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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2018
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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. |
format | Online Article Text |
id | pubmed-5985334 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
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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