View source for 7kkr


==Fluoride channel Fluc-Ec2 wild-type with bromide==
<StructureSection load='7kkr' size='340' side='right'caption='[[7kkr]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7kkr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KKR 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]] 3.11&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</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=7kkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kkr OCA], [https://pdbe.org/7kkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kkr RCSB], [https://www.ebi.ac.uk/pdbsum/7kkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kkr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6J5N4_ECOLX Q6J5N4_ECOLX] Important for reducing fluoride concentration in the cell, thus reducing its toxicity.[HAMAP-Rule:MF_00454][SAAS:SAAS00096000]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fluc family fluoride channels protect microbes against ambient environmental fluoride by undermining the cytoplasmic accumulation of this toxic halide. These proteins are structurally idiosyncratic, and thus the permeation pathway and mechanism have no analogy in other known ion channels. Although fluoride-binding sites were identified in previous structural studies, it was not evident how these ions access aqueous solution, and the molecular determinants of anion recognition and selectivity have not been elucidated. Using x-ray crystallography, planar bilayer electrophysiology, and liposome-based assays, we identified additional binding sites along the permeation pathway. We used this information to develop an oriented system for planar lipid bilayer electrophysiology and observed anion block at one of these sites, revealing insights into the mechanism of anion recognition. We propose a permeation mechanism involving alternating occupancy of anion-binding sites that are fully assembled only as the substrate approaches.

The fluoride permeation pathway and anion recognition in Fluc family fluoride channels.,McIlwain BC, Gundepudi R, Koff BB, Stockbridge RB Elife. 2021 Jul 12;10:e69482. doi: 10.7554/eLife.69482. PMID:34250906<ref>PMID:34250906</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7kkr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: McIlwain BC]]
[[Category: Stockbridge RB]]