1ots

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[[Image:1ots.gif|left|200px]]
[[Image:1ots.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1ots |SIZE=350|CAPTION= <scene name='initialview01'>1ots</scene>, resolution 2.51&Aring;
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The line below this paragraph, containing "STRUCTURE_1ots", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= ERIC OR B0155 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1ots| PDB=1ots | SCENE= }}
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|RELATEDENTRY=[[1ott|1OTT]], [[1otu|1OTU]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ots FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ots OCA], [http://www.ebi.ac.uk/pdbsum/1ots PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ots RCSB]</span>
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}}
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'''Structure of the Escherichia coli ClC Chloride channel and Fab Complex'''
'''Structure of the Escherichia coli ClC Chloride channel and Fab Complex'''
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[[Category: Dutzler, R.]]
[[Category: Dutzler, R.]]
[[Category: MacKinnon, R.]]
[[Category: MacKinnon, R.]]
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[[Category: clc chloride channel]]
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[[Category: Clc chloride channel]]
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[[Category: fab complex]]
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[[Category: Fab complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:16:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:50:14 2008''
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Revision as of 01:16, 3 May 2008

Image:1ots.gif


PDB ID 1ots

Drag the structure with the mouse to rotate
1ots, resolution 2.51Å ()
Ligands:
Gene: ERIC OR B0155 (Escherichia coli)
Related: 1ott, 1otu
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure of the Escherichia coli ClC Chloride channel and Fab Complex


Overview

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 Structure

1OTS is a Single protein structure of sequence from Escherichia coli and Mus musculus. Full crystallographic information is available from OCA.

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:12649487 Page seeded by OCA on Sat May 3 04:16:27 2008

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