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Curr Opin Struct Biol. 2015 Aug;33:76-91. doi: 10.1016/j.sbi.2015.07.015. Epub 2015 Aug 15.

Structure, mechanism and cooperation of bacterial multidrug transporters.

Author information

1
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK.
2
Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, UK.
3
Division of Structure and Function of Biomolecules, Department of Life Science, Tokyo Institute of Technology, Yokohama 226-8503, Japan.
4
Institute of Biochemistry, Goethe Universität Frankfurt, Max-von-Laue-Straße 9, D-60438 Frankfurt, Germany.
5
Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, UK. Electronic address: bfl20@cam.ac.uk.

Abstract

Cells from all domains of life encode energy-dependent trans-membrane transporters that can expel harmful substances including clinically applied therapeutic agents. As a collective body, these transporters perform as a super-system that confers tolerance to an enormous range of harmful compounds and consequently aid survival in hazardous environments. In the Gram-negative bacteria, some of these transporters serve as energy-transducing components of tripartite assemblies that actively efflux drugs and other harmful compounds, as well as deliver virulence agents across the entire cell envelope. We draw together recent structural and functional data to present the current models for the transport mechanisms for the main classes of multi-drug transporters and their higher-order assemblies.

PMID:
26282926
DOI:
10.1016/j.sbi.2015.07.015
[Indexed for MEDLINE]
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