View source for 5g0q


==beta-glucuronidase with an activity-based probe (N-alkyl cyclophellitol aziridine) bound==
<StructureSection load='5g0q' size='340' side='right'caption='[[5g0q]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5g0q]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G0Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5G0Q FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IF6:(1R,2S,3R,4S,5S,6R)-7-(8-AZIDOOCTYL)-3,4,5-TRIHYDROXY-'>IF6</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g0m|5g0m]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucuronidase Beta-glucuronidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.31 3.2.1.31] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5g0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g0q OCA], [http://pdbe.org/5g0q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g0q RCSB], [http://www.ebi.ac.uk/pdbsum/5g0q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g0q ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Humans express at least two distinct beta-glucuronidase enzymes that are involved in disease: exo-acting beta-glucuronidase (GUSB), whose deficiency gives rise to mucopolysaccharidosis type VII, and endo-acting heparanase (HPSE), whose overexpression is implicated in inflammation and cancers. The medical importance of these enzymes necessitates reliable methods to assay their activities in tissues. Herein, we present a set of beta-glucuronidase-specific activity-based probes (ABPs) that allow rapid and quantitative visualization of GUSB and HPSE in biological samples, providing a powerful tool for dissecting their activities in normal and disease states. Unexpectedly, we find that the supposedly inactive HPSE proenzyme proHPSE is also labeled by our ABPs, leading to surprising insights regarding structural relationships between proHPSE, mature HPSE, and their bacterial homologs. Our results demonstrate the application of beta-glucuronidase ABPs in tracking pathologically relevant enzymes and provide a case study of how ABP-driven approaches can lead to discovery of unanticipated structural and biochemical functionality.

Activity-based probes for functional interrogation of retaining beta-glucuronidases.,Wu L, Jiang J, Jin Y, Kallemeijn WW, Kuo CL, Artola M, Dai W, van Elk C, van Eijk M, van der Marel GA, Codee JDC, Florea BI, Aerts JMFG, Overkleeft HS, Davies GJ Nat Chem Biol. 2017 Jun 5. doi: 10.1038/nchembio.2395. PMID:28581485<ref>PMID:28581485</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5g0q" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glucuronisidase 3D structures|Glucuronisidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Beta-glucuronidase]]
[[Category: Large Structures]]
[[Category: Davies, G J]]
[[Category: Jiang, J B]]
[[Category: Jin, Y]]
[[Category: Overkleeft, H S]]
[[Category: Wu, L]]
[[Category: Activity-based probe]]
[[Category: Gh79]]
[[Category: Hydrolase]]
[[Category: Retaining enzyme]]