5a43
From Proteopedia
(Difference between revisions)
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a40|5a40]], [[5a41|5a41]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a40|5a40]], [[5a41|5a41]]</td></tr> | ||
| - | <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=5a43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a43 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a43 RCSB], [http://www.ebi.ac.uk/pdbsum/5a43 PDBsum]</span></td></tr> | + | <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=5a43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a43 OCA], [http://pdbe.org/5a43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a43 RCSB], [http://www.ebi.ac.uk/pdbsum/5a43 PDBsum]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/B7LI20_ECO45 B7LI20_ECO45]] Important for reducing fluoride concentration in the cell, thus reducing its toxicity.[HAMAP-Rule:MF_00454][SAAS:SAAS00096000] | [[http://www.uniprot.org/uniprot/B7LI20_ECO45 B7LI20_ECO45]] 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 == | ||
| + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5a43" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:58, 30 September 2015
Crystal structure of a dual topology fluoride ion channel.
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