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Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective

The MacB ABC transporter forms a tripartite efflux pump with the MacA adaptor protein and TolC outer membrane exit duct to expel antibiotics and export virulence factors from Gram-negative bacteria. Here, we review recent structural and functional data on MacB and its homologs. MacB has a fold that...

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Autores principales: Greene, Nicholas P., Kaplan, Elise, Crow, Allister, Koronakis, Vassilis
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5985334/
https://www.ncbi.nlm.nih.gov/pubmed/29892271
http://dx.doi.org/10.3389/fmicb.2018.00950
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author Greene, Nicholas P.
Kaplan, Elise
Crow, Allister
Koronakis, Vassilis
author_facet Greene, Nicholas P.
Kaplan, Elise
Crow, Allister
Koronakis, Vassilis
author_sort Greene, Nicholas P.
collection PubMed
description The MacB ABC transporter forms a tripartite efflux pump with the MacA adaptor protein and TolC outer membrane exit duct to expel antibiotics and export virulence factors from Gram-negative bacteria. Here, we review recent structural and functional data on MacB and its homologs. MacB has a fold that is distinct from other structurally characterized ABC transporters and uses a unique molecular mechanism termed mechanotransmission. Unlike other bacterial ABC transporters, MacB does not transport substrates across the inner membrane in which it is based, but instead couples cytoplasmic ATP hydrolysis with transmembrane conformational changes that are used to perform work in the extra-cytoplasmic space. In the MacAB-TolC tripartite pump, mechanotransmission drives efflux of antibiotics and export of a protein toxin from the periplasmic space via the TolC exit duct. Homologous tripartite systems from pathogenic bacteria similarly export protein-like signaling molecules, virulence factors and siderophores. In addition, many MacB-like ABC transporters do not form tripartite pumps, but instead operate in diverse cellular processes including antibiotic sensing, cell division and lipoprotein trafficking.
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spelling pubmed-59853342018-06-11 Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective Greene, Nicholas P. Kaplan, Elise Crow, Allister Koronakis, Vassilis Front Microbiol Microbiology The MacB ABC transporter forms a tripartite efflux pump with the MacA adaptor protein and TolC outer membrane exit duct to expel antibiotics and export virulence factors from Gram-negative bacteria. Here, we review recent structural and functional data on MacB and its homologs. MacB has a fold that is distinct from other structurally characterized ABC transporters and uses a unique molecular mechanism termed mechanotransmission. Unlike other bacterial ABC transporters, MacB does not transport substrates across the inner membrane in which it is based, but instead couples cytoplasmic ATP hydrolysis with transmembrane conformational changes that are used to perform work in the extra-cytoplasmic space. In the MacAB-TolC tripartite pump, mechanotransmission drives efflux of antibiotics and export of a protein toxin from the periplasmic space via the TolC exit duct. Homologous tripartite systems from pathogenic bacteria similarly export protein-like signaling molecules, virulence factors and siderophores. In addition, many MacB-like ABC transporters do not form tripartite pumps, but instead operate in diverse cellular processes including antibiotic sensing, cell division and lipoprotein trafficking. Frontiers Media S.A. 2018-05-28 /pmc/articles/PMC5985334/ /pubmed/29892271 http://dx.doi.org/10.3389/fmicb.2018.00950 Text en Copyright © 2018 Greene, Kaplan, Crow and Koronakis. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Greene, Nicholas P.
Kaplan, Elise
Crow, Allister
Koronakis, Vassilis
Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective
title Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective
title_full Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective
title_fullStr Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective
title_full_unstemmed Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective
title_short Antibiotic Resistance Mediated by the MacB ABC Transporter Family: A Structural and Functional Perspective
title_sort antibiotic resistance mediated by the macb abc transporter family: a structural and functional perspective
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5985334/
https://www.ncbi.nlm.nih.gov/pubmed/29892271
http://dx.doi.org/10.3389/fmicb.2018.00950
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