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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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</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'>[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='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> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/A0A140UHL2_AEGSP A0A140UHL2_AEGSP] |
| - | 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.
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| - | | + | |
| - | 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>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5ay7" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </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]]
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| - | [[Category: Xylanase]]
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