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http://purl.uniprot.org/citations/23526584http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23526584http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23526584http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.org/dc/terms/identifier"doi:10.1002/prot.24289"xsd:string
http://purl.uniprot.org/citations/23526584http://purl.org/dc/terms/identifier"doi:10.1002/prot.24289"xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Singh S."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Singh S."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Wang F."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Wang F."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Zhou M."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Zhou M."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Bingman C.A."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Bingman C.A."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Phillips G.N. Jr."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Thorson J.S."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Thorson J.S."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Phillips G.N."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Yennamalli R.M."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/author"Yennamalli R.M."xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/name"Proteins"xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/name"Proteins"xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/pages"1277-1282"xsd:string
http://purl.uniprot.org/citations/23526584http://purl.uniprot.org/core/pages"1277-1282"xsd:string