5d4y: Difference between revisions
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==A psychrophilic glycoside hydrolase family 10 endo-beta-1,4-xylanase== | |||
<StructureSection load='5d4y' size='340' side='right' caption='[[5d4y]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5d4y]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D4Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D4Y FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BXP:4-O-BETA-D-XYLOPYRANOSYL-BETA-D-XYLOPYRANOSE'>BXP</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ay7|5ay7]]</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=5d4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d4y OCA], [http://pdbe.org/5d4y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d4y RCSB], [http://www.ebi.ac.uk/pdbsum/5d4y 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5d4y" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Guo, R T]] | |||
[[Category: Zheng, Y]] | [[Category: Zheng, Y]] | ||
[[Category: | [[Category: Gh10]] | ||
[[Category: Hydrolase]] | |||
[[Category: Tim-barrel fold]] | |||
[[Category: Xylanase]] | |||
Revision as of 18:04, 26 February 2016
A psychrophilic glycoside hydrolase family 10 endo-beta-1,4-xylanase
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