Wang, FengbinZhou, MaoquanSingh, ShanteriYennamalli, Ragothaman M.Bingman, Craig A.Thorson, Jon S.Phillips, George N.Jr.2014-12-152014-12-152013Wang, Fengbin, Zhou, Maoquan, Singh, Shanteri, et al.. "Crystal structure of SsfS6, the putative C-glycosyltransferase involved in SF2575 biosynthesis." <i>Proteins: Structure, Function, and Bioinformatics,</i> 81, no. 7 (2013) Wiley: 1277-1282. http://dx.doi.org/10.1002/prot.24289.https://hdl.handle.net/1911/78740The 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 CC 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 Å 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.engThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Wiley.Journal articlenatural productantitumorGT-B foldX-ray diffractionmolecular dockingbiosynthesiscarbohydratehttp://dx.doi.org/10.1002/prot.24289