2h2s: Difference between revisions

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-[[Image:2h2s.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2h2s", creates the "Structure Box" on the page.
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-{{STRUCTURE_2h2s|  PDB=2h2s  |  SCENE=  }}
-'''Crystal Structure of E148A mutant of CLC-ec1 in SeCN-'''
+==Crystal Structure of E148A mutant of CLC-ec1 in SeCN-==
+<StructureSection load='2h2s' size='340' side='right'caption='[[2h2s]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2h2s]] 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=2H2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H2S FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEK:SELENOCYANATE+ION'>SEK</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2s OCA], [https://pdbe.org/2h2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h2s RCSB], [https://www.ebi.ac.uk/pdbsum/2h2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h2s ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/2h2s_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2h2s ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+CLC-ec1 is a bacterial archetype of CLC transporters, a ubiquitous class of proteins that catalyze transmembrane exchange of Cl- and H+ necessary for pH regulation of numerous physiological processes. Despite a profusion of high-resolution structures, the molecular mechanism of exchange remains unknown. Here, we rigorously demonstrate strict exchange stoichiometry of 2 Cl-/1 H+. In addition to Cl- and Br-, two non-halide ions, NO3- and SCN-, are shown to be transported by CLC-ec1, but with reduced H+ counter-transport. The loss of proton coupling to these anions is accompanied by an absence of bound anions in the central and external Cl- binding sites in the protein's anion selectivity region, as revealed by crystallographic comparison of Br- and SeCN- bound to this region.
-==Overview==
+Uncoupling of a CLC Cl-/H+ exchange transporter by polyatomic anions.,Nguitragool W, Miller C J Mol Biol. 2006 Sep 29;362(4):682-90. Epub 2006 Aug 14. PMID:16905147<ref>PMID:16905147</ref>
-CLC-ec1 is a bacterial archetype of CLC transporters, a ubiquitous class of proteins that catalyze transmembrane exchange of Cl- and H+ necessary for pH regulation of numerous physiological processes. Despite a profusion of high-resolution structures, the molecular mechanism of exchange remains unknown. Here, we rigorously demonstrate strict exchange stoichiometry of 2 Cl-/1 H+. In addition to Cl- and Br-, two non-halide ions, NO3- and SCN-, are shown to be transported by CLC-ec1, but with reduced H+ counter-transport. The loss of proton coupling to these anions is accompanied by an absence of bound anions in the central and external Cl- binding sites in the protein's anion selectivity region, as revealed by crystallographic comparison of Br- and SeCN- bound to this region.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-H2S 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=2H2S OCA].
+</div>
+<div class="pdbe-citations 2h2s" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Uncoupling of a CLC Cl-/H+ exchange transporter by polyatomic anions., Nguitragool W, Miller C, J Mol Biol. 2006 Sep 29;362(4):682-90. Epub 2006 Aug 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16905147 16905147]
+*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Miller C]]
-[[Category: Miller, C.]]
+[[Category: Nguitragool W]]
-[[Category: Nguitragool, W.]]
-[[Category: Antiport]]
-[[Category: Chloride]]
-[[Category: Clc]]
-[[Category: Transporter]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:48:09 2008''