View source for 5nkq


==Crystal structure of a dual topology fluoride ion channel.==
<StructureSection load='5nkq' size='340' side='right'caption='[[5nkq]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nkq]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5fxb 5fxb] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5a41 5a41]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NKQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.17&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=5nkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nkq OCA], [https://pdbe.org/5nkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nkq RCSB], [https://www.ebi.ac.uk/pdbsum/5nkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nkq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CRCB_BORPE CRCB_BORPE] Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nkq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bordetella pertussis]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Miller C]]
[[Category: Newstead S]]
[[Category: Stockbridge R]]