9w4b

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Current revision (07:20, 15 October 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9w4b is ON HOLD until Paper Publication
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==Crystal structure of beta-glucosidase CaBGL==
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<StructureSection load='9w4b' size='340' side='right'caption='[[9w4b]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9w4b]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Unclassified_Caldicellulosiruptor Unclassified Caldicellulosiruptor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9W4B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9W4B FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.34&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9w4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9w4b OCA], [https://pdbe.org/9w4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9w4b RCSB], [https://www.ebi.ac.uk/pdbsum/9w4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9w4b ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/I7DLX2_9FIRM I7DLX2_9FIRM]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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beta-Glucosidase (BGL) plays a crucial role in lignocellulose utilization by alleviating cellobiose inhibition of cellulases. Incorporation of the BGL from Caldicellulosiruptor sp. F32 (CaBGL) enhanced the overall efficiency of the consolidated bio-saccharification process. To optimize BGL performance under industrial conditions, we established a thermostable green fluorescent protein-based high-throughput screening platform coupled with structure-informed semi-rational design, enabling the generation of functionally enhanced CaBGL mutants. This approach identified mutant M418T, which exhibited more than two-fold catalytic activity compared to that of wild type in both the absence and presence of glucose at various concentrations. In vitro cellulose saccharification showed that M418T increased the saccharification rate coefficient by 43.27 % compared to the wild-type. The mechanisms underlying its improved property were further elucidated through structural analysis and molecular docking. Consequently, this work presents an effective approach for enhancing the performance of CaBGL and demonstrates the potential of a promising catalyst in lignocellulose conversion.
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Authors:
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Engineering of beta-glucosidase CaBGL with improved performance in cellulose hydrolysis.,You C, Zheng X, Qi K, Dong S, Liu YJ, Chen C, Cui Q, Feng Y Bioresour Technol. 2025 Oct 1;440:133424. doi: 10.1016/j.biortech.2025.133424. PMID:41043783<ref>PMID:41043783</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9w4b" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Unclassified Caldicellulosiruptor]]
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[[Category: Feng YG]]
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[[Category: You C]]

Current revision

Crystal structure of beta-glucosidase CaBGL

PDB ID 9w4b

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