Crystal structure of SsfS6, the putative C-glycosyltransferase involved in SF2575 biosynthesis

Fengbin Wang, Maoquan Zhou, Shanteri Singh, Ragothaman M. Yennamalli, Craig A. Bingman, Jon S. Thorson, George N. Phillips

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


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 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.

Original languageEnglish
Pages (from-to)1277-1282
Number of pages6
JournalProteins: Structure, Function and Bioinformatics
Issue number7
StatePublished - Jul 2013


  • Antitumor
  • Biosynthesis
  • Carbohydrate
  • GT-B fold
  • Molecular docking
  • Natural product
  • X-ray diffraction

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


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