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| | <StructureSection load='5ay7' size='340' side='right'caption='[[5ay7]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='5ay7' size='340' side='right'caption='[[5ay7]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ay7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aegilops_speltoides_subsp._speltoides Aegilops speltoides subsp. speltoides]. 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> | + | <table><tr><td colspan='2'>[[5ay7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aegilops_speltoides_subsp._speltoides Aegilops speltoides subsp. speltoides]. 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 [https://proteopedia.org/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> | + | </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> |
| - | <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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ay7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A140UHL2_AEGSP A0A140UHL2_AEGSP] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Aegilops speltoides subsp. speltoides]] | | [[Category: Aegilops speltoides subsp. speltoides]] |
| - | [[Category: Endo-1,4-beta-xylanase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Guo, R T]] | + | [[Category: Guo RT]] |
| - | [[Category: Li, Y]] | + | [[Category: Li Y]] |
| - | [[Category: Liu, W]] | + | [[Category: Liu W]] |
| - | [[Category: Zheng, Y]] | + | [[Category: Zheng Y]] |
| - | [[Category: Gh10]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Tim-barrel fold]]
| + | |
| - | [[Category: Xylanase]]
| + | |
| Structural highlights
Function
A0A140UHL2_AEGSP
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zheng Y, Li Y, Liu W, Chen CC, Ko TP, He M, Xu Z, Liu M, Luo H, Guo RT, Yao B, Ma Y. Structural insight into potential cold adaptation mechanism through a psychrophilic glycoside hydrolase family 10 endo-beta-1,4-xylanase. J Struct Biol. 2016 Mar;193(3):206-11. doi: 10.1016/j.jsb.2015.12.010. Epub 2015 , Dec 21. PMID:26719223 doi:http://dx.doi.org/10.1016/j.jsb.2015.12.010
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