The ABC maltose transporter.
Bacterial ATP-binding cassette (ABC) transporters and their homologues in eukaryotic cells form one of the largest superfamilies known today. They function as primary pumps that couple substrate translocation across the cytoplasmic membrane to ATP hydrolysis. Although ABC transporters have been studied for more than three decades, the structure of these multi-component systems is unknown, and the mechanism of transport is not understood. This article reviews one of the most widely studied ABC systems, the maltose transporter of Escherichia coli. A first structural model of the transport channel allows discussion of possible mechanisms of transport. In addition, recent experimental evidence suggests that regulation of gene expression and transport activity is far more complex than expected.
Fakultät für Biologie, Universität Konstanz, Germany. michael.ehrmann@uni-konstanz.de
M
M
Ehrmann
R
R
Ehrle
E
E
Hofmann
W
W
Boos
A
A
Schlösser
D018528:ATP-Binding Cassette Transporters / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism; D006801:Humans; D008320:Maltose / Q000378:metabolism*; D008954:Models, Biological
D018528:ATP-Binding Cassette Transporters; D008320:Maltose; D000251:Adenosine Triphosphatases