Download MendeleyStructure-Function Relationship of Aminopeptidase P from Pseudomonas aeruginosa.
Peng, C.T., Liu, L., Li, C.C., He, L.H., Li, T., Shen, Y.L., Gao, C., Wang, N.Y., Xia, Y., Zhu, Y.B., Song, Y.J., Lei, Q., Yu, L.T., Bao, R.(2017) Front Microbiol 8: 2385-2385
- PubMed: 29259588
- DOI: https://doi.org/10.3389/fmicb.2017.02385
- Primary Citation of Related Structures:
5WZE - PubMed 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-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.
Organizational Affiliation:
Pharmaceutical and Biological Engineering Department, School of Chemical Engineering, Sichuan University, Chengdu, China.
