View source for 6ier


==Apo structure of a beta-glucosidase 1317==
<StructureSection load='6ier' size='340' side='right'caption='[[6ier]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ier]] is a 1 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=6IER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IER 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]] 2.246&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=6ier FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ier OCA], [https://pdbe.org/6ier PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ier RCSB], [https://www.ebi.ac.uk/pdbsum/6ier PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ier ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A5H1ZR35_9BACT A0A5H1ZR35_9BACT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
beta-Glucosidase is the rate-limiting component of a cellulase-hydrolyzing reaction. Thermostability and glucose-tolerance are two critical criteria of the enzyme, which practically determine its performance in industrial applications. In this study, a thermostable and glucose-tolerant beta-glucosidase (named Bgl1317) belonging to the glycoside hydrolase family 1 was acquired from a metagenomic library of Turpan soil through functional screening. Bgl1317 showed excellent thermostability and glucose-tolerance and its crystal structure was subsequently determined at a high resolution. Rational design based on the structure was conducted, producing three beneficial mutations A397R, L188A and A262S. While A397R improved the cellobiose activity by 80%, L188A and A262S increased the IC50 value of glucose from 0.8 to 1.5M. The residues that may play a role in glucose-tolerance of GH1 beta-glucosidases were summarized and the performances of glucose-tolerant beta-glucosidases reported in recent years were discussed and compared. This study provides insights into enzymatic properties of Bgl1317 for engineering it into a powerful catalyst and beta-glucosidases in general.

Improving the cellobiose-hydrolysis activity and glucose-tolerance of a thermostable beta-glucosidase through rational design.,Liu X, Cao L, Zeng J, Liu Y, Xie W Int J Biol Macromol. 2019 Jun 12;136:1052-1059. doi:, 10.1016/j.ijbiomac.2019.06.029. PMID:31199970<ref>PMID:31199970</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ier" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Uncultured bacterium]]
[[Category: Liu X]]
[[Category: Xie W]]