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< | ==XcOGT in complex with UDP-S-GlcNAc== | ||
<StructureSection load='2xgo' size='340' side='right'caption='[[2xgo]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xgo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris Xanthomonas campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XGO 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]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZKD:URIDINE-DIPHOSPHATE-1-DEOXY-1-THIO-N-ACETYLGLUCOSAMINE'>ZKD</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=2xgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xgo OCA], [https://pdbe.org/2xgo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xgo RCSB], [https://www.ebi.ac.uk/pdbsum/2xgo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xgo ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8PC69_XANCP Q8PC69_XANCP] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xg/2xgo_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2xgo ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein glycosylation on serine/threonine residues with N-acetylglucosamine (O-GlcNAc) is a dynamic, inducible and abundant post-translational modification. It is thought to regulate many cellular processes and there are examples of interplay between O-GlcNAc and protein phosphorylation. In metazoa, a single, highly conserved and essential gene encodes the O-GlcNAc transferase (OGT) that transfers GlcNAc onto substrate proteins using UDP-GlcNAc as the sugar donor. Specific inhibitors of human OGT would be useful tools to probe the role of this post-translational modification in regulating processes in the living cell. Here, we describe the synthesis of novel UDP-GlcNAc/UDP analogues and evaluate their inhibitory properties and structural binding modes in vitro alongside alloxan, a previously reported weak OGT inhibitor. While the novel analogues are not active on living cells, they inhibit the enzyme in the micromolar range and together with the structural data provide useful templates for further optimisation. | |||
Substrate and product analogues as human O-GlcNAc transferase inhibitors.,Dorfmueller HC, Borodkin VS, Blair DE, Pathak S, Navratilova I, van Aalten DM Amino Acids. 2010 Jul 17. PMID:20640461<ref>PMID:20640461</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xgo" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[O-GlcNAc transferase 3D structures|O-GlcNAc transferase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Xanthomonas campestris]] | [[Category: Xanthomonas campestris]] | ||
[[Category: Blair DE]] | |||
[[Category: Blair | [[Category: Borodkin VS]] | ||
[[Category: Borodkin | [[Category: Dorfmueller HC]] | ||
[[Category: Dorfmueller | [[Category: Navratilova I]] | ||
[[Category: Navratilova | [[Category: Pathak S]] | ||
[[Category: Pathak | [[Category: Van Aalten DM]] | ||
[[Category: | |||
Latest revision as of 13:31, 20 December 2023
XcOGT in complex with UDP-S-GlcNAcXcOGT in complex with UDP-S-GlcNAc
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProtein glycosylation on serine/threonine residues with N-acetylglucosamine (O-GlcNAc) is a dynamic, inducible and abundant post-translational modification. It is thought to regulate many cellular processes and there are examples of interplay between O-GlcNAc and protein phosphorylation. In metazoa, a single, highly conserved and essential gene encodes the O-GlcNAc transferase (OGT) that transfers GlcNAc onto substrate proteins using UDP-GlcNAc as the sugar donor. Specific inhibitors of human OGT would be useful tools to probe the role of this post-translational modification in regulating processes in the living cell. Here, we describe the synthesis of novel UDP-GlcNAc/UDP analogues and evaluate their inhibitory properties and structural binding modes in vitro alongside alloxan, a previously reported weak OGT inhibitor. While the novel analogues are not active on living cells, they inhibit the enzyme in the micromolar range and together with the structural data provide useful templates for further optimisation. Substrate and product analogues as human O-GlcNAc transferase inhibitors.,Dorfmueller HC, Borodkin VS, Blair DE, Pathak S, Navratilova I, van Aalten DM Amino Acids. 2010 Jul 17. PMID:20640461[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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