View source for 4wsj


==Crystal structure of a bacterial fucodiase in complex with 1-((1R,2R,3R,4R,5R,6R)-2,3,4-trihydroxy-5-methyl-7-azabicyclo[4.1.0]heptan-7-yl)ethan-1-one==
<StructureSection load='4wsj' size='340' side='right'caption='[[4wsj]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wsj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WSJ 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]] 1.64&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3U3:N-[(1S,2R,3R,4S,5R)-3,4,5-TRIHYDROXY-2-METHYLCYCLOHEXYL]ACETAMIDE'>3U3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4wsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wsj OCA], [https://pdbe.org/4wsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wsj RCSB], [https://www.ebi.ac.uk/pdbsum/4wsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wsj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8A3I4_BACTN Q8A3I4_BACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
GH29 alpha-l-fucosidases catalyze the hydrolysis of alpha-l-fucosidic linkages. Deficiency in human lysosomal alpha-l-fucosidase (FUCA1) leads to the recessively inherited disorder, fucosidosis. Herein we describe the development of fucopyranose-configured cyclophellitol aziridines as activity-based probes (ABPs) for selective in vitro and in vivo labeling of GH29 alpha-l-fucosidases from bacteria, mice and man. Crystallographic analysis on bacterial alpha-l-fucosidase confirms that the ABPs act by covalent modification of the active site nucleophile. Competitive activity-based protein profiling identified l-fuconojirimycin as the single GH29 alpha-l-fucosidase inhibitor from eight configurational isomers.

In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 alpha-l-fucosidases.,Jiang J, Kallemeijn WW, Wright DW, van den Nieuwendijk AMCH, Rohde VC, Folch EC, van den Elst H, Florea BI, Scheij S, Donker-Koopman WE, Verhoek M, Li N, Schurmann M, Mink D, Boot RG, Codee JDC, van der Marel GA, Davies GJ, Aerts JMFG, Overkleeft HS Chem Sci. 2015 May 1;6(5):2782-false. doi: 10.1039/c4sc03739a. Epub 2015 Feb 9. PMID:29142681<ref>PMID:29142681</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4wsj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacteroides thetaiotaomicron VPI-5482]]
[[Category: Large Structures]]
[[Category: Davies GJ]]
[[Category: Wright DW]]