8ivy: Difference between revisions
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The | ==Beta-Glucosidase BglA mutant E166Q in complex with glucose== | ||
<StructureSection load='8ivy' size='340' side='right'caption='[[8ivy]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8ivy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IVY 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]] 1.95Å</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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=8ivy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ivy OCA], [https://pdbe.org/8ivy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ivy RCSB], [https://www.ebi.ac.uk/pdbsum/8ivy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ivy ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The thermophilic bacterium Clostridium thermocellum efficiently degrades polysaccharides into oligosaccharides. The metabolism of beta-1,4-linked cello-oligosaccharides is initiated by three enzymes, i.e., the cellodextrin phosphorylase (Cdp), the cellobiose phosphorylase (Cbp), and the beta-glucosidase A (BglA), in C. thermocellum. In comparison, how the oligosaccharides containing other kinds of linkage are utilized is rarely understood. In this study, we found that BglA could hydrolyze the beta-1,3-disaccharide laminaribiose with much higher activity than that against the beta-1,4-disaccharide cellobiose. The structural basis of the substrate specificity was analyzed by crystal structure determination and molecular docking. Genetic deletions of BglA and Cbp, respectively, and enzymatic analysis of cell extracts demonstrated that BglA is the key enzyme responsible for laminaribiose metabolism. Furthermore, the deletion of BglA can suppress the expression of Cbp and the deletion of Cbp can up-regulate the expression of BglA, indicating that BglA and Cbp have cross-regulation and BglA is also critical for cellobiose metabolism. These insights pave the way for both a fundamental understanding of metabolism and regulation in C. thermocellum and emphasize the importance of the degradation and utilization of polysaccharides containing beta-1,3-linked glycosidic bonds in lignocellulose biorefinery. | |||
Key roles of beta-glucosidase BglA for the catabolism of both laminaribiose and cellobiose in the lignocellulolytic bacterium Clostridium thermocellum.,Xiao Y, Dong S, Liu YJ, You C, Feng Y, Cui Q Int J Biol Macromol. 2023 Aug 7;250:126226. doi: 10.1016/j.ijbiomac.2023.126226. PMID:37558019<ref>PMID:37558019</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8ivy" style="background-color:#fffaf0;"></div> | ||
[[Category: Dong | == References == | ||
[[Category: Feng | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acetivibrio thermocellus]] | |||
[[Category: Large Structures]] | |||
[[Category: Dong S]] | |||
[[Category: Feng Y]] | |||
[[Category: Xiao Y]] | |||
Latest revision as of 08:54, 23 August 2023
Beta-Glucosidase BglA mutant E166Q in complex with glucoseBeta-Glucosidase BglA mutant E166Q in complex with glucose
Structural highlights
Publication Abstract from PubMedThe thermophilic bacterium Clostridium thermocellum efficiently degrades polysaccharides into oligosaccharides. The metabolism of beta-1,4-linked cello-oligosaccharides is initiated by three enzymes, i.e., the cellodextrin phosphorylase (Cdp), the cellobiose phosphorylase (Cbp), and the beta-glucosidase A (BglA), in C. thermocellum. In comparison, how the oligosaccharides containing other kinds of linkage are utilized is rarely understood. In this study, we found that BglA could hydrolyze the beta-1,3-disaccharide laminaribiose with much higher activity than that against the beta-1,4-disaccharide cellobiose. The structural basis of the substrate specificity was analyzed by crystal structure determination and molecular docking. Genetic deletions of BglA and Cbp, respectively, and enzymatic analysis of cell extracts demonstrated that BglA is the key enzyme responsible for laminaribiose metabolism. Furthermore, the deletion of BglA can suppress the expression of Cbp and the deletion of Cbp can up-regulate the expression of BglA, indicating that BglA and Cbp have cross-regulation and BglA is also critical for cellobiose metabolism. These insights pave the way for both a fundamental understanding of metabolism and regulation in C. thermocellum and emphasize the importance of the degradation and utilization of polysaccharides containing beta-1,3-linked glycosidic bonds in lignocellulose biorefinery. Key roles of beta-glucosidase BglA for the catabolism of both laminaribiose and cellobiose in the lignocellulolytic bacterium Clostridium thermocellum.,Xiao Y, Dong S, Liu YJ, You C, Feng Y, Cui Q Int J Biol Macromol. 2023 Aug 7;250:126226. doi: 10.1016/j.ijbiomac.2023.126226. PMID:37558019[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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