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5lvv
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Human OGT in complex with UDP and fused substrate peptide (Tab1)== | |
| + | <StructureSection load='5lvv' size='340' side='right' caption='[[5lvv]], [[Resolution|resolution]] 2.54Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5lvv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LVV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LVV FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5lvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lvv OCA], [http://pdbe.org/5lvv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lvv RCSB], [http://www.ebi.ac.uk/pdbsum/5lvv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lvv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | O-linked N-acetylglucosamine (O-GlcNAc) is an essential and dynamic post-translational modification found on hundreds of nucleocytoplasmic proteins in metazoa. Although a single enzyme, O-GlcNAc transferase (OGT), generates the entire cytosolic O-GlcNAc proteome, it is not understood how it recognizes its protein substrates, targeting only a fraction of serines/threonines in the metazoan proteome for glycosylation. We describe a trapped complex of human OGT with the C-terminal domain of TAB1, a key innate immunity-signalling O-GlcNAc protein, revealing extensive interactions with the tetratricopeptide repeats of OGT. Confirmed by mutagenesis, this interaction suggests that glycosylation substrate specificity is achieved by recognition of a degenerate sequon in the active site combined with an extended conformation C-terminal of the O-GlcNAc target site. | ||
| - | + | Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats.,Rafie K, Raimi O, Ferenbach AT, Borodkin VS, Kapuria V, van Aalten DMF Open Biol. 2017 Jun;7(6). pii: 170078. doi: 10.1098/rsob.170078. PMID:28659383<ref>PMID:28659383</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5lvv" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Raimi, O]] | ||
| + | [[Category: Glycosylation]] | ||
| + | [[Category: O-glcnac]] | ||
| + | [[Category: O-glcnac transferase]] | ||
| + | [[Category: Signalling]] | ||
| + | [[Category: Substrate recognition]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 10:22, 10 September 2017
Human OGT in complex with UDP and fused substrate peptide (Tab1)
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