1ots: Difference between revisions
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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== | ||
<StructureSection load='1ots' size='340' side='right' caption='[[1ots]], [[Resolution|resolution]] 2.51Å' scene=''> | <StructureSection load='1ots' size='340' side='right' caption='[[1ots]], [[Resolution|resolution]] 2.51Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ott|1ott]], [[1otu|1otu]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ott|1ott]], [[1otu|1otu]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERIC OR B0155 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERIC OR B0155 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1ots PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ots RCSB], [http://www.ebi.ac.uk/pdbsum/1ots PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1ots PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ots RCSB], [http://www.ebi.ac.uk/pdbsum/1ots PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ots ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ot/1ots_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ot/1ots_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1ots" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1ots" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:38, 15 February 2018
Structure of the Escherichia coli ClC Chloride channel and Fab ComplexStructure of the Escherichia coli ClC Chloride channel and Fab Complex
Structural highlights
Function[CLCA_ECOLI] Proton-coupled chloride transporter. Functions as antiport system and exchanges two chloride ions for 1 proton. Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response.[1] [2] [3] [4] [5] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedClC 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. 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[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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