TY - JOUR
T1 - Functional and structural characterization of PaeM, a colicin M-like bacteriocin produced by Pseudomonas aeruginosa
AU - Barreteau, Hélène
AU - Tiouajni, Mounira
AU - Graille, Marc
AU - Josseaume, Nathalie
AU - Bouhss, Ahmed
AU - Patin, Delphine
AU - Blanot, Didier
AU - Fourgeaud, Martine
AU - Mainardi, Jean Luc
AU - Arthur, Michel
AU - Van Tilbeurgh, Herman
AU - Mengin-Lecreulx, Dominique
AU - Touzé, Thierry
PY - 2012/10/26
Y1 - 2012/10/26
N2 - Background: Pathogenic Pseudomonas aeruginosa strains produce a colicin M-like bacteriocin exhibiting peptidoglycan lipid II-degrading activity. Results: We have determined the crystal structure of the Pseudomonas aeruginosa PaeM bacteriocin and functionally characterized its C-terminal activity domain. Conclusion: This study highlights structural plasticity of the active site of this enzyme family. Significance: The PaeM pyocin could potentially be exploited as antibacterial agent.
AB - Background: Pathogenic Pseudomonas aeruginosa strains produce a colicin M-like bacteriocin exhibiting peptidoglycan lipid II-degrading activity. Results: We have determined the crystal structure of the Pseudomonas aeruginosa PaeM bacteriocin and functionally characterized its C-terminal activity domain. Conclusion: This study highlights structural plasticity of the active site of this enzyme family. Significance: The PaeM pyocin could potentially be exploited as antibacterial agent.
U2 - 10.1074/jbc.M112.406439
DO - 10.1074/jbc.M112.406439
M3 - Article
C2 - 22977250
AN - SCOPUS:84868224059
SN - 0021-9258
VL - 287
SP - 37395
EP - 37405
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 44
ER -