1LNS: Crystal Structure Analysis Of The X-prolyl Dipeptidyl Aminopeptidase From Lactococcus Lactis

Citation:
Abstract
The X-prolyl dipeptidyl aminopeptidase (X-PDAP) from Lactococcus lactis is a dimeric enzyme catalyzing the removal of Xaa-Pro dipeptides from the N terminus of peptides. The structure of the enzyme was solved at 2.2 A resolution and provides a model for the peptidase family S15. Each monomer is composed of four domains. The larger one presents an alpha/beta hydrolase fold and comprises the active site serine. The specificity pocket is mainly built by residues from a small helical domain which is, together with the N-terminal domain, essential for dimerization. A C-terminal moiety probably plays a role in the tropism of X-PDAP toward the cellular membrane. These results give new insights for further exploration of the role of the enzymes of the SC clan.
PDB ID: 1LNSDownload
MMDB ID: 20922
PDB Deposition Date: 2002/5/3
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
Similar Structures:
Biological Unit for 1LNS: dimeric; determined by author
Molecular Components in 1LNS
Label Count Molecule
Proteins (2 molecules)
2
X-prolyl Dipeptidyl Aminopeptidase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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