View source for 7msn


==SunS glycosin S-glycosyltransferase==
<StructureSection load='7msn' size='340' side='right'caption='[[7msn]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7msn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MSN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7msn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7msn OCA], [https://pdbe.org/7msn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7msn RCSB], [https://www.ebi.ac.uk/pdbsum/7msn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7msn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SUNS_BACSU SUNS_BACSU] Transfers a hexose moiety onto 'Cys-41' of bacteriocin sublancin-168 (SunA). Accepts UDP-glucose (UDP-Glc), UDP-N-acetylglucosamine (UDP-GlcNAc), UDP-galactose (UDP-Gal), UDP-xylose (UDP-Xyl) and GDP-mannose as substrate.<ref>PMID:21196935</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Attachment of sugars to nitrogen and oxygen in peptides is ubiquitous in biology, but glycosylation of sulfur atoms has only been recently described. Here, we characterize two S-glycosyltransferases SunS and ThuS that selectively glycosylate one of five Cys residues in their substrate peptides; substitution of this Cys with Ser results in a strong decrease in glycosylation activity. Crystal structures of SunS and ThuS in complex with UDP-glucose or a derivative reveal an unusual architecture in which a glycosyltransferase type A (GTA) fold is decorated with additional domains to support homodimerization. Dimer formation creates an extended cavity for the substrate peptide, drawing functional analogy with O-glycosyltransferases involved in cell wall biosynthesis. This extended cavity contains a sharp bend that may explain the site selectivity of the glycosylation because the target Cys is in a Gly-rich stretch that can accommodate the bend. These studies establish a molecular framework for understanding the unusual S-glycosyltransferases.

Structural and mechanistic investigations of protein S-glycosyltransferases.,Fujinami D, Garcia de Gonzalo CV, Biswas S, Hao Y, Wang H, Garg N, Lukk T, Nair SK, van der Donk WA Cell Chem Biol. 2021 Dec 16;28(12):1740-1749.e6. doi:, 10.1016/j.chembiol.2021.06.009. Epub 2021 Jul 21. PMID:34283964<ref>PMID:34283964</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7msn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Garg N]]
[[Category: Nair SK]]