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1kpl

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[[Image:1kpl.gif|left|200px]]
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{{Structure
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MYS:PENTADECANE'>MYS</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|RELATEDENTRY=[[1kpk|1KPK]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kpl OCA], [http://www.ebi.ac.uk/pdbsum/1kpl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kpl RCSB]</span>
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'''Crystal Structure of the ClC Chloride Channel from S. typhimurium'''
'''Crystal Structure of the ClC Chloride Channel from S. typhimurium'''
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[[Category: Dutzler, R.]]
[[Category: Dutzler, R.]]
[[Category: MacKinnon, R.]]
[[Category: MacKinnon, R.]]
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[[Category: helical membrane protein]]
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[[Category: Helical membrane protein]]
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[[Category: homodimer]]
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[[Category: Homodimer]]
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[[Category: ion channel]]
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[[Category: Ion channel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:01:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:51:47 2008''
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Revision as of 20:01, 2 May 2008

Template:STRUCTURE 1kpl

Crystal Structure of the ClC Chloride Channel from S. typhimurium


Overview

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.

About this Structure

1KPL is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity., Dutzler R, Campbell EB, Cadene M, Chait BT, MacKinnon R, Nature. 2002 Jan 17;415(6869):287-94. PMID:11796999 Page seeded by OCA on Fri May 2 23:01:06 2008

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