Structural highlights
Publication Abstract from PubMed
The molecule known as SF2575 from Streptomyces sp. is a tetracycline polyketide natural product that displays antitumor activity against murine leukemia P388 in vivo. In the SF2575 biosynthetic pathway, SsfS6 has been implicated as the crucial C-glycosyltransferase (C-GT) that forms the C-C glycosidic bond between the sugar and the SF2575 tetracycline-like scaffold. Here, we report the crystal structure of SsfS6 in the free form and in complex with TDP, both at 2.4 A resolution. The structures reveal SsfS6 to adopt a GT-B fold wherein the TDP and docked putative aglycon are consistent with the overall C-glycosylation reaction. As one of only a few existing structures for C-glycosyltransferases, the structures described herein may serve as a guide to better understand and engineer C-glycosylation.Proteins 2013. (c) 2013 Wiley Periodicals, Inc.
Crystal structure of SsfS6, the putative C-glycosyltransferase involved in SF2575 biosynthesis.,Wang F, Zhou M, Singh S, Yennamalli RM, Bingman CA, Thorson JS, Phillips GN Jr Proteins. 2013 Mar 22. doi: 10.1002/prot.24289. PMID:23526584[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang F, Zhou M, Singh S, Yennamalli RM, Bingman CA, Thorson JS, Phillips GN Jr. Crystal structure of SsfS6, the putative C-glycosyltransferase involved in SF2575 biosynthesis. Proteins. 2013 Mar 22. doi: 10.1002/prot.24289. PMID:23526584 doi:10.1002/prot.24289
