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Structure of the Escherichia coli ClC Chloride channel E148A mutant and Fab Complex

OverviewOverview

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.

About this StructureAbout this Structure

1OTT is a Single protein structure of sequence from Escherichia coli and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Gating the selectivity filter in ClC chloride channels., Dutzler R, Campbell EB, MacKinnon R, Science. 2003 Apr 4;300(5616):108-12. Epub 2003 Mar 20. PMID:12649487 Page seeded by OCA on Sat May 3 04:16:26 2008

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OCA

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 '''Structure of the Escherichia coli ClC Chloride channel E148A mutant and Fab Complex'''
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 [[Category: Dutzler, R.]]
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-[[Category: chloride channel]]
+[[Category: Chloride channel]]
-[[Category: fab complex]]
+[[Category: Fab complex]]
-[[Category: ion channel]]
+[[Category: Ion channel]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:16:26 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:50:15 2008''