3e9j is a 4 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB.,Malojcic G, Owen RL, Grimshaw JP, Glockshuber R FEBS Lett. 2008 Oct 15;582(23-24):3301-7. Epub 2008 Sep 5. PMID:18775700[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑Malojcic G, Owen RL, Grimshaw JP, Glockshuber R. Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB. FEBS Lett. 2008 Oct 15;582(23-24):3301-7. Epub 2008 Sep 5. PMID:18775700 doi:S0014-5793(08)00718-7
