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Published March 2009 | Supplemental Material + Accepted Version
Journal Article Open

ABC transporters: the power to change

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.

Additional Information

© 2009 Nature Publishing Group. 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.

Attached Files

Accepted Version - nihms177334.pdf

Supplemental Material - Rees2009p9610.1038nrm2646_supp.pdf

Supplemental Material - Rees2009p9610.1038nrm2646_supp_2.pdf

Supplemental Material - Rees2009p9610.1038nrm2646_supp_3.pdf

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