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...
Main Authors: | , , , , , , , , |
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Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2021-04-01
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Series: | Communications Biology |
Online Access: | https://doi.org/10.1038/s42003-021-01968-8 |
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. |
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ISSN: | 2399-3642 |