1kpl: Difference between revisions
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'''Crystal Structure of the ClC Chloride Channel from S. typhimurium''' | {{Structure | ||
|PDB= 1kpl |SIZE=350|CAPTION= <scene name='initialview01'>1kpl</scene>, resolution 3.00Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MYS:PENTADECANE'>MYS</scene> and <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal Structure of the ClC Chloride Channel from S. typhimurium''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1KPL is a [ | 1KPL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KPL OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11796999 11796999] | ||
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ion channel]] | [[Category: ion channel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:20:33 2008'' | ||
Revision as of 10:20, 20 March 2008
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| 1kpl, resolution 3.00Å | |||||||||||||
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| Ligands: | CL, SO4, MYS and OCT | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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