6W5Q

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

6W5Q の概要

• エントリーDOI: 10.2210/pdb6w5q/pdb
• 分子名称: Peptidoglycan synthase activator LpoP, SULFATE ION, TRIETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: lipoprotein, activator, cell wall, protein binding
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 98467.06

構造登録者

Caveney, N.A.,Robb, C.S.,Simorre, J.P.,Strynadka, N.C.J. (登録日: 2020-03-13, 公開日: 2020-05-06, 最終更新日: 2023-10-18)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)