View source for 6jbs


==Bifunctional xylosidase/glucosidase LXYL==
<StructureSection load='6jbs' size='340' side='right'caption='[[6jbs]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jbs]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lened Lened]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JBS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JBS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Lxyl-p1-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5353 LENED])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6jbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jbs OCA], [http://pdbe.org/6jbs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jbs RCSB], [http://www.ebi.ac.uk/pdbsum/6jbs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jbs ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
LXYL-P1-2 is one of the few xylosidases that efficiently catalyze the reaction from 7-beta-xylosyl-10-deacetyltaxol (XDT) to 10-deacetyltaxol (DT), and is a potential enzyme used in Taxol industrial production. Here we report the crystal structure of LXYL-P1-2 and its XDT binding complex. These structures reveal an enzyme/product complex with the sugar conformation different from the enzyme/substrate complex reported previously in GH3 enzymes, even in the whole glycohydrolases family. In addition, the DT binding pocket is identified as the structural basis for the substrate specificity. Further structure analysis reveals common features in LXYL-P1-2 and Taxol binding protein tubulin, which might provide useful information for designing new Taxol carrier proteins for drug delivery.

Structures of beta-glycosidase LXYL-P1-2 reveals the product binding state of GH3 family and a specific pocket for Taxol recognition.,Yang L, Chen TJ, Wang F, Li L, Yu WB, Si YK, Chen JJ, Liu WC, Zhu P, Gong W Commun Biol. 2020 Jan 10;3(1):22. doi: 10.1038/s42003-019-0744-4. PMID:31925310<ref>PMID:31925310</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jbs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lened]]
[[Category: Gong, W M]]
[[Category: Yang, L Y]]
[[Category: Bifunctional]]
[[Category: Glycoside hydrolase]]
[[Category: Hydrolase]]
[[Category: Xylosidase]]