5WZE

The structure of Pseudomonas aeruginosa aminopeptidase PepP

Summary for 5WZE

• Entry DOI: 10.2210/pdb5wze/pdb
• Descriptor: Aminopeptidase P, 1,2-ETHANEDIOL, SODIUM ION, ... (11 entities in total)
• Functional Keywords: aminopeptidase, pseudomonas aeruginosa, pathogenicity, hydrolase
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 4
• Total formula weight: 206089.67

Authors

Bao, R.,Peng, C.T.,Liu, L.,He, L.H.,Li, C.C.,Li, T.,Shen, Y.L.,Zhu, Y.B.,Song, Y.J. (deposition date: 2017-01-17, release date: 2018-01-17, Last modification date: 2023-11-22)

Primary citation

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.
Structure-Function Relationship of Aminopeptidase P from Pseudomonas aeruginosa.
Front Microbiol, 8:2385-2385, 2017

PubMed Abstract: is a virulence-associated gene in , making it an attractive target for anti 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 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.

PubMed: 29259588
DOI: 10.3389/fmicb.2017.02385

Experimental method

X-RAY DIFFRACTION (1.783 Å)