7msk
From Proteopedia
(Difference between revisions)
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==ThuS glycosin S-glycosyltransferase== | ==ThuS glycosin S-glycosyltransferase== | ||
| - | <StructureSection load='7msk' size='340' side='right'caption='[[7msk]]' scene=''> | + | <StructureSection load='7msk' size='340' side='right'caption='[[7msk]], [[Resolution|resolution]] 2.06Å' 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=7MSK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MSK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7msk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis_serovar_andalousiensis_BGSC_4AW1 Bacillus thuringiensis serovar andalousiensis BGSC 4AW1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MSK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MSK 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=7msk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7msk OCA], [https://pdbe.org/7msk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7msk RCSB], [https://www.ebi.ac.uk/pdbsum/7msk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7msk 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]] 2.06Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=U2F:URIDINE-5-DIPHOSPHATE-2-DEOXY-2-FLUORO-ALPHA-D-GLUCOSE'>U2F</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=7msk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7msk OCA], [https://pdbe.org/7msk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7msk RCSB], [https://www.ebi.ac.uk/pdbsum/7msk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7msk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/C3GCL5_BACTU C3GCL5_BACTU] | ||
| + | <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 7msk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus thuringiensis serovar andalousiensis BGSC 4AW1]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Garg N]] | [[Category: Garg N]] | ||
[[Category: Nair SK]] | [[Category: Nair SK]] | ||
Current revision
ThuS glycosin S-glycosyltransferase
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