5kbn

The crystal structure of fluoride channel Fluc Ec2 F80I Mutant

spinqualitylabelsall models 5kbn, resolution 2.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5kbn is a 4 chain structure with sequence from Escherichia coli and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.48Å Ligands: DMU, F, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6J5N4_ECOLX Important for reducing fluoride concentration in the cell, thus reducing its toxicity.[HAMAP-Rule:MF_00454][SAAS:SAAS00096000] Publication Abstract from PubMed 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. Mechanistic signs of double-barreled structure in a fluoride ion channel.,Last NB, Kolmakova-Partensky L, Shane T, Miller C Elife. 2016 Jul 23;5. pii: e18767. doi: 10.7554/eLife.18767. PMID:27449280 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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