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| | ==Crystal structure of endo-1,4-beta-xylanase from Caldicellulosiruptor owensensis== | | ==Crystal structure of endo-1,4-beta-xylanase from Caldicellulosiruptor owensensis== |
| - | <StructureSection load='5y3x' size='340' side='right' caption='[[5y3x]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='5y3x' size='340' side='right'caption='[[5y3x]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5y3x]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Calow Calow]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y3X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y3X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5y3x]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldicellulosiruptor_owensensis_OL Caldicellulosiruptor owensensis OL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y3X FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Calow_0124 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632518 CALOW])</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]] 2.1Å</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=5y3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y3x OCA], [https://pdbe.org/5y3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y3x RCSB], [https://www.ebi.ac.uk/pdbsum/5y3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y3x 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=5y3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y3x OCA], [http://pdbe.org/5y3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y3x RCSB], [http://www.ebi.ac.uk/pdbsum/5y3x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y3x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E4Q2A4_CALOW E4Q2A4_CALOW] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Calow]] | + | [[Category: Caldicellulosiruptor owensensis OL]] |
| - | [[Category: Endo-1,4-beta-xylanase]] | + | [[Category: Large Structures]] |
| - | [[Category: Liu, T F]] | + | [[Category: Liu TF]] |
| - | [[Category: Liu, X]] | + | [[Category: Liu X]] |
| - | [[Category: Sun, L C]] | + | [[Category: Sun LC]] |
| - | [[Category: Xin, F J]] | + | [[Category: Xin FJ]] |
| - | [[Category: Zhang, Y B]] | + | [[Category: Zhang YB]] |
| - | [[Category: Gh10 xylanase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Thermostability]]
| + | |
| Structural highlights
Function
E4Q2A4_CALOW
Publication Abstract from PubMed
Xylanase (EC 3.2.1.8) is a kind of enzymes that degrade xylan into xylose, which has been widely used in a variety of industrial applications. Particularly, xylanases from thermophilic microorganisms show distinct advantages in the industries which need high temperature conditions. The CoXynA gene, which is identified from thermophilic bacterium Caldicellulosiruptor owensensis, encoding a glycoside hydrolase family 10 xylanase, was overexpressed in Escherichia coli. The recombinant CoXynA showed optimal activity at 90 degrees C and pH 7. Its half-life is about 1 h at 80 degrees C. The activity of CoXynA was not affected by most cations. CoXynA showed distinct substrate specificities for beech wood xylan and birch wood xylan. The crystal structure of CoXynA was solved and the molecular dynamics simulation was performed for CoXynA. The relatively high thermostability of CoXynA is proposed to be the increased overall protein rigidity resulted from the shortened length and reduced fluctuation of Loop 7.
Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-beta-Xylanase from Caldicellulosiruptor owensensis.,Liu X, Liu T, Zhang Y, Xin F, Mi S, Wen B, Gu T, Shi X, Wang F, Sun L J Agric Food Chem. 2017 Dec 13. doi: 10.1021/acs.jafc.7b03607. PMID:29236500[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu X, Liu T, Zhang Y, Xin F, Mi S, Wen B, Gu T, Shi X, Wang F, Sun L. Structural Insights into the Thermophilic Adaption Mechanism of Endo-1,4-beta-Xylanase from Caldicellulosiruptor owensensis. J Agric Food Chem. 2017 Dec 13. doi: 10.1021/acs.jafc.7b03607. PMID:29236500 doi:http://dx.doi.org/10.1021/acs.jafc.7b03607
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