View source for 4zrs


==Crystal structure of a cloned feruloyl esterase from a soil metagenomic library==
<StructureSection load='4zrs' size='340' side='right'caption='[[4zrs]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zrs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4ZRS 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=4zrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zrs OCA], [https://pdbe.org/4zrs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zrs RCSB], [https://www.ebi.ac.uk/pdbsum/4zrs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zrs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E7DJY5_9BACT E7DJY5_9BACT] 
<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&reg;/PubMed&reg;, 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: Large Structures]]
[[Category: Uncultured bacterium]]
[[Category: Cao L]]
[[Category: Chen R]]
[[Category: Liu Y]]
[[Category: Xie W]]