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• W2027718963 abstract "The ATP binding cassette (ABC) transporter LmrA from the bacterium Lactococcus lactis is a homolog of the human multidrug resistance P-glycoprotein (ABCB1), the activity of which impairs the efficacy of chemotherapy. In a previous study, LmrA was shown to mediate ethidium efflux by an ATP-dependent proton-ethidium symport reaction in which the carboxylate E314 is critical. The functional importance of this key residue for ABC proteins was suggested by its conservation in a wider family of related transporters; however, the structural basis of its role was not apparent. Here, we have used homology modeling to define the structural environment of E314. The residue is nested in a hydrophobic environment that probably elevates its pKa, accounting for the pH dependency of drug efflux that we report in this work. Functional analyses of wild-type and mutant proteins in cells and proteoliposomes support our proposal for the mechanistic role of E314 in proton-coupled ethidium transport. As the carboxylate is known to participate in proton translocation by secondary-active transporters, our observations suggest that this substituent can play a similar role in the activity of ABC transporters." @default.
• W2027718963 created "2016-06-24" @default.
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• W2027718963 date "2005-07-22" @default.
• W2027718963 modified "2023-10-16" @default.
• W2027718963 title "A critical role of a carboxylate in proton conduction by the ATP‐binding cassette multidrug transporter LmrA" @default.
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• W2027718963 doi "https://doi.org/10.1096/fj.04-3558fje" @default.
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