1AZW

PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI

Summary for 1AZW

• Entry DOI: 10.2210/pdb1azw/pdb
• Descriptor: PROLINE IMINOPEPTIDASE (2 entities in total)
• Functional Keywords: aminopeptidase, proline iminopeptidase, serine protease, xanthomonas campestris
• Biological source: Xanthomonas citri
• Cellular location: Cytoplasm (By similarity): P52279
• Total number of polymer chains: 2
• Total formula weight: 71041.49

Authors

Medrano, F.J.,Alonso, J.,Garcia, J.L.,Romero, A.,Bode, W.,Gomis-Ruth, F.X. (deposition date: 1997-11-22, release date: 1999-01-13, Last modification date: 2024-02-07)

Primary citation

Medrano, F.J.,Alonso, J.,Garcia, J.L.,Romero, A.,Bode, W.,Gomis-Ruth, F.X.
Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family.
EMBO J., 17:1-9, 1998

PubMed Abstract: The proline iminopeptidase from Xanthomonas campestris pv. citri is a serine peptidase that catalyses the removal of N-terminal proline residues from peptides with high specificity. We have solved its three-dimensional structure by multiple isomorphous replacement and refined it to a crystallographic R-factor of 19.2% using X-ray data to 2.7 A resolution. The protein is folded into two contiguous domains. The larger domain shows the general topology of the alpha/beta hydrolase fold, with a central eight-stranded beta-sheet flanked by two helices and the 11 N-terminal residues on one side, and by four helices on the other side. The smaller domain is placed on top of the larger domain and essentially consists of six helices. The active site, located at the end of a deep pocket at the interface between both domains, includes a catalytic triad of Ser110, Asp266 and His294. Cys269, located at the bottom of the active site very close to the catalytic triad, presumably accounts for the inhibition by thiol-specific reagents. The overall topology of this iminopeptidase is very similar to that of yeast serine carboxypeptidase. The striking secondary structure similarity to human lymphocytic prolyl oligopeptidase and dipeptidyl peptidase IV makes this proline iminopeptidase structure a suitable model for the three-dimensional structure of other peptidases of this family.

PubMed: 9427736
DOI: 10.1093/emboj/17.1.1

Experimental method

X-RAY DIFFRACTION (2.7 Å)