2fee: Difference between revisions

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-[[Image:2fee.png|left|200px]]
-{{STRUCTURE_2fee|  PDB=2fee  |  SCENE=  }}
+==Structure of the Cl-/H+ exchanger CLC-ec1 from E.Coli in NaBr==
+<StructureSection load='2fee' size='340' side='right'caption='[[2fee]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2fee]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FEE 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]] 3.2&#8491;</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=2fee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fee OCA], [https://pdbe.org/2fee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fee RCSB], [https://www.ebi.ac.uk/pdbsum/2fee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fee 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/fe/2fee_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=2fee ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+CLC-ec1 is a prokaryotic CLC-type Cl(-)/H+ exchange transporter. Little is known about the mechanism of H+ coupling to Cl-. A critical glutamate residue, E148, was previously shown to be required for Cl(-)/H+ exchange by mediating proton transfer between the protein and the extracellular solution. To test whether an analogous H+ acceptor exists near the intracellular side of the protein, we performed a mutagenesis scan of inward-facing carboxyl-bearing residues and identified E203 as the unique residue whose neutralization abolishes H+ coupling to Cl- transport. Glutamate at this position is strictly conserved in all known CLCs of the transporter subclass, while valine is always found here in CLC channels. The x-ray crystal structure of the E203Q mutant is similar to that of the wild-type protein. Cl- transport rate in E203Q is inhibited at neutral pH, and the double mutant, E148A/E203Q, shows maximal Cl- transport, independent of pH, as does the single mutant E148A. The results argue that substrate exchange by CLC-ec1 involves two separate but partially overlapping permeation pathways, one for Cl- and one for H+. These pathways are congruent from the protein's extracellular surface to E148, and they diverge beyond this point toward the intracellular side. This picture demands a transport mechanism fundamentally different from familiar alternating-access schemes.
-===Structure of the Cl-/H+ exchanger CLC-ec1 from E.Coli in NaBr===
+Separate ion pathways in a Cl-/H+ exchanger.,Accardi A, Walden M, Nguitragool W, Jayaram H, Williams C, Miller C J Gen Physiol. 2005 Dec;126(6):563-70. PMID:16316975<ref>PMID:16316975</ref>
-{{ABSTRACT_PUBMED_16316975}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 2fee" style="background-color:#fffaf0;"></div>
-[[2fee]] is a 6 chain structure of [[Monoclonal Antibody]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FEE OCA].
 ==See Also==
-*[[Monoclonal Antibody|Monoclonal Antibody]]
+*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:016316975</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
 [[Category: Homo sapiens]]
-[[Category: Accardi, A.]]
+[[Category: Large Structures]]
-[[Category: Jayaram, H.]]
+[[Category: Accardi A]]
-[[Category: Miller, C.]]
+[[Category: Jayaram H]]
-[[Category: Nguitragool, W.]]
+[[Category: Miller C]]
-[[Category: Walden, M P.]]
+[[Category: Nguitragool W]]
-[[Category: Williams, C.]]
+[[Category: Walden MP]]
-[[Category: Chloride/proton exchange transporter]]
+[[Category: Williams C]]
-[[Category: Clc-ec1]]
-[[Category: Clca_ecoli]]
-[[Category: Membrane protein]]
-[[Category: Proton transport]]