inaba

doi:10.1107/S090904950706061X

Protein disulfide bond generation in Escherichia coli DsbB-DsbA

Kenji Inaba

Division of Organic- and Biomaterials Research

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

Protein disulfide bond formation is catalyzed by a series of Dsb enzymes present in the periplasm of Escherichia coli. The crystal structure of the DsbB-DsbA-ubiquinone ternary complex provided important insights into mechanisms of the de novo disulfide bond generation cooperated by DsbB and ubiquinone and of the disulfide bond shuttle from DsbB to DsbA. The structural basis for prevention of the crosstalk between the DsbA-DsbB oxidative and the DsbC-DsbD reductive pathways has also been proposed.

Original language	English
Pages (from-to)	199-201
Number of pages	3
Journal	Journal of Synchrotron Radiation
Volume	15
Issue number	3
DOIs	https://doi.org/10.1107/S090904950706061X
Publication status	Published - 2008 Apr 18

Keywords

Escherichia coli
Protein disulfide bond generation

ASJC Scopus subject areas

Radiation
Nuclear and High Energy Physics
Instrumentation

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AB - Protein disulfide bond formation is catalyzed by a series of Dsb enzymes present in the periplasm of Escherichia coli. The crystal structure of the DsbB-DsbA-ubiquinone ternary complex provided important insights into mechanisms of the de novo disulfide bond generation cooperated by DsbB and ubiquinone and of the disulfide bond shuttle from DsbB to DsbA. The structural basis for prevention of the crosstalk between the DsbA-DsbB oxidative and the DsbC-DsbD reductive pathways has also been proposed.

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