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• W2487933339 abstract "The Fluc family of F− ion channels protects prokaryotes and lower eukaryotes from the toxicity of environmental F−. In bacteria, these channels are built as dual-topology dimers whereby the two subunits assemble in antiparallel transmembrane orientation. Recent crystal structures suggested that Fluc channels contain two separate ion-conduction pathways, each with two F− binding sites, but no functional correlates of this unusual architecture have been reported. Experiments here fill this gap by examining the consequences of mutating two conserved F−-coordinating phenylalanine residues. Substitution of each phenylalanine specifically extinguishes its associated F− binding site in crystal structures and concomitantly inhibits F− permeation. Functional analysis of concatemeric channels, which permit mutagenic manipulation of individual pores, show that each pore can be separately inactivated without blocking F− conduction through its symmetry-related twin. The results strongly support dual-pathway architecture of Fluc channels." @default.
• W2487933339 created "2016-08-23" @default.
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• W2487933339 date "2016-07-23" @default.
• W2487933339 modified "2023-09-24" @default.
• W2487933339 title "Mechanistic signs of double-barreled structure in a fluoride ion channel" @default.
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• W2487933339 doi "https://doi.org/10.7554/elife.18767" @default.
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