View source for 5vvt


==Structural Investigations of the Substrate Specificity of Human O-GlcNAcase==
<StructureSection load='5vvt' size='340' side='right'caption='[[5vvt]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vvt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VVT 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=5vvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vvt OCA], [https://pdbe.org/5vvt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vvt RCSB], [https://www.ebi.ac.uk/pdbsum/5vvt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vvt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ELK1_HUMAN ELK1_HUMAN] Stimulates transcription. Binds to purine-rich DNA sequences. Can form a ternary complex with the serum response factor and the ETS and SRF motifs of the fos serum response element.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The O-linked beta-N-acetyl glucosamine (O-GlcNAc) modification dynamically regulates the functions of numerous proteins. A single human enzyme O-linked beta-N-acetyl glucosaminase (O-GlcNAcase or OGA) hydrolyzes this modification. To date, it remains largely unknown how OGA recognizes various substrates. Here we report the structures of OGA in complex with each of four distinct glycopeptide substrates that contain a single O-GlcNAc modification on a serine or threonine residue. Intriguingly, these glycopeptides bind in a bidirectional yet conserved conformation within the substrate-binding cleft of OGA. This study provides fundamental insights into a general principle that confers the substrate binding adaptability and specificity to OGA in O-GlcNAc regulation.O-linked beta-N-acetyl glucosamine (O-GlcNAc) is an important protein modification that is hydrolyzed by O-GlcNAcase (OGA). Here the authors give insights into OGA substrate recognition by presenting four human OGA structures complexed with glycopeptide substrates containing a single O-GlcNAc modification on either a serine or threonine.

Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase.,Li B, Li H, Hu CW, Jiang J Nat Commun. 2017 Sep 22;8(1):666. doi: 10.1038/s41467-017-00865-1. PMID:28939839<ref>PMID:28939839</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vvt" style="background-color:#fffaf0;"></div>

==See Also==
*[[O-GlcNAcase|O-GlcNAcase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Hu C-W]]
[[Category: Jiang J]]
[[Category: Li B]]
[[Category: Li H]]