1kpl: Difference between revisions

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Crystal Structure of the ClC Chloride Channel from S. typhimurium

OverviewOverview

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 StructureAbout this Structure

1KPL is a Single protein structure of sequence from Salmonella typhimurium with , , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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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OCA

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-[[Image:1kpl.gif|left|200px]]<br /><applet load="1kpl" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1kpl.gif|left|200px]]<br /><applet load="1kpl" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1kpl, resolution 3.00&Aring;" />
 '''Crystal Structure of the ClC Chloride Channel from S. typhimurium'''<br />
 ==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.
+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==
-KPL 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 CL, SO4, MYS and OCT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KPL OCA].
+KPL 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].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Cadene, M.]]
-[[Category: Campbell, E.B.]]
+[[Category: Campbell, E B.]]
-[[Category: Chait, B.T.]]
+[[Category: Chait, B T.]]
 [[Category: Dutzler, R.]]
 [[Category: MacKinnon, R.]]
@@ Line 26: / Line 26: @@
 [[Category: ion channel]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:35:13 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:40 2008''