• Orbit mini

    Simultaneous recording from four lipid bilayers

2016 - Mechanistic signs of double-barreled structure in a fluoride ion channel

Icon Orbit Mini  Orbit mini publication in eLIFE (2016)

Authors:
Last N.B., Kolmakova-Partensky L., Shane T., Miller C.

 

Journal: 
eLife (2016) 5:e18767


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.


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