title: 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.
authors.affiliation: Division of Chemistry and Chemical Engineering 114-96, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, California 91125, USA. dcrees@caltech.edu
authors.forename: Douglas C
authors.initials: DC
authors.lastname: Rees
authors.forename: Eric
authors.initials: E
authors.lastname: Johnson
authors.forename: Oded
authors.initials: O
authors.lastname: Lewinson
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D001692:Biological Transport / Q000235:genetics; D019281:Dimerization; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D018528:ATP-Binding Cassette Transporters