Functional Reassembly of the Escherichia coli Maltose Transporter following Purification of a MalF-MalG Subassembly

摘要

Taking advantage of a chaperone-like function of MalK, a stable complex of MalF-MalG could be solubilized from the Escherichia coli membrane and purified in high yield in the absence of MalK. This MalF-MalG complex was competent for efficient reassembly of a functional MalFGK2 maltose transporter complex both in detergent solution and in proteoliposomes.