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Curr Opin Struct Biol. 2013 Aug;23(4):492-8. doi: 10.1016/ Epub 2013 Apr 27.

Molecular mechanism of the Escherichia coli maltose transporter.

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Department of Biological Sciences, Purdue University, Howard Hughes Medical Institute, 240 Martin Jischke Boulevard, West Lafayette, IN 47907, United States.


ATP-binding cassette (ABC) transporters are ubiquitous membrane proteins that import and export a large variety of materials across the lipid bilayer. A key question that drives ABC transporter research is how ATP hydrolysis is coupled to substrate translocation. This review uses the maltose transporter of Escherichia coli as a model system to understand the molecular mechanism of ABC importers. X-ray crystallography was used to capture the structures of the maltose transporter in multiple conformations. These structures, interpreted in the light of functional data, are discussed to address the following questions: first, what is the nature of conformational changes in a transport cycle? Second, how does substrate activate ATPase activity? Third, how does ATP hydrolysis enable substrate transport?

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