8IVY
Beta-Glucosidase BglA mutant E166Q in complex with glucose
Summary for 8IVY
Entry DOI | 10.2210/pdb8ivy/pdb |
Descriptor | Beta-glucosidase, GLYCEROL, beta-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | beta-glucosidase, complex, glucose, laminaribiose, hydrolase |
Biological source | Acetivibrio thermocellus |
Total number of polymer chains | 2 |
Total formula weight | 110700.49 |
Authors | |
Primary citation | Xiao, Y.,Dong, S.,Liu, Y.J.,You, C.,Feng, Y.,Cui, Q. Key roles of beta-glucosidase BglA for the catabolism of both laminaribiose and cellobiose in the lignocellulolytic bacterium Clostridium thermocellum. Int.J.Biol.Macromol., 250:126226-126226, 2023 Cited by PubMed Abstract: The thermophilic bacterium Clostridium thermocellum efficiently degrades polysaccharides into oligosaccharides. The metabolism of β-1,4-linked cello-oligosaccharides is initiated by three enzymes, i.e., the cellodextrin phosphorylase (Cdp), the cellobiose phosphorylase (Cbp), and the β-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 β-1,3-disaccharide laminaribiose with much higher activity than that against the β-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 β-1,3-linked glycosidic bonds in lignocellulose biorefinery. PubMed: 37558019DOI: 10.1016/j.ijbiomac.2023.126226 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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