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Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa

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Caveney, Nathanael | Egan, Alexander | Ayala, Isabel | Laguri, Cédric | Robb, Craig | Breukink, Eefjan | Vollmer, Waldemar | Strynadka, Natalie | Simorre, Jean-Pierre

Edité par CCSD ; Elsevier (Cell Press) -

International audience. Peptidoglycan (PG) is an essential component of the bacterial cell wall and is assembled from a lipid II precursor by glycosyltransferase and transpeptidase reactions catalyzed in particular by bifunctional class A penicillin-binding proteins (aPBPs). In the major clinical pathogen Pseudomonas aeruginosa, PBP1B is anchored within the cytoplasmic membrane but regulated by a bespoke outer membrane-localized lipoprotein known as LpoP. Here, we report the structure of LpoP, showing an extended N-terminal, flexible tether followed by a well-ordered C-terminal tandem-tetratricopeptide repeat domain. We show that LpoP stimulates both PBP1B transpeptidase and glycosyltransferase activities in vitro and interacts directly via its C terminus globular domain with the central UB2H domain of PBP1B. Contrary to the situation in E. coli, P. aeruginosa CpoB does not regulate PBP1B/LpoP in vitro. We propose a mechanism that helps to underscore similarities and differences in class A PBP activation across Gram-negative bacteria.

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