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The ATP switch model for ABC transporters.

Christopher F Higgins¹, Kenneth J Linton

¹MRC Clinical Sciences Centre, Imperial College Hammersmith Hospital Campus, Du Cane Road, London W12 0NN, UK. christopher.higgins@csc.mrc.ac.uk

Nature Structural & Molecular Biology

|September 29, 2004

Summary

ABC transporters move molecules across cell membranes using nucleotide-binding and transmembrane domains. The ATP-switch model explains how ATP binding and hydrolysis regulate transporter function and conformational changes.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

ATP-binding cassette (ABC) transporters are essential membrane proteins.
They facilitate the active transport of various molecules across cellular membranes.
ABC transporters consist of two nucleotide-binding domains (NBDs) and two transmembrane domains (TMDs).

Purpose of the Study:

To elucidate the mechanism of action for ABC transporters.
To explain how ATP binding and hydrolysis regulate transporter conformation and function.

Main Methods:

Biochemical assays
Structural biology techniques
Genetic studies

Main Results:

Related Experiment Videos

The ATP-switch model was developed based on recent studies.

ATP binding induces NBD dimer formation.

ATP hydrolysis causes NBD dimer dissociation.

Conclusions:

The NBD dimer cycle acts as a regulatory switch.
This switch controls conformational changes in the TMDs.
These conformational changes are critical for mediating membrane transport.