View source for 3wue


==The wild type crystal structure of b-1,4-Xylanase (XynAS9) with xylobiose from Streptomyces sp. 9==
<StructureSection load='3wue' size='340' side='right'caption='[[3wue]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wue]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WUE 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]] 2.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRD_900116:4beta-beta-xylobiose'>PRD_900116</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3wue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wue OCA], [https://pdbe.org/3wue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wue RCSB], [https://www.ebi.ac.uk/pdbsum/3wue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wue ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/XYNA_STRSQ XYNA_STRSQ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The glycoside hydrolase 10 (GH10) xylanase from Streptomyces sp. 9 (XynAS9) can operate in a broad range of pH and temperature, and thus is a potential candidate for commercial applications. Recently, we engineered XynAS9 via mutating several residues in accordance with the consensus sequences of GH10 thermophilic xylanases in an attempt to improve the enzyme thermostability and thermotolerance. The most promising effects were observed in the double mutant V81P/G82E. In order to investigate the molecular mechanism of the improved thermal profile of XynAS9, complex crystal structures of the wild type (WT) and mutant (MT) enzyme were solved at 1.88-2.05A resolution. The structures reveal a classical GH10 (beta/alpha)8 TIM-barrel fold. In MT XynAS9, E82 forms several interactions to its neighboring residues, which might aid in stabilizing the local structure. Furthermore, the MT structure showed lower B factors for individual residues compared to the WT structure, reflecting the increased MT protein rigidity. Analyses of the XynAS9 structures also delineate the detailed enzyme-substrate interaction network. More importantly, possible explanations for the enhanced thermal profiles of MT XynAS9 are proposed, which may be a useful strategy for enzyme engineering in the future.

Structural perspectives of an engineered beta-1,4-xylanase with enhanced thermostability.,Chen CC, Luo H, Han X, Lv P, Ko TP, Peng W, Huang CH, Wang K, Gao J, Zheng Y, Yang Y, Zhang J, Yao B, Guo RT J Biotechnol. 2014 Sep 3;189C:175-182. doi: 10.1016/j.jbiotec.2014.08.030. PMID:25193708<ref>PMID:25193708</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wue" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp]]
[[Category: Chen CC]]
[[Category: Gao J]]
[[Category: Guo RT]]
[[Category: Han X]]
[[Category: Huang CH]]
[[Category: Ko TP]]
[[Category: Lv P]]
[[Category: Peng W]]
[[Category: Yang Y]]
[[Category: Zheng Y]]