Xinquan Wang,Xiangyuan He,Shoujun Yang,Xiaomin An,Wenrui Chang, andDongcai Liang
The three-dimensional structure of a thermostable β-glycosidase (GlyTn) from the thermophilic eubacterium Thermus nonproteolyticus HG102 was determined at a resolution of 2.4 Å. The core of the structure adopts the (βα)8 barrel fold. The sequence alignments and the positions of the two Glu residues in the active center indicate that GlyTn belongs to the glycosyl hydrolases of retaining family 1. We have analyzed the structural features of GlyTn related to the thermostability and compared its structure with those of other mesophilic glycosidases from plants, eubacteria, and hyperthermophilic enzymes from archaea. Several possible features contributing to the thermostability of GlyTn were elucidated.
