4G2T

Crystal Structure of Streptomyces sp. SF2575 glycosyltransferase SsfS6, complexed with thymidine diphosphate

Summary for 4G2T

• Entry DOI: 10.2210/pdb4g2t/pdb
• Related: 4FZR
• Descriptor: SsfS6, THYMIDINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: structural genomics, psi-biology, protein structure initiative, enzyme discovery for natural product biosynthesis, natpro, glycosyltransferase, transferase
• Biological source: Streptomyces sp. SF2575
• Total number of polymer chains: 1
• Total formula weight: 43489.04

Authors

Wang, F.,Zhou, M.,Singh, S.,Bingman, C.A.,Thorson, J.S.,Phillips Jr., G.N.,Enzyme Discovery for Natural Product Biosynthesis (NatPro) (deposition date: 2012-07-12, release date: 2012-07-25, Last modification date: 2024-10-09)

Primary citation

Wang, F.,Zhou, M.,Singh, S.,Yennamalli, R.M.,Bingman, C.A.,Thorson, J.S.,Phillips, G.N.
Crystal structure of SsfS6, the putative C-glycosyltransferase involved in SF2575 biosynthesis.
Proteins, 81:1277-1282, 2013

PubMed Abstract: 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.

PubMed: 23526584
DOI: 10.1002/prot.24289

Experimental method

X-RAY DIFFRACTION (2.405 Å)