Protein disulfide bond generation in Escherichia coli DsbB-DsbA

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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 languageEnglish
Pages (from-to)199-201
Number of pages3
JournalJournal of Synchrotron Radiation
Volume15
Issue number3
DOIs
Publication statusPublished - 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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