The ATP-binding cassette (ABC) transporters are primary transporters that couple the energy stored in adenosine triphosphate (ATP) to the movement of molecules across the membrane. ABC transporters can be divided into exporters and importers; importers mediate the uptake of essential nutrients into cells and are found predominantly in prokaryotes whereas exporters transport molecules out of cells or into organelles and are found in all organisms. ABC exporters have been linked with multi-drug resistance in both bacterial and eukaryotic cells. ABC transporters are powered by the hydrolysis of ATP and transport their substrate via the alternating access mechanism, whereby the protein alternates between a conformation in which the substrate-binding site is accessible from the outside of the membrane, outward-facing and one in which it is inward-facing. In this mini-review, the structures of different ABC transporter types in different conformations are presented within the context of the alternating access mechanism and how they have shaped our current understanding of the mechanism of ABC transporters.
Review Article| October 09 2015
Structural basis for the mechanism of ABC transporters
Konstantinos Beis 1
*Department of Life Sciences, Imperial College London, Exhibition Road, London, South Kensington, SW7 2AZ, U.K.
†Membrane Protein Lab, Diamond Light Source, Harwell Science and Innovation Campus, Chilton, Oxfordshire, OX11 0DE, U.K.
‡Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot, Oxfordshire OX11 0FA, U.K.
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Konstantinos Beis; Structural basis for the mechanism of ABC transporters. Biochem Soc Trans 1 October 2015; 43 (5): 889–893. doi: https://doi.org/10.1042/BST20150047
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