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The ATP switch model for ABC transporters

Nature Structural & Molecular Biology volume 11, pages 918–926 (2004)Cite this article

Abstract

ABC transporters mediate active translocation of a diverse range of molecules across all cell membranes. They comprise two nucleotide-binding domains (NBDs) and two transmembrane domains (TMDs). Recent biochemical, structural and genetic studies have led to the ATP-switch model in which ATP binding and ATP hydrolysis, respectively, induce formation and dissociation of an NBD dimer. This provides an exquisitely regulated switch that induces conformational changes in the TMDs to mediate membrane transport.

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Figure 1: Schematic representation of the vitamin B12 transporter BtuCD of E. coli (PDB entry 1L7V)12.
Figure 2: Structure of the NBDs of ABC transporters.
Figure 3: The ATP switch model for the transport cycle of an ABC transporter.

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Acknowledgements

We are grateful for the contributions of many present and former members of the laboratory and collaborators, particularly R. Callaghan, R. van Veen, C. Martin, R.Ford and M. Rosenberg. We also thank many colleagues throughout the world for sharing information and stimulating discussions. The authors' research is funded by the UK Medical Research Council.

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  1. MRC Clinical Sciences Centre, Imperial College Hammersmith Hospital Campus, Du Cane Road, London, W12 0NN, UK

    Christopher F Higgins & Kenneth J Linton

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Correspondence to Christopher F Higgins.

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Higgins, C., Linton, K. The ATP switch model for ABC transporters. Nat Struct Mol Biol 11, 918–926 (2004). https://doi.org/10.1038/nsmb836

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