Related Experiment Video

Updated: Feb 16, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

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Structure-Function Relationship of Aminopeptidase P from Pseudomonas aeruginosa

Cui-Ting Peng1,2, Li Liu1,2, Chang-Cheng Li2

  • 1Pharmaceutical and Biological Engineering Department, School of Chemical Engineering, Sichuan University, Chengdu, China.

Frontiers in Microbiology
|December 21, 2017
PubMed

Insights

Pseudomonas aeruginosa

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • The gene *PepP* in *Pseudomonas aeruginosa* encodes aminopeptidases P (Pa-PepP), a crucial virulence factor.
  • Pa-PepP is an X-prolyl peptidase with essential roles in bacterial pathogenesis.

Purpose of the Study:

  • To elucidate the structural and functional characteristics of Pa-PepP.
  • To identify potential targets for anti-*P. aeruginosa* drug development.

Main Methods:

  • X-ray crystallography to determine the structure of Pa-PepP.
  • Biochemical assays to study enzyme activity and metal ion effects.
  • Bacterial invasion assays to assess virulence.

Main Results:

  • The crystal structure revealed a canonical pita-bread fold and a tetrameric assembly with a trimetal manganese cluster at the active site.
  • A unique surface loop was identified as critical for large-substrate binding and *P. aeruginosa* virulence.
  • Metal ions were shown to influence enzyme activity and potentially inhibit its function.

Conclusions:

  • Structural and functional insights into Pa-PepP provide a basis for designing specific inhibitors.
  • Targeting Pa-PepP offers a promising strategy for combating *P. aeruginosa* infections.

Keywords:
Pseudomonas aeruginosaX-ray crystallographyaminopeptidase Ptri-nuclear formvirulence

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