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2fec
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:2fec.png|left|200px]] | ||
| - | < | + | ==Structure of the E203Q mutant of the Cl-/H+ exchanger CLC-ec1 from E.Coli== |
| - | + | <StructureSection load='2fec' size='340' side='right'caption='[[2fec]], [[Resolution|resolution]] 3.97Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[2fec]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FEC FirstGlance]. <br> | |
| - | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ots|1ots]], [[2fed|2fed]], [[2fee|2fee]]</div></td></tr> | |
| - | -- | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clcA, eriC ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2fec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fec OCA], [https://pdbe.org/2fec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fec RCSB], [https://www.ebi.ac.uk/pdbsum/2fec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fec 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/2fec_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2fec 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. | ||
| - | + | 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> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2fec" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Bacillus coli migula 1895]] |
| - | + | [[Category: Human]] | |
| - | + | [[Category: Large Structures]] | |
| - | == | + | [[Category: Accardi, A]] |
| - | + | [[Category: Jayaram, H]] | |
| - | [[Category: | + | [[Category: Miller, C]] |
| - | [[Category: | + | [[Category: Nguitragool, W]] |
| - | [[Category: | + | [[Category: Walden, M P]] |
| - | [[Category: Accardi, A | + | [[Category: Williams, C]] |
| - | [[Category: Jayaram, H | + | |
| - | [[Category: Miller, C | + | |
| - | [[Category: Nguitragool, W | + | |
| - | [[Category: Walden, M P | + | |
| - | [[Category: Williams, C | + | |
[[Category: Chloride/proton exchange transporter]] | [[Category: Chloride/proton exchange transporter]] | ||
[[Category: Clc-ec1]] | [[Category: Clc-ec1]] | ||
[[Category: Clca_ecoli]] | [[Category: Clca_ecoli]] | ||
| - | + | [[Category: Membrane protein]] | |
| - | + | [[Category: Proton transport]] | |
Current revision
Structure of the E203Q mutant of the Cl-/H+ exchanger CLC-ec1 from E.Coli
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