title: Functional reassembly of the Escherichia coli maltose transporter following purification of a MalF-MalG subassembly.
abstract: 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.
authors.affiliation: Department of Molecular Virology and Microbiology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
authors.forename: Susan
authors.initials: S
authors.lastname: Sharma
authors.forename: Johnny A
authors.initials: JA
authors.lastname: Davis
authors.forename: Tulin
authors.initials: T
authors.lastname: Ayvaz
authors.forename: Beth
authors.initials: B
authors.lastname: Traxler
authors.forename: Amy L
authors.initials: AL
authors.lastname: Davidson
mesh_terms: 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*
chemical_list: 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