5lvv: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5lvv is ~~ON HOLD until Paper~~ Publication

==Human OGT in complex with UDP and fused substrate peptide (Tab1)==

== 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>

== 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.

~~Authors~~:

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>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Raimi, O]]

[[Category: Glycosylation]]

[[Category: O-glcnac]]

[[Category: O-glcnac transferase]]

[[Category: Signalling]]

[[Category: Substrate recognition]]

[[Category: Transferase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5lvv is ON HOLD  until Paper Publication
+==Human OGT in complex with UDP and fused substrate peptide (Tab1)==
+<StructureSection load='5lvv' size='340' side='right' caption='[[5lvv]], [[Resolution|resolution]] 2.54&Aring;' 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</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]]