8j3m: Difference between revisions
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==Structure of GH1 Br2 beta-glucosidase from bovine rumen metagenome== | |||
<StructureSection load='8j3m' size='340' side='right'caption='[[8j3m]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8j3m]] is a 4 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=8J3M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8J3M 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]] 1.999Å</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=SO4:SULFATE+ION'>SO4</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=8j3m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8j3m OCA], [https://pdbe.org/8j3m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8j3m RCSB], [https://www.ebi.ac.uk/pdbsum/8j3m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8j3m ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1S5SJM8_9BACT A0A1S5SJM8_9BACT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ruminant animals rely on the activities of beta-glucosidases from residential microbes to convert feed fibers into glucose for further metabolic uses. In this report, we determined the structures of Br2, which is a glycoside hydrolase family 1 beta-glucosidase from the bovine rumen metagenome. Br2 folds into a classical (beta/alpha)(8)-TIM barrel domain but displays unique structural features at loop beta5-->alpha5 and alpha-helix 5, resulting in different positive subsites from those of other GH1 enzymes. Br2 exhibited the highest specificity toward laminaritriose, suggesting its involvement in beta-glucan hydrolysis in digested feed. We then substituted the residues at subsites +1 and + 2 of Br2 with those of Halothermothrix orenii beta-glucosidase. The C170E and C221T mutations provided favorable interactions with glucooligosaccharide substrates at subsite +2, while the A219N mutation probably improved the substrate preference for cellobiose and gentiobiose relative to laminaribiose at subsite +1. The N407Y mutation increased the affinity toward cellooligosaccharides. These results give further insights into the molecular determinants responsible for substrate specificity in GH1 beta-glucosidases and may provide a basis for future enzyme engineering applications. | |||
Structural and mutational analysis of glycoside hydrolase family 1 Br2 beta-glucosidase derived from bovine rumen metagenome.,Kaenying W, Tagami T, Suwan E, Pitsanuwong C, Chomngam S, Okuyama M, Kongsaeree P, Kimura A, Kongsaeree PT Heliyon. 2023 Nov 7;9(11):e21923. doi: 10.1016/j.heliyon.2023.e21923. eCollection , 2023 Nov. PMID:38034805<ref>PMID:38034805</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8j3m" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Uncultured bacterium]] | |||
[[Category: Kaenying W]] | |||
[[Category: Kongsaeree PT]] | |||
[[Category: Tagami T]] | |||
Latest revision as of 10:48, 12 March 2025
Structure of GH1 Br2 beta-glucosidase from bovine rumen metagenome
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