5ay7

</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=5ay7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ay7 OCA], [https://pdbe.org/5ay7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ay7 RCSB], [https://www.ebi.ac.uk/pdbsum/5ay7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ay7 ProSAT]</span></td></tr>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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