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• W2065283927 startingPage "2834" @default.
• W2065283927 abstract "In ion-coupled transport proteins, occupation of selective ion-binding sites is required to trigger conformational changes that lead to substrate translocation. Neurotransmitter transporters, targets of abused and therapeutic drugs, require Na(+) and Cl(-) for function. We recently proposed a chloride-binding site in these proteins not present in Cl(-)-independent prokaryotic homologues. Here we describe conversion of the Cl(-)-independent prokaryotic tryptophan transporter TnaT to a fully functional Cl(-)-dependent form by a single point mutation, D268S. Mutations in TnaT-D268S, in wild type TnaT and in serotonin transporter provide direct evidence for the involvement of each of the proposed residues in Cl(-) coordination. In both SERT and TnaT-D268S, Cl(-) and Na(+) mutually increased each other's potency, consistent with electrostatic interaction through adjacent binding sites. These studies establish the site where Cl(-) binds to trigger conformational change during neurotransmitter transport." @default.
• W2065283927 created "2016-06-24" @default.
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• W2065283927 date "2011-01-01" @default.
• W2065283927 modified "2023-09-29" @default.
• W2065283927 title "Reconstructing a Chloride-binding Site in a Bacterial Neurotransmitter Transporter Homologue" @default.
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• W2065283927 doi "https://doi.org/10.1074/jbc.m110.186064" @default.
• W2065283927 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3024779" @default.
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