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...

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Autores principales: Daniel Yero, Mireia Díaz-Lobo, Lionel Costenaro, Oscar Conchillo-Solé, Adrià Mayo, Mario Ferrer-Navarro, Marta Vilaseca, Isidre Gibert, Xavier Daura
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/50977891a64d4ef6a08754ef5a6e7656
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spelling oai:doaj.org-article:50977891a64d4ef6a08754ef5a6e76562021-12-02T18:15:09ZThe Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm10.1038/s42003-021-01968-82399-3642https://doaj.org/article/50977891a64d4ef6a08754ef5a6e76562021-04-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-01968-8https://doaj.org/toc/2399-3642Yero 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.Daniel YeroMireia Díaz-LoboLionel CostenaroOscar Conchillo-SoléAdrià MayoMario Ferrer-NavarroMarta VilasecaIsidre GibertXavier DauraNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-16 (2021)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
Daniel Yero
Mireia Díaz-Lobo
Lionel Costenaro
Oscar Conchillo-Solé
Adrià Mayo
Mario Ferrer-Navarro
Marta Vilaseca
Isidre Gibert
Xavier Daura
The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm
description 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.
format article
author Daniel Yero
Mireia Díaz-Lobo
Lionel Costenaro
Oscar Conchillo-Solé
Adrià Mayo
Mario Ferrer-Navarro
Marta Vilaseca
Isidre Gibert
Xavier Daura
author_facet Daniel Yero
Mireia Díaz-Lobo
Lionel Costenaro
Oscar Conchillo-Solé
Adrià Mayo
Mario Ferrer-Navarro
Marta Vilaseca
Isidre Gibert
Xavier Daura
author_sort Daniel Yero
title The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm
title_short The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm
title_full The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm
title_fullStr The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm
title_full_unstemmed The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm
title_sort pseudomonas aeruginosa substrate-binding protein ttg2d functions as a general glycerophospholipid transporter across the periplasm
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/50977891a64d4ef6a08754ef5a6e7656
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