Structure-Function Relationship of Aminopeptidase P from Pseudomonas aeruginosa.

ABSTRACT: PepP is a virulence-associated gene in Pseudomonas aeruginosa, making it an attractive target for anti-P. aeruginosa drug development. The encoded protein, aminopeptidases P (Pa-PepP), is a type of X-prolyl peptidase that possesses diverse biological functions. The crystal structure verified its canonical pita-bread fold and functional tetrameric assembly, and the functional studies measured the influences of different metal ions on the activity. A trimetal manganese cluster was observed at the active site, elucidating the mechanism of inhibition by metal ions. Additionally, a loop extending from the active site appeared to be important for specific large-substrate binding. Based on the structural comparison and bacterial invasion assays, we showed that this non-conser

SUBMITTER: Peng CT 

PROVIDER: S-EPMC5723419 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature