Abstract:
:Disulfide bond formation is a critical step in the folding of many secretory proteins. In bacteria, disulfide bonds are introduced by the periplasmic dithiol oxidase DsbA, which transfers its catalytic disulfide bond to folding polypeptides. Reduced DsbA is reoxidized by ubiquinone Q8, catalyzed by inner membrane quinone reductase DsbB. Here, we report the preparation of a kinetically stable ternary complex between wild-type DsbB, containing all essential cysteines, Q8 and DsbA covalently bound to DsbB. The crystal structure of this trapped DsbB reaction intermediate exhibits a charge-transfer interaction between Q8 and the Cys44 in the DsbB reaction center providing experimental evidence for the mechanism of de novo disulfide bond generation in DsbB.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Malojcić G,Owen RL,Grimshaw JP,Glockshuber Rdoi
10.1016/j.febslet.2008.07.063subject
Has Abstractpub_date
2008-10-15 00:00:00pages
3301-7issue
23-24eissn
0014-5793issn
1873-3468pii
S0014-5793(08)00718-7journal_volume
582pub_type
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