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. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
CITATION STYLE
Barreteau, H., Tiouajni, M., Graille, M., Josseaume, N., Bouhss, A., Patin, D., … Touzé, T. (2012). Functional and structural characterization of PaeM, a colicin M-like bacteriocin produced by Pseudomonas aeruginosa. Journal of Biological Chemistry, 287(44), 37395–37405. https://doi.org/10.1074/jbc.M112.406439
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