6W5Q

Structure of the globular C-terminal domain of P. aeruginosa LpoP

Summary for 6W5Q

• Entry DOI: 10.2210/pdb6w5q/pdb
• Descriptor: Peptidoglycan synthase activator LpoP, SULFATE ION, TRIETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: lipoprotein, activator, cell wall, protein binding
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 8
• Total formula weight: 98467.06

Authors

Caveney, N.A.,Robb, C.S.,Simorre, J.P.,Strynadka, N.C.J. (deposition date: 2020-03-13, release date: 2020-05-06, Last modification date: 2023-10-18)

Primary citation

Caveney, N.A.,Egan, A.J.F.,Ayala, I.,Laguri, C.,Robb, C.S.,Breukink, E.,Vollmer, W.,Strynadka, N.C.J.,Simorre, J.P.
Structure of the Peptidoglycan Synthase Activator LpoP in Pseudomonas aeruginosa.
Structure, 28:643-650.e5, 2020

PubMed Abstract: 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.

PubMed: 32320673
DOI: 10.1016/j.str.2020.03.012

Experimental method

X-RAY DIFFRACTION (2.2 Å)