3det

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[[Image:3det.png|left|200px]]
 
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==Structure of the E148A, Y445A doubly ungated mutant of E.coli CLC_Ec1, Cl-/H+ antiporter==
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The line below this paragraph, containing "STRUCTURE_3det", creates the "Structure Box" on the page.
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<StructureSection load='3det' size='340' side='right'caption='[[3det]], [[Resolution|resolution]] 2.80&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'>[[3det]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] 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=3DET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DET FirstGlance]. <br>
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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]] 2.8&#8491;</td></tr>
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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=3det FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3det OCA], [https://pdbe.org/3det PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3det RCSB], [https://www.ebi.ac.uk/pdbsum/3det PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3det ProSAT]</span></td></tr>
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{{STRUCTURE_3det| PDB=3det | SCENE= }}
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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/de/3det_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=3det 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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The CLC family of Cl(-)-transporting proteins includes both Cl(-) channels and Cl(-)/H(+) exchange transporters. CLC-ec1, a structurally known bacterial homolog of the transporter subclass, exchanges two Cl(-) ions per proton with strict, obligatory stoichiometry. Point mutations at two residues, Glu(148) and Tyr(445), are known to impair H(+) movement while preserving Cl(-) transport. In the x-ray crystal structure of CLC-ec1, these residues form putative "gates" flanking an ion-binding region. In mutants with both of the gate-forming side chains reduced in size, H(+) transport is abolished, and unitary Cl(-) transport rates are greatly increased, well above values expected for transporter mechanisms. Cl(-) transport rates increase as side-chain volume at these positions is decreased. The crystal structure of a doubly ungated mutant shows a narrow conduit traversing the entire protein transmembrane width. These characteristics suggest that Cl(-) flux through uncoupled, ungated CLC-ec1 occurs via a channel-like electrodiffusion mechanism rather than an alternating-exposure conformational cycle that has been rendered proton-independent by the gate mutations.
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===Structure of the E418A, Y445A doubly ungated mutant of E.coli CLC_Ec1, Cl-/H+ antiporter===
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Ion permeation through a Cl--selective channel designed from a CLC Cl-/H+ exchanger.,Jayaram H, Accardi A, Wu F, Williams C, Miller C Proc Natl Acad Sci U S A. 2008 Aug 12;105(32):11194-9. Epub 2008 Aug 4. PMID:18678918<ref>PMID:18678918</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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The line below this paragraph, {{ABSTRACT_PUBMED_18678918}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3det" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18678918 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18678918}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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[[3det]] is a 6 chain structure with 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=3DET OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:018678918</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Accardi, A.]]
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[[Category: Accardi A]]
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[[Category: Jayaram, H.]]
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[[Category: Jayaram H]]
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[[Category: Miller, C.]]
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[[Category: Miller C]]
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[[Category: Williams, C.]]
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[[Category: Williams C]]
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[[Category: Wu, F.]]
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[[Category: Wu F]]
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[[Category: Antiporter]]
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[[Category: Chloride]]
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[[Category: Clc_ec1]]
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[[Category: Doubly ungated mutant]]
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[[Category: Exchange-transporter]]
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[[Category: Inner membrane]]
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[[Category: Ion transport]]
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[[Category: Membrane]]
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[[Category: Membrane protein]]
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[[Category: Stress response]]
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[[Category: Transmembrane]]
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Current revision

Structure of the E148A, Y445A doubly ungated mutant of E.coli CLC_Ec1, Cl-/H+ antiporter

PDB ID 3det

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