NMR assignment of the periplasmic oxidoreductase DsbH from Chlamydia.
نویسندگان
چکیده
Chlamydia use a complex of outer envelope proteins, which are highly cross-linked by disulfide bonds, to protect their infectious developmental form from lysis. Reported herein are the NMR chemical shift assignments of DsbH, a novel disulfide oxidoreductase from Chlamydia.
منابع مشابه
Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase.
The Chlamydia family of human pathogens uses outer envelope proteins that are highly cross-linked by disulfide bonds but nevertheless keeps an unusually high number of unpaired cysteines in its secreted proteins. To gain insight into chlamydial disulfide bond catalysis, the structure, function, and substrate interaction of a novel periplasmic oxidoreductase, termed DsbH, were determined. The st...
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عنوان ژورنال:
- Biomolecular NMR assignments
دوره 1 2 شماره
صفحات -
تاریخ انتشار 2007