View source for 6kvh


==The mutant crystal structure of endo-polygalacturonase (T284A) from Talaromyces leycettanus JCM 12802==
<StructureSection load='6kvh' size='340' side='right'caption='[[6kvh]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6kvh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Evansstolkia_leycettana Evansstolkia leycettana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KVH 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]] 1.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6kvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kvh OCA], [https://pdbe.org/6kvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kvh RCSB], [https://www.ebi.ac.uk/pdbsum/6kvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kvh ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Thermostability is a key property of industrial enzymes. Endo-polygalacturonases of the glycoside hydrolase family 28 have many practical applications, but only few of their structures have been determined, and the reasons for their stability remain unclear. We identified and characterized the Talaromyces leycettanus JCM12802 endo-polygalacturonase TlPGA, which differs from other GH28 family members because of its high catalytic activity, with an optimum temperature of 70 degrees C. Distinctive features were revealed by comparison of thermophilic TlPGA and all known structures of fungal endo-polygalacturonases, including a relatively large exposed polar accessible surface area in thermophilic TlPGA. By mutating potentially important residues in thermophilic TlPGA, we identified Thr284 as a critical residue. Mutant T284A was comparable to thermophilic TlPGA in melting temperature but exhibited a significantly lower half-life and half-inactivation temperature, implicating residue Thr284 in the kinetic stability of thermophilic TlPGA. Structure analysis of thermophilic TlPGA and mutant T284A revealed that a carbon-oxygen hydrogen bond between the hydroxyl group of Thr284 and the Calpha atom of Gln255, and the stable conformation adopted by Gln255, contribute to its kinetic stability. Our results clarify the mechanism underlying the kinetic stability of GH28 endo-polygalacturonases and may guide the engineering of thermostable enzymes for industrial applications.

Structural Insights into the Mechanisms Underlying the Kinetic Stability of GH28 Endo-Polygalacturonase.,Tu T, Wang Z, Luo Y, Li Y, Su X, Wang Y, Zhang J, Rouvinen J, Yao B, Hakulinen N, Luo H J Agric Food Chem. 2021 Jan 20;69(2):815-823. doi: 10.1021/acs.jafc.0c06941. Epub, 2021 Jan 6. PMID:33404235<ref>PMID:33404235</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6kvh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Evansstolkia leycettana]]
[[Category: Large Structures]]
[[Category: Luo H]]
[[Category: Tu T]]
[[Category: Wang Z]]
[[Category: Yao B]]