View source for 9wjk


==Crystal structure of mouse EOGT-UDP complex==
<StructureSection load='9wjk' size='340' side='right'caption='[[9wjk]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9wjk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9WJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9WJK 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=9wjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9wjk OCA], [https://pdbe.org/9wjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9wjk RCSB], [https://www.ebi.ac.uk/pdbsum/9wjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9wjk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EOGT_MOUSE EOGT_MOUSE] Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines of folded EGF-like domains.<ref>PMID:22310717</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Epidermal growth factor (EGF) domain-specific O-linked N-acetylglucosamine transferase (EOGT), a glycosyltransferase (GT) 61 family member, catalyzes O-N-acetylglucosamine (O-GlcNAc) transfer from uridine diphosphate (UDP)-GlcNAc to serine or threonine residues within EGF domains in the endoplasmic reticulum. In this study, we determined the crystal structure of the EOGT-UDP complex and identified the critical residues mediating their interactions, which were validated via site-directed mutagenesis and enzyme activity assays. These residues were conserved in EOGT orthologs across metazoans, and UDP binding occurred independently of divalent metal ions and the canonical Asp-X-Asp motif. Although EOGT catalyzes O-GlcNAcylation, similar to O-GlcNAc transferase (OGT), it shares little sequence similarity with OGT and belongs to a distinct GT family. Instead, EOGT is more closely related to protein O-linked-mannose beta1,4-N-acetylglucosaminyltransferase 2 (POMGNT2). Structural comparison with POMGNT2 revealed a conserved triad of one asparagine and two arginine residues, the N-R-R constellation. These elements were conserved across metazoans and green plants (Viridiplantae), suggesting a unifying mechanism of UDP recognition and providing a framework to interpret disease-associated EOGT mutations and assess the evolution of catalytically active GT61 family enzymes.

Crystal structure of epidermal growth factor domain-specific O-linked N-acetylglucosamine transferase reveals a conserved N-R-R constellation for uridine diphosphate recognition in the GT61 family.,Tashima Y, Nagae M, Jiang J, Okajima T PNAS Nexus. 2026 Apr 15;5(4):pgag115. doi: 10.1093/pnasnexus/pgag115. eCollection , 2026 Apr. PMID:42058885<ref>PMID:42058885</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9wjk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Nagae M]]
[[Category: Okajima T]]
[[Category: Tashima Y]]