The maltose transport complex of E.coli is one of the most well-characterized members of the ATP-Binding Cassette (ABC) protein superfamily. ABC proteins represent the largest superfamily of transmembrane proteins in prokaryotes and eukaryotes, performing diverse functions from ion transport by the cystic fibrosis transmembrane regulator to multiple drug efflux by the P-glycoprotein transporter and sugar transport by the maltose transporter. Characterization of the mechanism of transport for ABC transporters is currently being investigated both biochemically and structurally, however some uncertainty remains as to how the individual subunits of these multisubunit transporters interact. This review discusses the current knowledge of the mechanism of maltose transport, as it relates to the ABC superfamily of transporters as a whole.