1ots

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{{Seed}}
 
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[[Image:1ots.png|left|200px]]
 
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==Structure of the Escherichia coli ClC Chloride channel and Fab Complex==
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The line below this paragraph, containing "STRUCTURE_1ots", creates the "Structure Box" on the page.
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<StructureSection load='1ots' size='340' side='right'caption='[[1ots]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ots]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OTS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.51&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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{{STRUCTURE_1ots| PDB=1ots | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ots FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ots OCA], [https://pdbe.org/1ots PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ots RCSB], [https://www.ebi.ac.uk/pdbsum/1ots PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ots ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CLCA_ECOLI 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.<ref>PMID:12384697</ref> <ref>PMID:14985752</ref> <ref>PMID:16341087</ref> <ref>PMID:16905147</ref> <ref>PMID:18678918</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ot/1ots_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ots ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Structure of the Escherichia coli ClC Chloride channel and Fab Complex===
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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<ref>PMID:12649487</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ots" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12649487}}, adds the Publication Abstract to the page
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12649487 is the PubMed ID number.
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_12649487}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1OTS is a 6 chains structure of sequences 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].
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==Reference==
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<ref group="xtra">PMID:12649487</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Campbell, E B.]]
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[[Category: Campbell EB]]
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[[Category: Dutzler, R.]]
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[[Category: Dutzler R]]
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[[Category: MacKinnon, R.]]
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[[Category: MacKinnon R]]
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[[Category: Clc chloride channel]]
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[[Category: Fab complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:22:44 2009''
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Current revision

Structure of the Escherichia coli ClC Chloride channel and Fab Complex

PDB ID 1ots

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