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1kpl

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[[Image:1kpl.gif|left|200px]]<br /><applet load="1kpl" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kpl.gif|left|200px]]
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caption="1kpl, resolution 3.00&Aring;" />
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'''Crystal Structure of the ClC Chloride Channel from S. typhimurium'''<br />
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{{Structure
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|PDB= 1kpl |SIZE=350|CAPTION= <scene name='initialview01'>1kpl</scene>, resolution 3.00&Aring;
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|SITE=
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|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>
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal Structure of the ClC Chloride Channel from S. typhimurium'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1KPL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=MYS:'>MYS</scene> and <scene name='pdbligand=OCT:'>OCT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KPL OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11796999 11796999]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:40 2008''
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''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


PDB ID 1kpl

Drag the structure with the mouse to rotate
, resolution 3.00Å
Ligands: , , and
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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