4zrs: Difference between revisions
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''' | ==Crystal structure of a cloned feruloyl esterase from a soil metagenomic library== | ||
<StructureSection load='4zrs' size='340' side='right' caption='[[4zrs]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4zrs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZRS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZRS FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEB:O-BENZYLSULFONYL-SERINE'>SEB</scene></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=4zrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zrs OCA], [http://pdbe.org/4zrs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zrs RCSB], [http://www.ebi.ac.uk/pdbsum/4zrs PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
To improve the thermostability of EstF27, two rounds of random mutagenesis were performed. A thermostable mutant, M6, with six amino acid substitutions was obtained. The half-life of M6 at 55 degrees C is 1680 h, while that of EstF27 is 0.5 h. The Kcat/Km value of M6 is 1.9-fold higher than that of EstF27. The concentrations of ferulic acid released from destarched wheat bran by EstF27 and M6 at their respective optimal temperatures were 223.2 +/- 6.8 and 464.8 +/- 11.9 muM, respectively. To further understand the structural basis of the enhanced thermostability, the crystal structure of M6 is determined at 2.0 A. Structural analysis shows that a new disulfide bond and hydrophobic interactions formed by the mutations may play an important role in stabilizing the protein. This study not only provides us with a robust catalyst, but also enriches our knowledge about the structure-function relationship of feruloyl esterase. | |||
Enhancing the Thermostability of Feruloyl Esterase EstF27 by Directed Evolution and the Underlying Structural Basis.,Cao LC, Chen R, Xie W, Liu YH J Agric Food Chem. 2015 Sep 23;63(37):8225-33. doi: 10.1021/acs.jafc.5b03424., Epub 2015 Sep 10. PMID:26329893<ref>PMID:26329893</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4zrs" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cao, L]] | [[Category: Cao, L]] | ||
[[Category: Chen, R]] | [[Category: Chen, R]] | ||
[[Category: Liu, Y]] | [[Category: Liu, Y]] | ||
[[Category: Xie, W]] | |||
[[Category: Feruloyl esterase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Metagenomic library]] | |||
Revision as of 15:38, 3 February 2016
Crystal structure of a cloned feruloyl esterase from a soil metagenomic library
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