1ots: Difference between revisions
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[[Image:1ots.gif|left|200px]] | [[Image:1ots.gif|left|200px]] | ||
'''Structure of the Escherichia coli ClC Chloride channel and Fab Complex''' | {{Structure | ||
|PDB= 1ots |SIZE=350|CAPTION= <scene name='initialview01'>1ots</scene>, resolution 2.51Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= | |||
|GENE= ERIC OR B0155 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Structure of the Escherichia coli ClC Chloride channel and Fab Complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1OTS is a [ | 1OTS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OTS OCA]. | ||
==Reference== | ==Reference== | ||
Gating the selectivity filter in ClC chloride channels., Dutzler R, Campbell EB, MacKinnon R, Science. 2003 Apr 4;300(5616):108-12. Epub 2003 Mar 20. PMID:[http:// | Gating the selectivity filter in ClC chloride channels., Dutzler R, Campbell EB, MacKinnon R, Science. 2003 Apr 4;300(5616):108-12. Epub 2003 Mar 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12649487 12649487] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: fab complex]] | [[Category: fab complex]] | ||
''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 13:15:30 2008'' | ||
Revision as of 14:15, 20 March 2008
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| , resolution 2.51Å | |||||||
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| Ligands: | |||||||
| Gene: | ERIC OR B0155 (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the Escherichia coli ClC Chloride channel and Fab Complex
OverviewOverview
ClC channels conduct chloride (Cl-) ions across cell membranes and thereby govern the electrical activity of muscle cells and certain neurons, the transport of fluid and electrolytes across epithelia, and the acidification of intracellular vesicles. The structural basis of ClC channel gating was studied. Crystal structures of wild-type and mutant Escherichia coli ClC channels bound to a monoclonal Fab fragment reveal three Cl- binding sites within the 15-angstrom neck of an hourglass-shaped pore. The Cl- binding site nearest the extracellular solution can be occupied either by a Cl- ion or by a glutamate carboxyl group. Mutations of this glutamate residue in Torpedo ray ClC channels alter gating in electrophysiological assays. These findings reveal a form of gating in which the glutamate carboxyl group closes the pore by mimicking a Cl- ion.
About this StructureAbout this Structure
1OTS is a Single protein structure of sequence from Escherichia coli and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Gating the selectivity filter in ClC chloride channels., Dutzler R, Campbell EB, MacKinnon R, Science. 2003 Apr 4;300(5616):108-12. Epub 2003 Mar 20. PMID:12649487
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