Projection structure of a ClC-type chloride channel at 6.5 Å resolution

Joseph A. Mindell (), Merritt Maduke, Christopher Miller and Nikolaus Grigorieff
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Joseph A. Mindell: Howard Hughes Medical Institute
Merritt Maduke: Howard Hughes Medical Institute
Christopher Miller: Howard Hughes Medical Institute
Nikolaus Grigorieff: Howard Hughes Medical Institute

Nature, 2001, vol. 409, issue 6817, 219-223

Abstract: Abstract Virtually all cells in all eukaryotic organisms express ion channels of the ClC type, the only known molecular family of chloride-ion-selective channels. The diversity of ClC channels highlights the multitude and range of functions served by gated chloride-ion conduction in biological membranes, such as controlling electrical excitability in skeletal muscle, maintaining systemic blood pressure, acidifying endosomal compartments, and regulating electrical responses of GABA (γ-aminobutyric acid)-containing interneurons in the central nervous system1. Previously, we expressed and purified a prokaryotic ClC channel homologue2. Here we report the formation of two-dimensional crystals of this ClC channel protein reconstituted into phospholipid bilayer membranes. Cryo-electron microscopic analysis of these crystals yields a projection structure at 6.5 Å resolution, which shows off-axis water-filled pores within the dimeric channel complex.

Date: 2001
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DOI: 10.1038/35051631

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