1np2
Crystal structure of thermostable beta-glycosidase from thermophilic eubacterium Thermus nonproteolyticus HG102
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OverviewOverview
The three-dimensional structure of a thermostable beta-glycosidase, (Gly(Tn)) from the thermophilic eubacterium Thermus nonproteolyticus HG102, was determined at a resolution of 2.4 A. The core of the structure adopts, the (betaalpha)(8) barrel fold. The sequence alignments and the positions, of the two Glu residues in the active center indicate that Gly(Tn) belongs, to the glycosyl hydrolases of retaining family 1. We have analyzed the, structural features of Gly(Tn) 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 Gly(Tn) were elucidated.
About this StructureAbout this Structure
1NP2 is a Single protein structure of sequence from Thermus nonproteolyticus. Active as Beta-glucosidase, with EC number 3.2.1.21 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for thermostability of beta-glycosidase from the thermophilic eubacterium Thermus nonproteolyticus HG102., Wang X, He X, Yang S, An X, Chang W, Liang D, J Bacteriol. 2003 Jul;185(14):4248-55. PMID:12837801
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