Data on the crystal structures of β-glucosidase from Thermoanaerobacterium saccharolyticum

Abstract

β-Glucosidase (Bgl) is a biomass-degrading enzyme that hydrolyzes cellobiose and glucose-substituted polysaccharides into glucose, playing a crucial role in enzymatic saccharification during biofuel production. Despite the wealth of structural information available on Bgl, the molecular properties of the loops above the substrate-binding pocket remain unexplored. In previous study, to better understand the molecular functions of these loop regions, four crystal structures of Thermoanaerobacterium saccharolyticum Bgl (TsaBgl) were determined. The molecular flexibility and conformational changes of the loop regions in TsaBgl were analysed, expanding our understanding of their roles in the Bgl family. The data processing and structure determination details provided here are valuable for further studies on the structural properties of these loop regions.