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| - | ==Crystal structure of a dual topology fluoride ion channel==
| + | #REDIRECT [[5nkq]] |
| - | <StructureSection load='5a41' size='340' side='right' caption='[[5a41]], [[Resolution|resolution]] 2.17Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[5a41]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A41 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A41 FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a40|5a40]], [[5a43|5a43]]</td></tr>
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| - | <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=5a41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a41 OCA], [http://pdbe.org/5a41 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a41 RCSB], [http://www.ebi.ac.uk/pdbsum/5a41 PDBsum]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[http://www.uniprot.org/uniprot/CRCB_BORPE CRCB_BORPE]] Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | To contend with hazards posed by environmental fluoride, microorganisms export this anion through F(-)-specific ion channels of the Fluc family. Since the recent discovery of Fluc channels, numerous idiosyncratic features of these proteins have been unearthed, including strong selectivity for F(-) over Cl(-) and dual-topology dimeric assembly. To understand the chemical basis for F(-) permeation and how the antiparallel subunits convene to form a F(-)-selective pore, here we solve the crystal structures of two bacterial Fluc homologues in complex with three different monobody inhibitors, with and without F(-) present, to a maximum resolution of 2.1 A. The structures reveal a surprising 'double-barrelled' channel architecture in which two F(-) ion pathways span the membrane, and the dual-topology arrangement includes a centrally coordinated cation, most likely Na(+). F(-) selectivity is proposed to arise from the very narrow pores and an unusual anion coordination that exploits the quadrupolar edges of conserved phenylalanine rings.
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| - | Crystal structures of a double-barrelled fluoride ion channel.,Stockbridge RB, Kolmakova-Partensky L, Shane T, Koide A, Koide S, Miller C, Newstead S Nature. 2015 Sep 24;525(7570):548-51. doi: 10.1038/nature14981. Epub 2015 Sep 7. PMID:26344196<ref>PMID:26344196</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5a41" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Koide, A]]
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| - | [[Category: Koide, S]]
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| - | [[Category: Kolmakova-Partensky, L]]
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| - | [[Category: Miller, C]]
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| - | [[Category: Newstead, S]]
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| - | [[Category: Shane, T]]
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| - | [[Category: Stockbridge, R B]]
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| - | [[Category: Fluc]]
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| - | [[Category: Fluoride channel]]
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| - | [[Category: Monobody]]
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| - | [[Category: Transport protein]] | + | |
