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FEBS Lett. 1994 Jun 6;346(1):55-8.

Maltose transport system of Escherichia coli: an ABC-type transporter.

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Department of Molecular and Cell Biology, University of California, Berkeley 94720.


The maltose transport system of E. coli is composed of a periplasmic maltose-binding protein (MBP), the presumed transmembrane channel made up of MalF and MalG proteins, and two copies of the ATPase subunit, MalK. The membrane-associated transporter complex was purified in a functional form both from the wild-type strain and from mutants that do not require MBP for transport, and was reconstituted into proteoliposomes. A major function of MBP is to send a transmembrane signal, in the presence of ligands, to the ATPase subunits on the inner side of the membrane. In addition, MBP performs a special function in the translocation of the larger ligands, maltodextrins, perhaps by aligning them for entry into the channel.

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