1kpl: Difference between revisions
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|PDB= 1kpl |SIZE=350|CAPTION= <scene name='initialview01'>1kpl</scene>, resolution 3.00Å | |PDB= 1kpl |SIZE=350|CAPTION= <scene name='initialview01'>1kpl</scene>, resolution 3.00Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand= | |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> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1kpk|1KPK]] | |||
|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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[[Category: Dutzler, R.]] | [[Category: Dutzler, R.]] | ||
[[Category: MacKinnon, R.]] | [[Category: MacKinnon, R.]] | ||
[[Category: helical membrane protein]] | [[Category: helical membrane protein]] | ||
[[Category: homodimer]] | [[Category: homodimer]] | ||
[[Category: ion channel]] | [[Category: ion channel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:51:47 2008'' | ||
Revision as of 21:51, 30 March 2008
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| , resolution 3.00Å | |||||||
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| Ligands: | , , , | ||||||
| Related: | 1KPK
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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