| Literature DB >> 15805537 |
Susan Sharma1, Johnny A Davis, Tulin Ayvaz, Beth Traxler, Amy L Davidson.
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.Entities:
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Year: 2005 PMID: 15805537 PMCID: PMC1070360 DOI: 10.1128/JB.187.8.2908-2911.2005
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490