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Structure, mechanism and cooperation of bacterial multidrug transporters.


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Type

Article

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Authors

van Veen, Hendrik W 
Murakami, Satoshi 
Pos, Klaas M 
Luisi, Ben F 

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.

Description

Keywords

ATP-Binding Cassette Transporters, Anti-Bacterial Agents, Bacterial Proteins, Cell Membrane, Cell Wall, Drug Resistance, Multiple, Bacterial, Gram-Negative Bacteria, Membrane Transport Proteins, Protein Conformation

Journal Title

Curr Opin Struct Biol

Conference Name

Journal ISSN

0959-440X
1879-033X

Volume Title

33

Publisher

Elsevier BV
Sponsorship
Biotechnology and Biological Sciences Research Council (BB/K017713/1)
Medical Research Council (MC_PC_13059)
Human Frontier Science Program (HFSP) (RPG0034/2013)
Biotechnology and Biological Sciences Research Council (BB/I002383/1)
BL and DD are supported by the Medical Research Council (MRC), Human Frontiers Science Program (HFSP), and the Wellcome Trust. Work in the Van Veen lab is supported by the Biotechnology and Biological Sciences Research Council (BBSRC), MRC, HFSP, Royal Society, Society for Antimicrobial Chemotherapy (BSAC), Herchel Smith Foundation, and Commonwealth Trust. Work in the Pos lab is supported by the German Research Foundation (SFB 807, Transport and Communication across Biological Membranes and FOR2251, Adaptation and persistence of the emerging pathogen Acinetobacter baumannii), the DFG-EXC115 (Cluster of Excellence Macromolecular Complexes at the Goethe-University Frankfurt), Innovative Medicines Initiative Joint Undertaking Project Translocation (IMI-Translocation), EU Marie Curie Actions ITN, HFSP and the German-Israeli Foundation (GIF). The SM laboratory is supported by ERATO Murata Lipid Active Structure Project, Japan Science and Technology Agency, the Advanced Research for Medical Products Mining Program of the National Institute of Biomedical Innovation (NIBIO) and HFSP.