View source for 5kom


==The crystal structure of fluoride channel Fluc Ec2 F83I Mutant==
<StructureSection load='5kom' size='340' side='right'caption='[[5kom]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5kom]] 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=5KOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KOM 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]] 2.69&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <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=5kom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kom OCA], [https://pdbe.org/5kom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kom RCSB], [https://www.ebi.ac.uk/pdbsum/5kom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kom 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 ==
The Fluc family of F(-) ion channels protects prokaryotes and lower eukaryotes from the toxicity of environmental F(-). In bacteria, these channels are built as dual-topology dimers whereby the two subunits assemble in antiparallel transmembrane orientation. Recent crystal structures suggested that Fluc channels contain two separate ion-conduction pathways, each with two F(-) binding sites, but no functional correlates of this unusual architecture have been reported. Experiments here fill this gap by examining the consequences of mutating two conserved F(-)-coordinating phenylalanine residues. Substitution of each phenylalanine specifically extinguishes its associated F(-) binding site in crystal structures and concomitantly inhibits F(-) permeation. Functional analysis of concatemeric channels, which permit mutagenic manipulation of individual pores, show that each pore can be separately inactivated without blocking F(-) conduction through its symmetry-related twin. The results strongly support dual-pathway architecture of Fluc channels.

Mechanistic signs of double-barreled structure in a fluoride ion channel.,Last NB, Kolmakova-Partensky L, Shane T, Miller C Elife. 2016 Jul 23;5. pii: e18767. doi: 10.7554/eLife.18767. PMID:27449280<ref>PMID:27449280</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5kom" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Kolmakova-Partensky L]]
[[Category: Last NB]]
[[Category: Miller C]]
[[Category: Shane T]]