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Antibiotic resistance mediated by the MacB ABC transporter family : a structural and functional perspective

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Greene, Nicholas P., Kaplan, Elise, Crow, Allister and Koronakis, Vassilis (2018) Antibiotic resistance mediated by the MacB ABC transporter family : a structural and functional perspective. Frontiers in Microbiology, 9 . 950. doi:10.3389/fmicb.2018.00950 ISSN 1664-302X.

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Official URL: http://dx.doi.org/10.3389/fmicb.2018.00950

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Abstract

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.

Item Type: Journal Article
Subjects: Q Science > QR Microbiology
R Medicine > RM Therapeutics. Pharmacology
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Drug resistance in microorganisms, Antibiotics
Journal or Publication Title: Frontiers in Microbiology
Publisher: Frontiers Research Foundation
ISSN: 1664-302X
Official Date: 28 May 2018
Dates:
DateEvent
28 May 2018Published
24 April 2018Accepted
Volume: 9
Article Number: 950
DOI: 10.3389/fmicb.2018.00950
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons)
Date of first compliant deposit: 29 May 2018
Date of first compliant Open Access: 30 May 2018
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
MR/N000994/1[MRC] Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
101828/Z/13/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269

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