Functional reassembly of the Escherichia coli maltose transporter following purification of a MalF-MalG subassembly.
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 MalFGK(2) maltose transporter complex both in detergent solution and in proteoliposomes.
Sharma
Susan
S
Department of Molecular Virology and Microbiology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Davis
Johnny A
JA
Ayvaz
Tulin
T
Traxler
Beth
B
Davidson
Amy L
AL
D018528:ATP-Binding Cassette Transporters / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D008320:Maltose / Q000378:metabolism; D009004:Monosaccharide Transport Proteins / Q000378:metabolism*
D018528:ATP-Binding Cassette Transporters; D029968:Escherichia coli Proteins; C461639:MalF protein, E coli; C079123:MalG protein, E coli; C489398:MalK protein, E coli; D009004:Monosaccharide Transport Proteins; C461599:maltose transport system, E coli; D008320:Maltose