6w5q

Publication Abstract from PubMed

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.

Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa.,Caveney NA, Egan AJF, Ayala I, Laguri C, Robb CS, Breukink E, Vollmer W, Strynadka NCJ, Simorre JP Structure. 2020 Apr 9. pii: S0969-2126(20)30094-0. doi:, 10.1016/j.str.2020.03.012. PMID:32320673^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.