3CSK: Structure Of Dpp Iii From Saccharomyces Cerevisiae

Dipeptidyl-peptidases III (DPP III) are zinc-dependent enzymes that specifically cleave the first two amino acids from the N terminus of different length peptides. In mammals, DPP III is associated with important physiological functions and is a potential biomarker for certain types of cancer. Here, we present the 1.95-A crystal structure of yeast DPP III representing the prototype for the M49 family of metallopeptidases. It shows a novel fold with two domains forming a wide cleft containing the catalytic metal ion. DPP III exhibits no overall similarity to other metallopeptidases, such as thermolysin and neprilysin, but zinc coordination and catalytically important residues are structurally conserved. Substrate recognition is accomplished by a binding site for the N terminus of the peptide at an appropriate distance from the metal center and by a series of conserved arginine residues anchoring the C termini of different length substrates.
PDB ID: 3CSKDownload
MMDB ID: 64884
PDB Deposition Date: 2008/4/10
Updated in MMDB: 2008/06
Experimental Method:
x-ray diffraction
Resolution: 1.95  Å
Source Organism:
Similar Structures:
Biological Unit for 3CSK: monomeric; determined by author and by software (PISA)
Molecular Components in 3CSK
Label Count Molecule
Protein (1 molecule)
Probable Dipeptidyl-peptidase 3(Gene symbol: YOL057W)
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB