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  • Review Article
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ABC transporters: the power to change

Nature Reviews Molecular Cell Biology volume 10, pages 218–227 (2009)Cite this article

Key Points

  • ATP-binding cassette (ABC) transporters constitute a ubiquitous superfamily of integral membrane proteins that are responsible for the ATP-powered translocation of many substrates across membranes.

  • ABC transporters have a characteristic architecture that consists minimally of four domains: two ABC domains (or nucleotide-binding domains) with highly conserved sequence motifs and two transmembrane domains (TMDs). Additional domains can be fused to these core elements to confer regulatory functions, and a periplasmic binding protein is required for ligand delivery to prokaryotic importer members of this family.

  • Similarities in the structure of the ABC domains structure support a common mechanism by which ABC transporters, both importers and exporters, orchestrate a series of nucleotide- and substrate-dependent conformational changes that result in substrate translocation across the membrane through an 'alternating-access'-type model. As ABC domains are also integrated into non-transport systems, including proteins that are involved in DNA repair and chromosome maintenance, it is likely that a common set of ATP-dependent conformational changes are relevant to all of these processes.

  • The conformation of ABC transporters that is catalytically competent for nucleotide hydrolysis involves the binding of an ATP molecule between conserved sequence motifs at the interface between the two ABC domains. As a transporter cycles through the different stages of nucleotide binding and hydrolysis, the interface between the two ABC domains switches from the closed state, which is characteristic of ATP binding, to a more open conformation, which is associated with non-ATP states.

  • TMDs are structurally heterogeneous, and three distinct sets of folds have been recognized. Although the detailed folds vary, they all interact with the helical domains of the ABCs through 'coupling helices', which are located in the loops between membrane-spanning helices. These interactions connect the conformations of the TMDs to the nucleotide state of the ABC domains.

  • The activity of ABC transporters can be regulated at the level of protein function through the actions of domains that are fused to the ABCs and/or TMDs. Recent structural studies have established that trans-inhibition, in which the uptake of an extracellular substrate is inhibited by increasing intracellular concentrations of that species, can involve ligand binding to the carboxy-terminal domains of the ABCs that sterically separate these domains and prevent their association, which is required for ATP hydrolysis.

  • Although idealized kinetic models can be described that qualitatively highlight aspects of the transport mechanism, an important goal is to develop quantitative models that detail the kinetic and molecular mechanisms by which ABC transporters couple the binding and hydrolysis of ATP to substrate translocation.

Abstract

ATP-binding cassette (ABC) transporters constitute a ubiquitous superfamily of integral membrane proteins that are responsible for the ATP-powered translocation of many substrates across membranes. The highly conserved ABC domains of ABC transporters provide the nucleotide-dependent engine that drives transport. By contrast, the transmembrane domains that create the translocation pathway are more variable. Recent structural advances with prokaryotic ABC transporters have provided a qualitative molecular framework for deciphering the transport cycle. An important goal is to develop quantitative models that detail the kinetic and molecular mechanisms by which ABC transporters couple the binding and hydrolysis of ATP to substrate translocation.

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Figure 1: Molecular architecture of ABC transporters.
Figure 2: Structure and dimer interactions of an ABC subunit.
Figure 3: Polypeptide folds of a single transmembrane domain in ABC transporters.
Figure 4: Nucleotide–protein interactions in the active sites of various ATPases.
Figure 5: Relationships between dimeric ABC structures.

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Acknowledgements

We thank A.T. Lee and J.B. Howard for discussions and their long-term contributions to our research in this area. The support of the Fulbright Foundation and Jane Coffin Childs Memorial Funds for Medical Research (O.L.) and National Institutes of Health grant GM45162 (D.C.R) is gratefully acknowledged.

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  1. Division of Chemistry and Chemical Engineering 114-96, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, 91125, California, USA

    Douglas C. Rees, Eric Johnson & Oded Lewinson

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DATABASES

Protein Data Bank

1H8E

1L7V

1M34

1Q12

2HYD

2ONJ

2ONK

2NQ2

2QI9

2R6G

3B5W

3B5X

3B5Z

3B60

3D31

3DHW

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Glossary

ABC

(ATP-binding cassette). A set of conserved sequence motifs that defines an eponymous family of ATPases. ABC is often used interchangeably with nucleotide-binding domain (NBD).

BtuCD

The vitamin B12 uptake system that is composed of the integral membrane protein subunit BtuC and the ATP-binding cassette subunit BtuD.

Sav1866

A bacterial ATP-binding cassette exporter from Staphylococcus aureus that is homologous to eukaryotic multidrug resistance transporters.

MalFGK2

A maltose transporter, which is composed of two homologous integral membrane subunits — MalF and MalG — and two copies of the ATP-binding cassette subunit MalK.

F1-ATPase

A stable, water-soluble subassembly of the membrane-bound ATP synthase, of which the active site for ATP synthesis and hydrolysis is located at the interface between homologous α- and β-subunits.

Nitrogenase

The enzyme system that catalyses the ATP-dependent reduction of dinitrogen to ammonia during the process of biological nitrogen fixation. The nitrogenase Fe-protein contains the binding site for ATP.

G protein

One of a family of GTP-binding proteins that are involved in signal transduction, in which GTP binding and hydrolysis and subsequent nucleotide exchange drive a series of conformational changes that are used in signalling cascades.

AAA+ ATPase

(ATPases associated with diverse cellular activities). A large family of structurally conserved ATPases in which assembly of the ATPase active site requires subunit oligomerization.

MetNI

A Met transporter, which is composed of the integral membrane protein MetI and the ATP-binding cassette subunit MetN.

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Rees, D., Johnson, E. & Lewinson, O. ABC transporters: the power to change. Nat Rev Mol Cell Biol 10, 218–227 (2009). https://doi.org/10.1038/nrm2646

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