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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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

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spelling	doaj-50977891a64d4ef6a08754ef5a6e76562021-04-11T11:26:13ZengNature Publishing GroupCommunications Biology2399-36422021-04-014111610.1038/s42003-021-01968-8The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasmDaniel Yero0Mireia Díaz-Lobo1Lionel Costenaro2Oscar Conchillo-Solé3Adrià Mayo4Mario Ferrer-Navarro5Marta Vilaseca6Isidre Gibert7Xavier Daura8Institut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB)Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyInstitut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB)Institut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB)Institut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB)Institut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB)Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyInstitut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB)Institut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB)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.https://doi.org/10.1038/s42003-021-01968-8
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Daniel Yero Mireia Díaz-Lobo Lionel Costenaro Oscar Conchillo-Solé Adrià Mayo Mario Ferrer-Navarro Marta Vilaseca Isidre Gibert Xavier Daura
spellingShingle	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 Communications Biology
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 Publishing Group
series	Communications Biology
issn	2399-3642
publishDate	2021-04-01
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.
url	https://doi.org/10.1038/s42003-021-01968-8
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The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm

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