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Gating the Selectivity Filter in ClC Chloride Channels

Dutzler, Raimund, Campbell, Ernest B., MacKinnon, Roderick·2003·Science
DOI 10.1126/science.1082708
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Abstract

ClC channels conduct chloride (Cl – ) ions across cell membranes and thereby govern the electrical activity of muscle cells and certain neurons, the transport of fluid and electrolytes across epithelia, and the acidification of intracellular vesicles. The structural basis of ClC channel gating was studied. Crystal structures of wild-type and mutant Escherichia coli ClC channels bound to a monoclonal Fab fragment reveal three Cl – binding sites within the 15-angstrom neck of an hourglass-shaped pore. The Cl – binding site nearest the extracellular solution can be occupied either by a Cl – ion or by a glutamate carboxyl group. Mutations of this glutamate residue in Torpedo ray ClC channels alter gating in electrophysiological assays. These findings reveal a form of gating in which the glutamate carboxyl group closes the pore by mimicking a Cl – ion.

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Crossref · 10.1126/science.1082708

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  • In CLC channels, the equivalent glutamate gates the conduction pathway depending on its protonation state, and in CLC transporters, the glutamate participates in transport of the permeant H+.

    “In the CLC channels, the equivalent glutamate gates the conduction pathway depending on its protonation state(54), and in the CLC transporters, the glutamate participates in transport of the permeant H+(55–57).”

    From Membrane exporters of fluoride ion (2021) · cites this paper as [56]

Citations

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Metadata

Authors
Dutzler, R., Campbell, E. B., & MacKinnon, R.
Affiliations
Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2003-04-04
Volume
300
Issue
5616
Pages
108-112
ISSN
  • 0036-8075
  • 1095-9203
DOI
10.1126/science.1082708
Cited by
727
References
0
Language
en

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