Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10537549 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2014 | 7 Pages |
Abstract
Here we report the 3Â Ã
resolution crystal structure of Bacillus licheniformis γ-GT (BlGT) and that of its complex with l-Glu. X-ray structures confirm that BlGT belongs to the N-terminal nucleophilic hydrolase superfamily and reveal that the protein possesses an opened active site cleft similar to that reported for the homologous enzyme from Bacillus subtilis, but different from those observed for human γ-GT and for γ-GTs from other microorganisms. Data suggest that the binding of l-Glu induces a reordering of the C-terminal tail of BlGT large subunit and allow the identification of a cluster of acid residues that are potentially involved in the recognition of a metal ion. The role of these residues on the conformational stability of BlGT has been studied by characterizing the autoprocessing, enzymatic activity, chemical and thermal denaturation of four new Ala single mutants. The results show that replacement of Asp568 with an Ala affects both the autoprocessing and structural stability of the protein.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Long-Liu Lin, Yi-Yu Chen, Meng-Chun Chi, Antonello Merlino,