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| | ==Structure of the E148A mutant of CLC-ec1 deltaNC construct in 20mM Bromide== | | ==Structure of the E148A mutant of CLC-ec1 deltaNC construct in 20mM Bromide== |
| - | <StructureSection load='4kkc' size='340' side='right' caption='[[4kkc]], [[Resolution|resolution]] 3.18Å' scene=''> | + | <StructureSection load='4kkc' size='340' side='right'caption='[[4kkc]], [[Resolution|resolution]] 3.18Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kkc]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KKC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KKC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kkc]] 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=4KKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KKC FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kk5|4kk5]], [[4kk6|4kk6]], [[4kk8|4kk8]], [[4kk9|4kk9]], [[4kka|4kka]], [[4kkb|4kkb]], [[4kjw|4kjw]], [[4kjp|4kjp]], [[4kjq|4kjq]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.18Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0155, clcA, eriC, JW5012, yadQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4kkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkc OCA], [https://pdbe.org/4kkc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kkc RCSB], [https://www.ebi.ac.uk/pdbsum/4kkc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kkc ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4kkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kkc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kkc RCSB], [http://www.ebi.ac.uk/pdbsum/4kkc PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4kkc" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Lim, H H]] | + | [[Category: Mus musculus]] |
| - | [[Category: Miller, C]] | + | [[Category: Lim H-H]] |
| - | [[Category: Membrane transporter]] | + | [[Category: Miller C]] |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
Cl-/H+ antiporters of the CLC superfamily transport anions across biological membranes in varied physiological contexts. These proteins are weakly selective among anions commonly studied, including Cl-, Br-, I-, NO3- and SCN-, but they seem to be very selective against F-. The recent discovery of a new CLC clade of F-/H+ antiporters, which are highly selective for F- over Cl-, led us to investigate the mechanism of Cl--over-F- selectivity by a CLC Cl-/H+ antiporter, CLC-ec1. By subjecting purified CLC-ec1 to anion transport measurements, electrophysiological recording, equilibrium ligand-binding studies and X-ray crystallography, we show that F- binds in the Cl- transport pathway with affinity similar to Cl- but stalls the transport cycle. Examination of various mutant antiporters implies a 'lock-down' mechanism of F- inhibition, in which F-, by virtue of its unique hydrogen-bonding chemistry, greatly retards a proton-linked conformational change essential for the transport cycle of CLC-ec1.
Fluoride-dependent interruption of the transport cycle of a CLC Cl/H antiporter.,Lim HH, Stockbridge RB, Miller C Nat Chem Biol. 2013 Sep 15. doi: 10.1038/nchembio.1336. PMID:24036509[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Iyer R, Iverson TM, Accardi A, Miller C. A biological role for prokaryotic ClC chloride channels. Nature. 2002 Oct 17;419(6908):715-8. PMID:12384697 doi:10.1038/nature01000
- ↑ Accardi A, Miller C. Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels. Nature. 2004 Feb 26;427(6977):803-7. PMID:14985752 doi:10.1038/nature02314
- ↑ Lobet S, Dutzler R. Ion-binding properties of the ClC chloride selectivity filter. EMBO J. 2006 Jan 11;25(1):24-33. Epub 2005 Dec 8. PMID:16341087
- ↑ Nguitragool W, Miller C. Uncoupling of a CLC Cl-/H+ exchange transporter by polyatomic anions. J Mol Biol. 2006 Sep 29;362(4):682-90. Epub 2006 Aug 14. PMID:16905147 doi:10.1016/j.jmb.2006.07.006
- ↑ Jayaram H, Accardi A, Wu F, Williams C, Miller C. Ion permeation through a Cl--selective channel designed from a CLC Cl-/H+ exchanger. Proc Natl Acad Sci U S A. 2008 Aug 12;105(32):11194-9. Epub 2008 Aug 4. PMID:18678918
- ↑ Lim HH, Stockbridge RB, Miller C. Fluoride-dependent interruption of the transport cycle of a CLC Cl/H antiporter. Nat Chem Biol. 2013 Sep 15. doi: 10.1038/nchembio.1336. PMID:24036509 doi:http://dx.doi.org/10.1038/nchembio.1336
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