8Z2X

Crystal structure of exo-beta-(1,3)-glucanase from Aspergillus oryzae (AoBgl) as a complex with cellobiose

Summary for 8Z2X

• Entry DOI: 10.2210/pdb8z2x/pdb
• Related PRD ID: PRD_900005
• Descriptor: Glucan 1,3-beta-glucosidase A, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: cellobiose, glucose, exoglucanase, aspergillus oryzae, gh5, laminarin, laminaritriose, hydrolase
• Biological source: Aspergillus oryzae
• Total number of polymer chains: 1
• Total formula weight: 45967.78

Authors

Banerjee, B.,Kamale, C.K.,Suryawanshi, A.B.,Bhaumik, P. (deposition date: 2024-04-13, release date: 2024-11-06, Last modification date: 2025-01-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.73 Å)