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Article Dans Une Revue Nature Année : 2002

X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity

Résumé

The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. Genetic defects in ClC Cl- channels underlie several familial muscle and kidney diseases. Here we present the X-ray structures of two prokaryotic ClC Cl- channels from Salmonella enterica serovar typhimurium and Escherichia coli at 3.0 and 3.5 A, respectively. Both structures reveal two identical pores, each pore being formed by a separate subunit contained within a homodimeric membrane protein. Individual subunits are composed of two roughly repeated halves that span the membrane with opposite orientations. This antiparallel architecture defines a selectivity filter in which a Cl- ion is stabilized by electrostatic interactions with alpha-helix dipoles and by chemical coordination with nitrogen atoms and hydroxyl groups. These findings provide a structural basis for further understanding the function of ClC Cl- channels, and establish the physical and chemical basis of their anion selectivity.
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hal-02150146 , version 1 (07-06-2019)

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Youxing Jiang, Alice Lee, Jiayun Chen, Martine Cadène, Brian Chait, et al.. X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity. Nature, 2002, 415 (6869), pp.287-294. ⟨10.1038/415287a⟩. ⟨hal-02150146⟩
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