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4mqx
From Proteopedia
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| - | {{STRUCTURE_4mqx| PDB=4mqx | SCENE= }} | ||
| - | ===CLC-ec1 Fab Complex Cysless A399C-A432C mutant=== | ||
| - | == | + | ==CLC-ec1 Fab Complex Cysless A399C-A432C mutant== |
| - | [[http://www.uniprot.org/uniprot/CLCA_ECOLI CLCA_ECOLI | + | <StructureSection load='4mqx' size='340' side='right'caption='[[4mqx]], [[Resolution|resolution]] 3.52Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4mqx]] 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=4MQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MQX FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4mqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mqx OCA], [https://pdbe.org/4mqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mqx RCSB], [https://www.ebi.ac.uk/pdbsum/4mqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mqx 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 == | ||
| + | CLC-type exchangers mediate transmembrane Cl(-) transport. Mutations altering their gating properties cause numerous genetic disorders. However, their transport mechanism remains poorly understood. In conventional models, two gates alternatively expose substrates to the intra- or extracellular solutions. A glutamate was identified as the only gate in the CLCs, suggesting that CLCs function by a nonconventional mechanism. Here we show that transport in CLC-ec1, a prokaryotic homolog, is inhibited by cross-links constraining movement of helix O far from the transport pathway. Cross-linked CLC-ec1 adopts a wild-type-like structure, indicating stabilization of a native conformation. Movements of helix O are transduced to the ion pathway via a direct contact between its C terminus and a tyrosine that is a constitutive element of the second gate of CLC transporters. Therefore, the CLC exchangers have two gates that are coupled through conformational rearrangements outside the ion pathway. | ||
| - | + | Conformational changes required for H(+)/Cl(-) exchange mediated by a CLC transporter.,Basilio D, Noack K, Picollo A, Accardi A Nat Struct Mol Biol. 2014 May;21(5):456-63. doi: 10.1038/nsmb.2814. Epub 2014 Apr, 20. PMID:24747941<ref>PMID:24747941</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <references | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4mqx" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | + | [[Category: Mus musculus]] | |
| + | [[Category: Accardi A]] | ||
| + | [[Category: Basilio D]] | ||
| + | [[Category: Noack K]] | ||
| + | [[Category: Picollo A]] | ||
Current revision
CLC-ec1 Fab Complex Cysless A399C-A432C mutant
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