Abstract
The three-dimensional structure of Salmonella typhimurium aspartyl dipeptidase, peptidase E, was solved crystallographically and refined to 1.2-Å resolution, The structure of this 25-kDa enzyme consists of two mixed β-sheets forming a V, flanked by six α-helices. The active site contains a Ser-His-Glu catalytic triad and is the first example of a serine peptidase/protease with a glutamate in the catalytic triad. The active site Ser is located on a strand-helix motif reminiscent of that found in α/β-hydrolases, but the polypeptide fold and the organization of the catalytic triad differ from those of the known serine proteases. This enzyme is a member of a family of serine hydrolases and appears to represent a new example of convergent evolution of peptidase activity.
Original language | English |
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Pages (from-to) | 14097-14102 |
Number of pages | 6 |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 97 |
Issue number | 26 |
DOIs | |
Publication status | Published - Dec 19 2000 |
Externally published | Yes |
Keywords
- Peptidase E
- Protease
- Protein crystallography
- Serine hydrolase
ASJC Scopus subject areas
- General