1KPL: Crystal Structure Of The Clc Chloride Channel From S. Typhimurium

Citation:
Abstract
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.
PDB ID: 1KPLDownload
MMDB ID: 71226
PDB Deposition Date: 2001/12/31
Updated in MMDB: 2010/12
Experimental Method:
x-ray diffraction
Resolution: 3  Å
Source Organism:
Similar Structures:
Biological Unit for 1KPL: dimeric; determined by author
Molecular Components in 1KPL
Label Count Molecule
Proteins (2 molecules)
2
Putative CLC Family, Chlorine Transport Protein(Gene symbol: yadQ)
Molecule annotation
Chemicals (6 molecules)
1
2
2
3
3
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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