Structure, function, and evolution of bacterial ATP-binding cassette systems.

ABSTRACT:

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 regula

SUBMITTER: Davidson AL 

PROVIDER: S-EPMC2415747 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature