6jfp: Difference between revisions
New page: '''Unreleased structure''' The entry 6jfp is ON HOLD Authors: Xie, W., Chen, R. Description: Crystal structure of the beta-glucosidase Bgl15 Category: Unreleased Structures [[Categ... |
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==Crystal structure of the beta-glucosidase Bgl15== | |||
<StructureSection load='6jfp' size='340' side='right'caption='[[6jfp]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6jfp]] 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=6JFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JFP 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]] 2.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</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=6jfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jfp OCA], [https://pdbe.org/6jfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jfp RCSB], [https://www.ebi.ac.uk/pdbsum/6jfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jfp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A5B9BHU3_9BACT A0A5B9BHU3_9BACT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In this study, a Petri-dish-based double-layer high-throughput screening method was established to improve glucose tolerance of beta-glucosidase Bgl15. Two beneficial mutations were identified, and the joint mutant 2R1 improved the half-maximal inhibitory concentration of glucose from 0.04 to 2.1 M. The crystal structure of 2R1 was subsequently determined at 2.7 A. Structure analysis revealed that enhancement of glucose tolerance may be due to improved transglycosylation activity made possible by a hydrophobic binding site for glucose as an acceptor and more stringent control of a putative water channel. To further ameliorate the application potential of the enzyme, it was engineered to increase the half-life at 50 degrees C from 0.8 h (Bgl15) to 180 h (mutant 5R1). Furthermore, supplementation of 5R1 to the cellulase cocktail significantly improved glucose production from pretreated sugar cane bagasse by 38%. Consequently, this study provided an efficient approach to enhance glucose tolerance and generated a promising catalyst for cellulose saccharification. | |||
Engineering of beta-Glucosidase Bgl15 with Simultaneously Enhanced Glucose Tolerance and Thermostability To Improve Its Performance in High-Solid Cellulose Hydrolysis.,Cao L, Chen R, Huang X, Li S, Zhang S, Yang X, Qin Z, Kong W, Xie W, Liu Y J Agric Food Chem. 2020 May 13;68(19):5391-5401. doi: 10.1021/acs.jafc.0c01817., Epub 2020 May 4. PMID:32338906<ref>PMID:32338906</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6jfp" style="background-color:#fffaf0;"></div> | ||
[[Category: Chen | |||
==See Also== | |||
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Uncultured bacterium]] | |||
[[Category: Chen R]] | |||
[[Category: Xie W]] | |||
Latest revision as of 13:08, 22 November 2023
Crystal structure of the beta-glucosidase Bgl15Crystal structure of the beta-glucosidase Bgl15
Structural highlights
FunctionPublication Abstract from PubMedIn this study, a Petri-dish-based double-layer high-throughput screening method was established to improve glucose tolerance of beta-glucosidase Bgl15. Two beneficial mutations were identified, and the joint mutant 2R1 improved the half-maximal inhibitory concentration of glucose from 0.04 to 2.1 M. The crystal structure of 2R1 was subsequently determined at 2.7 A. Structure analysis revealed that enhancement of glucose tolerance may be due to improved transglycosylation activity made possible by a hydrophobic binding site for glucose as an acceptor and more stringent control of a putative water channel. To further ameliorate the application potential of the enzyme, it was engineered to increase the half-life at 50 degrees C from 0.8 h (Bgl15) to 180 h (mutant 5R1). Furthermore, supplementation of 5R1 to the cellulase cocktail significantly improved glucose production from pretreated sugar cane bagasse by 38%. Consequently, this study provided an efficient approach to enhance glucose tolerance and generated a promising catalyst for cellulose saccharification. Engineering of beta-Glucosidase Bgl15 with Simultaneously Enhanced Glucose Tolerance and Thermostability To Improve Its Performance in High-Solid Cellulose Hydrolysis.,Cao L, Chen R, Huang X, Li S, Zhang S, Yang X, Qin Z, Kong W, Xie W, Liu Y J Agric Food Chem. 2020 May 13;68(19):5391-5401. doi: 10.1021/acs.jafc.0c01817., Epub 2020 May 4. PMID:32338906[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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