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Microbiology and Molecular Biology Reviews, June 2008, p. 317-364, Vol. 72, No. 2
1092-2172/08/$08.00+0     doi:10.1128/MMBR.00031-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems

Amy L. Davidson,1* Elie Dassa,2 Cedric Orelle,1 and Jue Chen3

Department of Chemistry, Purdue University, West Lafayette, Indiana 47907,1 Unité des Membranes Bactériennes, CNRS URA2172, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France,2 Department of Biology, Purdue University, West Lafayette, Indiana 479073

Summary: ATP-binding cassette (ABC) systems are universally distributed among living organisms and function in many different aspects of bacterial physiology. ABC transporters are best known for their role in the import of essential nutrients and the export of toxic molecules, but they can also mediate the transport of many other physiological substrates. In a classical transport reaction, two highly conserved ATP-binding domains or subunits couple the binding/hydrolysis of ATP to the translocation of particular substrates across the membrane, through interactions with membrane-spanning domains of the transporter. Variations on this basic theme involve soluble ABC ATP-binding proteins that couple ATP hydrolysis to nontransport processes, such as DNA repair and gene expression regulation. Insights into the structure, function, and mechanism of action of bacterial ABC proteins are reported, based on phylogenetic comparisons as well as classic biochemical and genetic approaches. The availability of an increasing number of high-resolution structures has provided a valuable framework for interpretation of recent studies, and realistic models have been proposed to explain how these fascinating molecular machines use complex dynamic processes to fulfill their numerous biological functions. These advances are also important for elucidating the mechanism of action of eukaryotic ABC proteins, because functional defects in many of them are responsible for severe human inherited diseases.

* Corresponding author. Mailing address: Department of Chemistry, 560 Oval Drive, Purdue University, West Lafayette, IN 47907. Phone: (765) 494-5291. Fax: (765) 494-0239. E-mail: adavidso{at}purdue.edu

Microbiology and Molecular Biology Reviews, June 2008, p. 317-364, Vol. 72, No. 2
1092-2172/08/$08.00+0     doi:10.1128/MMBR.00031-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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