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.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1070360 | PMC |
| http://dx.doi.org/10.1128/JB.187.8.2908-2911.2005 | DOI Listing |
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