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Pflugers Arch. 2007 Feb;453(5):555-67. Epub 2006 Aug 26.

Structure and function of ABC transporters: the ATP switch provides flexible control.

Author information

1
MRC Clinical Sciences Centre, Imperial College Hammersmith Hospital Campus, London, UK. kenneth.linton@csc.mrc.ac.uk

Abstract

ATP-binding cassette (ABC) transporters are ubiquitous integral membrane proteins that facilitate the transbilayer movement of ligands. They comprise, minimally, two transmembrane domains, which impart ligand specificity, and two nucleotide-binding domains (NBDs), which power the transport cycle. Almost 25 years of biochemistry is reviewed in light of the recent structure analyses resulting in the ATP-switch model for function in which the NBDs switch between a dimeric conformation, closed around two molecules of ATP, and a nucleotide-free, dimeric 'open' conformation. The flexibility of this switching mechanism has evolved to provide different kinetic control for different transporters and has also been co-opted to diverse functions other than transmembrane transport.

PMID:
16937116
DOI:
10.1007/s00424-006-0126-x
[Indexed for MEDLINE]

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