The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm

Yero et al. elucidate the function of Ttg2D, a Pseudomonas aeruginosa periplasmic protein, in maintaining phospholipid asymmetry between the outer and inner membrane. Gram negative bacteria have inner and outer membranes that differ in phospholipd composition. Using X-ray crystallography and mass sp...

Full description

Bibliographic Details
Main Authors: Daniel Yero, Mireia Díaz-Lobo, Lionel Costenaro, Oscar Conchillo-Solé, Adrià Mayo, Mario Ferrer-Navarro, Marta Vilaseca, Isidre Gibert, Xavier Daura
Format: Article
Language:English
Published: Nature Publishing Group 2021-04-01
Series:Communications Biology
Online Access:https://doi.org/10.1038/s42003-021-01968-8
Description
Summary:Yero et al. elucidate the function of Ttg2D, a Pseudomonas aeruginosa periplasmic protein, in maintaining phospholipid asymmetry between the outer and inner membrane. Gram negative bacteria have inner and outer membranes that differ in phospholipd composition. Using X-ray crystallography and mass spectrometry, the authors show that Ttg2D can carry two diacyl glycerophospholipids or a cardiolipin. The authors also identify a role for Ttg2D in resistance against antibiotics that use a lipid-mediated pathway into the cell.
ISSN:2399-3642