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7e56
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The mutant crystal structure of endo-polygalacturonase (T316C/G344C) from Talaromyces leycettanus JCM 12802== |
| + | <StructureSection load='7e56' size='340' side='right'caption='[[7e56]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7e56]] 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=7E56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E56 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]] 1.4Å</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=7e56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e56 OCA], [https://pdbe.org/7e56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e56 RCSB], [https://www.ebi.ac.uk/pdbsum/7e56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e56 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A6M9BP13_9EURO A0A6M9BP13_9EURO] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Thermostable enzymes have many advantages for industrial applications. Therefore, in this study, computer-aided design technology was used to improve the thermostability of a highly active endo-polygalacturonase from Talaromyces leycettanus JCM12802 at an optimal temperature of 70 degrees C. The melting temperature and specific activity of the obtained mutant T316C/G344C were increased by 10 degrees C and 36.5%, respectively, compared with the wild-type enzyme. The crystal structure of the T316C/G344C mutant showed no formation of a disulfide bond between the introduced cysteines, indicating a different mechanism than the conventional mechanism underlying improved enzyme thermostability. The cysteine substitutions directly formed a new alkyl hydrophobic interaction and caused conformational changes in the side chains of the adjacent residues Asn315 and Thr343, which in turn caused a local reconstruction of hydrogen bonds. This method greatly improved the thermostability of the enzyme without affecting its activity; thus, our findings are of great significance for both theoretical research and practical applications. | ||
| - | + | Cysteine Engineering of an Endo-polygalacturonase from Talaromyces leycettanus JCM 12802 to Improve Its Thermostability.,Wang S, Meng K, Su X, Hakulinen N, Wang Y, Zhang J, Luo H, Yao B, Huang H, Tu T J Agric Food Chem. 2021 Jun 9;69(22):6351-6359. doi: 10.1021/acs.jafc.1c01618., Epub 2021 May 27. PMID:34043362<ref>PMID:34043362</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7e56" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Evansstolkia leycettana]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Luo H]] | ||
| + | [[Category: Tu T]] | ||
| + | [[Category: Yao B]] | ||
Current revision
The mutant crystal structure of endo-polygalacturonase (T316C/G344C) from Talaromyces leycettanus JCM 12802
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