This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
7msn
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==SunS glycosin S-glycosyltransferase== | ==SunS glycosin S-glycosyltransferase== | ||
| - | <StructureSection load='7msn' size='340' side='right'caption='[[7msn]]' scene=''> | + | <StructureSection load='7msn' size='340' side='right'caption='[[7msn]], [[Resolution|resolution]] 3.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>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> | + | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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> | </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®/PubMed®, 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Garg N]] | [[Category: Garg N]] | ||
[[Category: Nair SK]] | [[Category: Nair SK]] | ||
Current revision
SunS glycosin S-glycosyltransferase
| |||||||||||
