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4kjp
From Proteopedia
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| - | {{STRUCTURE_4kjp| PDB=4kjp | SCENE= }} | ||
| - | ===Structure of the CLC-ec1 deltaNC construct in the absence of halide=== | ||
| - | {{ABSTRACT_PUBMED_24036509}} | ||
| - | == | + | ==Structure of the CLC-ec1 deltaNC construct in the absence of halide== |
| - | [[http://www.uniprot.org/uniprot/CLCA_ECOLI CLCA_ECOLI | + | <StructureSection load='4kjp' size='340' side='right'caption='[[4kjp]], [[Resolution|resolution]] 3.20Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4kjp]] 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=4KJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KJP FirstGlance]. <br> | ||
| + | </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=4kjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kjp OCA], [https://pdbe.org/4kjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kjp RCSB], [https://www.ebi.ac.uk/pdbsum/4kjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kjp 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:24036509</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | + | <div class="pdbe-citations 4kjp" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Lim H-H]] | ||
| + | [[Category: Miller C]] | ||
Current revision
Structure of the CLC-ec1 deltaNC construct in the absence of halide
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