The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad

Kjell Håkansson, Andrew H.J. Wang, Charles G. Miller

Research output: Contribution to journalArticlepeer-review

36 Citations (Scopus)

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 languageEnglish
Pages (from-to)14097-14102
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume97
Issue number26
DOIs
Publication statusPublished - Dec 19 2000
Externally publishedYes

Keywords

  • Peptidase E
  • Protease
  • Protein crystallography
  • Serine hydrolase

ASJC Scopus subject areas

  • General

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