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The ATP-binding cassette family: a structural perspective

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Abstract

The ATP-binding cassette family is one of the largest groupings of membrane proteins, moving allocrites across lipid membranes, using energy from ATP. In bacteria, they reside in the inner membrane and are involved in both uptake and export. In eukaryotes, these transporters reside in the cell’s internal membranes as well as in the plasma membrane and are unidirectional—out of the cytoplasm. The range of substances that these proteins can transport is huge, which makes them interesting for structure–function studies. Moreover, their abundance in nature has made them targets for structural proteomics consortia. There are eight independent structures for ATP-binding cassette transporters, making this one of the best characterised membrane protein families. Our understanding of the mechanism of transport across membranes and membrane protein structure in general has been enhanced by recent developments for this family.

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Acknowledgements

The authors wish to acknowledge the many useful discussions, insights and explanations from the countless people who have contributed directly and indirectly to this review. In particular we would like to thank Richard Callaghan, Ian Kerr, Kenny Linton, Amy Davidson, Susan Cole, Jack Riordan, John Hunt, Geoffrey Chang, Stephen Aller, Andrew Ward, Tony George, Karl Küchler, Jim Naismith and Chris Whitfield for crystallising thoughts (as well as proteins) that have enabled this review to be written.

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  1. Department of Molecular and Cellular Biology, College of Biological Sciences, University of Guelph, Guelph, ON, N1G 2W1, Canada

    Veronica Kos

  2. Faculty of Life Sciences, Manchester Interdisplinary Biocentre, The University of Manchester, Manchester, M1 7DN, UK

    Robert Curtis Ford

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Kos, V., Ford, R.C. The ATP-binding cassette family: a structural perspective. Cell. Mol. Life Sci. 66, 3111–3126 (2009). https://doi.org/10.1007/s00018-009-0064-9

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