View source for 5abe


==Structure of GH84 with ligand==
<StructureSection load='5abe' size='340' side='right'caption='[[5abe]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5abe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron Bacteroides thetaiotaomicron]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ABE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ABE 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=XQO:2-[(2S,3S,4R,5R)-5-(HYDROXYMETHYL)-3,4-BIS(OXIDANYL)-1-PENTYL-PYRROLIDIN-2-YL]-N-METHYL-ETHANAMIDE'>XQO</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=5abe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5abe OCA], [https://pdbe.org/5abe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5abe RCSB], [https://www.ebi.ac.uk/pdbsum/5abe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5abe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OGA_BACTN OGA_BACTN] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pyrrolidine-based iminocyclitols are a promising class of glycosidase inhibitors. Reported herein is a convenient epimerization strategy that provides direct access to a range of stereoisomeric iminocyclitol inhibitors of O-GlcNAcase (OGA), the enzyme responsible for catalyzing removal of O-GlcNAc from nucleocytoplasmic proteins. Structural details regarding the binding of these inhibitors to a bacterial homologue of OGA reveal the basis for potency. These compounds are orally available and permeate into rodent brain to increase O-GlcNAc, and should prove useful tools for studying the role of OGA in health and disease.

A Convenient Approach to Stereoisomeric Iminocyclitols: Generation of Potent Brain-Permeable OGA Inhibitors.,Bergeron-Brlek M, Goodwin-Tindall J, Cekic N, Roth C, Zandberg WF, Shan X, Varghese V, Chan S, Davies GJ, Vocadlo DJ, Britton R Angew Chem Int Ed Engl. 2015 Nov 6. doi: 10.1002/anie.201507985. PMID:26545827<ref>PMID:26545827</ref>

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

==See Also==
*[[O-GlcNAcase|O-GlcNAcase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacteroides thetaiotaomicron]]
[[Category: Large Structures]]
[[Category: Bergeron-Brlek M]]
[[Category: Britton R]]
[[Category: Cekic N]]
[[Category: Chan S]]
[[Category: Davies GJ]]
[[Category: Goodwin-Tindall J]]
[[Category: Roth C]]
[[Category: Shan X]]
[[Category: Varghese V]]
[[Category: Vocadlo DJ]]
[[Category: Zandberg WF]]