6kj0: Difference between revisions

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-'''Unreleased structure'''
-The entry 6kj0 is ON HOLD  until Paper Publication
+==Bifunctional xylosidase/glucosidase LXYL mutant E529Q C2221==
+<StructureSection load='6kj0' size='340' side='right'caption='[[6kj0]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6kj0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KJ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KJ0 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BKR:Deacetyltaxol'>BKR</scene>, <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=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></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=6kj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kj0 OCA], [http://pdbe.org/6kj0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kj0 RCSB], [http://www.ebi.ac.uk/pdbsum/6kj0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kj0 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.
-Authors: Gong, W.M., Yang, L.Y.
+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>
-Description: Bifunctional xylosidase/glucosidase LXYL mutant E529Q C2221
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Gong, W.M]]
+<div class="pdbe-citations 6kj0" style="background-color:#fffaf0;"></div>
-[[Category: Yang, L.Y]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Gong, W M]]
+[[Category: Yang, L Y]]
+[[Category: Bifunctional]]
+[[Category: Glycoside hydrolase]]
+[[Category: Hydrolase]]
+[[Category: Xylosidase]]