View source for 7cpk


==Xylanase R from Bacillus sp. TAR-1==
<StructureSection load='7cpk' size='340' side='right'caption='[[7cpk]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7cpk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._TAR1 Bacillus sp. TAR1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CPK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></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=7cpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cpk OCA], [https://pdbe.org/7cpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cpk RCSB], [https://www.ebi.ac.uk/pdbsum/7cpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cpk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/XYNA_HALH5 XYNA_HALH5] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The mechanism of thermostabilization of GH10 xylanase, XynR, from Bacillus sp. strain TAR-1 by the mutation of S92 to E was investigated. Thermodynamic analysis revealed that thermostabilization was driven by the decrease in entropy change of activation for thermal inactivation. Crystallographic analysis suggested that this mutation suppressed the fluctuation of the amino acid residues at position 92-95.

Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E.,Suzuki M, Takita T, Kuwata K, Nakatani K, Li T, Katano Y, Kojima K, Mizutani K, Mikami B, Yatsunami R, Nakamura S, Yasukawa K Biosci Biotechnol Biochem. 2021 Feb 18;85(2):386-390. doi: 10.1093/bbb/zbaa003. PMID:33604642<ref>PMID:33604642</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7cpk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus sp. TAR1]]
[[Category: Large Structures]]
[[Category: Katano Y]]
[[Category: Kojima K]]
[[Category: Kuwata K]]
[[Category: Li T]]
[[Category: Mikami B]]
[[Category: Mizutani K]]
[[Category: Nakamura S]]
[[Category: Nakatani K]]
[[Category: Suzuki M]]
[[Category: Takita T]]
[[Category: Yasukawa K]]
[[Category: Yatsunami R]]