8z2y
From Proteopedia
High-resolution crystal structure of exo-beta-(1,3)-glucanase from Aspergillus oryzae (AoBgl) as a complex with glucose
Structural highlights
FunctionEXGA_ASPOR Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase (By similarity).[1] Publication Abstract from PubMedExo-beta-(1,3)-glucanases are promising enzymes for use in the biofuel industry as they hydrolyse sugars such as laminarin, a major constituent of the algal cell wall. This study reports structural and biochemical characterizations of Aspergillus oryzae exo-beta-(1,3)-glucanase (AoBgl) belonging to the GH5 family. Purified AoBgl hydrolyses beta-(1,3)-glycosidic linkages of the oligosaccharide laminaritriose and the polysaccharide laminarin effectively. We have determined three high-resolution structures of AoBgl: (a) the apo form at 1.75 A, (b) the complexed form with bound cellobiose at 1.73 A and (c) the glucose-bound form at 1.20 A. The crystal structures, molecular dynamics simulation studies and site-directed mutagenesis reveal the mode of substrate binding and interactions at the active site. The results also indicate that AoBgl effectively hydrolyses trisaccharides and higher oligosaccharides. The findings from our structural and biochemical studies would aid in rational engineering efforts to generate superior AoBgl variants and similar GH5 enzymes for their industrial use. Crystal structures of Aspergillus oryzae exo-beta-(1,3)-glucanase reveal insights into oligosaccharide binding, recognition, and hydrolysis.,Banerjee B, Kamale CK, Suryawanshi AB, Dasgupta S, Noronha S, Bhaumik P FEBS Lett. 2024 Oct 24. doi: 10.1002/1873-3468.15045. PMID:39448541[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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