View source for 7wwh


==Crystal structure of the Geobacillus thermoglucosidasius feruloyl esterase GthFAE==
<StructureSection load='7wwh' size='340' side='right'caption='[[7wwh]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7wwh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Parageobacillus_thermoglucosidasius Parageobacillus thermoglucosidasius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WWH 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]] 1.92&#8491;</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=7wwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wwh OCA], [https://pdbe.org/7wwh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wwh RCSB], [https://www.ebi.ac.uk/pdbsum/7wwh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wwh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A369WTY0_PARTM A0A369WTY0_PARTM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Feruloyl esterases are indispensable biocatalysts catalyzing the cleavage of ester bonds between polysaccharides and their hydroxycinnamoyl cross-links. GthFAE from Geobacillus thermoglucosidasius was identified as a thermophilic alkaline feruloyl esterase with potential applications in paper manufacturing. To improve the enzymatic properties rationally and efficiently, the structure of GthFAE was solved at 1.9 A, revealing a core domain of classical alpha/beta hydrolase fold and an inserted alpha/beta cap domain. In silico analysis based on it helped us to investigate whether the residues at the active center have positive effects on the stability, and how. Several site-directed mutations were conducted, of which substitutions at residues T41 and T150 apparently improved the thermostability. The combination mutant T41N/T150R exhibited an optimal temperature of 65 degrees C, a 6.4 degrees C higher Tm compared to wild type by 80 degrees C, and a 35-fold longer in half-life (201 min) at 70 degrees C. Molecular dynamics simulations further illustrated that the structure of T41N/T150R was more stable than the wild type and T150R stabilized the cap domain by introducing salt bridges to the region with E154 and D164. This study not only highlighted residues within the active center on their thermostability improving effects, but also contributed to the prospective industrial application of GthFAE.

Structure-guided rational design of the Geobacillus thermoglucosidasius feruloyl esterase GthFAE to improve its thermostability.,Yang W, Sun L, Dong P, Chen Y, Zhang H, Huang X, Wu L, Chen L, Jing D, Wu Y Biochem Biophys Res Commun. 2022 Feb 20;600:117-122. doi:, 10.1016/j.bbrc.2022.02.074. PMID:35219099<ref>PMID:35219099</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7wwh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Parageobacillus thermoglucosidasius]]
[[Category: Wu Y]]
[[Category: Yang W]]