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Publication Abstract from PubMed

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-conserved surface loop was critical for P. aeruginosa virulence. Taken together, these findings can extend our understanding of the catalytic mechanism and virulence-related functions of Pa-PepP and provide a solid foundation for the design of specific inhibitors against pathogenic-bacterial infections.

Structure-Function Relationship of Aminopeptidase P from Pseudomonas aeruginosa.,Peng CT, Liu L, Li CC, He LH, Li T, Shen YL, Gao C, Wang NY, Xia Y, Zhu YB, Song YJ, Lei Q, Yu LT, Bao R Front Microbiol. 2017 Dec 5;8:2385. doi: 10.3389/fmicb.2017.02385. eCollection, 2017. PMID:29259588^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.