8Z2Y

High-resolution crystal structure of exo-beta-(1,3)-glucanase from Aspergillus oryzae (AoBgl) as a complex with glucose

8Z2Y の概要

• エントリーDOI: 10.2210/pdb8z2y/pdb
• 分子名称: Glucan 1,3-beta-glucosidase A, 1,2-ETHANEDIOL, GLYCEROL, ... (7 entities in total)
• 機能のキーワード: cellobiose, glucose, exoglucanase, aspergillus oryzae, gh5, laminarin, laminaritriose, hydrolase
• 由来する生物種: Aspergillus oryzae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45907.19

構造登録者

Banerjee, B.,Kamale, C.K.,Suryawanshi, A.B.,Bhaumik, P. (登録日: 2024-04-13, 公開日: 2024-11-06, 最終更新日: 2025-01-29)

主引用文献

Banerjee, B.,Kamale, C.K.,Suryawanshi, A.B.,Dasgupta, S.,Noronha, S.,Bhaumik, P.
Crystal structures of Aspergillus oryzae exo-beta-(1,3)-glucanase reveal insights into oligosaccharide binding, recognition, and hydrolysis.
Febs Lett., 599:53-73, 2025

PubMed Abstract: Exo-β-(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-β-(1,3)-glucanase (AoBgl) belonging to the GH5 family. Purified AoBgl hydrolyses β-(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 Å, (b) the complexed form with bound cellobiose at 1.73 Å and (c) the glucose-bound form at 1.20 Å. 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.

PubMed: 39448541
DOI: 10.1002/1873-3468.15045

実験手法

X-RAY DIFFRACTION (1.2 Å)