1FY2

Aspartyl Dipeptidase

Summary for 1FY2

• Entry DOI: 10.2210/pdb1fy2/pdb
• Related: 1FYE
• Descriptor: ASPARTYL DIPEPTIDASE, CADMIUM ION (3 entities in total)
• Functional Keywords: serine protease, peptidase, catalytic triad, strand-helix motif, hydrolase
• Biological source: Salmonella typhimurium
• Cellular location: Cytoplasm: P36936
• Total number of polymer chains: 1
• Total formula weight: 24905.71

Authors

Hakansson, K.,Wang, A.H.-J.,Miller, C.G. (deposition date: 2000-09-28, release date: 2001-01-10, Last modification date: 2024-02-07)

Primary citation

Hakansson, K.,Wang, A.H.,Miller, C.G.
The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad.
Proc.Natl.Acad.Sci.USA, 97:14097-14102, 2000

PubMed Abstract: The three-dimensional structure of Salmonella typhimurium aspartyl dipeptidase, peptidase E, was solved crystallographically and refined to 1.2-A resolution. The structure of this 25-kDa enzyme consists of two mixed beta-sheets forming a V, flanked by six alpha-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 alpha/beta-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.

PubMed: 11106384
DOI: 10.1073/pnas.260376797

Experimental method

X-RAY DIFFRACTION (1.2 Å)