Protein disulfide bond generation in Escherichia coli DsbB–DsbA
نویسنده
چکیده
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.
منابع مشابه
A Mutation in Either dsbA or dsbB, a Gene Encoding a Component of a Periplasmic Disulfide Bond-Catalyzing System, Is Required for High-Level Expression of the Bacteroides fragilis Metallo-b-Lactamase, CcrA, in Escherichia coli
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عنوان ژورنال:
- Journal of Synchrotron Radiation
دوره 15 شماره
صفحات -
تاریخ انتشار 2008