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Evolution toward maximum transport capacity of the Ttg2 ABC system in Pseudomonas aeruginosa

View ORCID ProfileDaniel Yero, View ORCID ProfileLionel Costenaro, View ORCID ProfileOscar Conchillo-Solé, Mireia Díaz-Lobo, Adrià Mayo, View ORCID ProfileMario Ferrer-Navarro, View ORCID ProfileMarta Vilaseca, View ORCID ProfileIsidre Gibert, View ORCID ProfileXavier Daura
doi: https://doi.org/10.1101/834812
Daniel Yero
1Institut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB), Barcelona, Spain
2Departament de Genètica i de Microbiologia, UAB, Barcelona, Spain
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Lionel Costenaro
1Institut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB), Barcelona, Spain
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Oscar Conchillo-Solé
1Institut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB), Barcelona, Spain
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Mireia Díaz-Lobo
3Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona, Spain
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Adrià Mayo
1Institut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB), Barcelona, Spain
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Mario Ferrer-Navarro
1Institut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB), Barcelona, Spain
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Marta Vilaseca
3Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Barcelona, Spain
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Isidre Gibert
1Institut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB), Barcelona, Spain
2Departament de Genètica i de Microbiologia, UAB, Barcelona, Spain
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  • For correspondence: Xavier.Daura@uab.cat Isidre.Gibert@uab.cat
Xavier Daura
1Institut de Biotecnologia i de Biomedicina (IBB), Universitat Autònoma de Barcelona (UAB), Barcelona, Spain
4Catalan Institution for Research and Advanced Studies (ICREA), Barcelona, Spain
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  • For correspondence: Xavier.Daura@uab.cat Isidre.Gibert@uab.cat
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Abstract

In Pseudomonas aeruginosa, Ttg2D is the soluble periplasmic phospholipid-binding component of an ABC transport system thought to be involved in maintaining the asymmetry of the outer membrane. The crystallographic structure of Ttg2D at 2.5Å resolution reveals that this protein can bind two diacyl phospholipids. Native and denaturing mass spectrometry experiments confirm that Ttg2D binds two phospholipid molecules, which may have different head groups. Analysis of the available structures of Ttg2D orthologs allowed us to classify this protein family as a novel substrate-binding protein fold and to venture the evolutionary events that differentiated the orthologs binding one or two phospholipids. In addition, gene knockout experiments in P. aeruginosa PAO1 and multidrug-resistant strains show that disruption of this system leads to outer membrane permeabilization. This demonstrates the role of this system in low-level intrinsic resistance against certain antibiotics that use a lipid-mediated pathway to permeate through membranes.

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  • https://www.rcsb.org/structure/6HSY

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Posted November 08, 2019.
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Evolution toward maximum transport capacity of the Ttg2 ABC system in Pseudomonas aeruginosa
Daniel Yero, Lionel Costenaro, Oscar Conchillo-Solé, Mireia Díaz-Lobo, Adrià Mayo, Mario Ferrer-Navarro, Marta Vilaseca, Isidre Gibert, Xavier Daura
bioRxiv 834812; doi: https://doi.org/10.1101/834812
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Evolution toward maximum transport capacity of the Ttg2 ABC system in Pseudomonas aeruginosa
Daniel Yero, Lionel Costenaro, Oscar Conchillo-Solé, Mireia Díaz-Lobo, Adrià Mayo, Mario Ferrer-Navarro, Marta Vilaseca, Isidre Gibert, Xavier Daura
bioRxiv 834812; doi: https://doi.org/10.1101/834812

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