9w4b

Crystal structure of beta-glucosidase CaBGL

spinqualitylabelsall models 9w4b, resolution 2.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9w4b is a 12 chain structure with sequence from Unclassified Caldicellulosiruptor. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.34Å Ligands: GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function I7DLX2_9FIRM Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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