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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/D6MSX4_9ACTN D6MSX4_9ACTN] | | [https://www.uniprot.org/uniprot/D6MSX4_9ACTN D6MSX4_9ACTN] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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<ref>PMID:23526584</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4g2t" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
