5ay7: Difference between revisions

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'''Unreleased structure'''


The entry 5ay7 is ON HOLD  until Paper Publication
==A psychrophilic glycoside hydrolase family 10 endo-beta-1,4-xylanase==
<StructureSection load='5ay7' size='340' side='right' caption='[[5ay7]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ay7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AY7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AY7 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d4y|5d4y]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></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=5ay7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ay7 OCA], [http://pdbe.org/5ay7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ay7 RCSB], [http://www.ebi.ac.uk/pdbsum/5ay7 PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The cold-adapted xylanases can catalyze at low temperature and hold great potential in food industry applications. Here we describe the first crystal structure of a cold-adapted glycoside hydrolase (GH) family 10 xylanase XynGR40 and its complex with xylobiose at 2.15 and 2.50A resolution. The enzyme folds into a typical GH10 (beta/alpha)8 TIM-barrel, with E132 and E243 serving as the catalytic residues. The xylobiose was observed to occupy the -1 and -2 subsites. Structural comparison with a thermophilic GH10 xylanase highlighting various parameters that may explain the cold adaptation features were analyzed. Synergistic effects of the increased exposure of hydrophobic residues, the higher flexibility of substrate-binding residues, more flexible loops, and the ratios of special amino acid residues, may result in the cold adaptation of XynGR40.


Authors: Guo, R.T., Zheng, Y., Li, Y., Liu, W.
Structural insight into potential cold adaptation mechanism through a psychrophilic glycoside hydrolase family 10 endo-beta-1,4-xylanase.,Zheng Y, Li Y, Liu W, Chen CC, Ko TP, He M, Xu Z, Liu M, Luo H, Guo RT, Yao B, Ma Y J Struct Biol. 2016 Mar;193(3):206-11. doi: 10.1016/j.jsb.2015.12.010. Epub 2015 , Dec 21. PMID:26719223<ref>PMID:26719223</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5ay7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Guo, R T]]
[[Category: Li, Y]]
[[Category: Liu, W]]
[[Category: Liu, W]]
[[Category: Zheng, Y]]
[[Category: Zheng, Y]]
[[Category: Li, Y]]
[[Category: Gh10]]
[[Category: Guo, R.T]]
[[Category: Hydrolase]]
[[Category: Tim-barrel fold]]
[[Category: Xylanase]]
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