This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5kom

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

The crystal structure of fluoride channel Fluc Ec2 F83I Mutant

Structural highlights

5kom is a 4 chain structure with sequence from Escherichia coli and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.69Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q6J5N4_ECOLX Important for reducing fluoride concentration in the cell, thus reducing its toxicity.[HAMAP-Rule:MF_00454][SAAS:SAAS00096000]

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5kom"

@@ Line 3: / Line 3: @@
 <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 [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KOM FirstGlance]. <br>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
+</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">crcB, AC789_145pl00540, AKG99_27195, AL505_410006, AN206_26275, AUQ25_20445, ECONIH1_26550, ECS286_0026, MJ49_27125, pCTXM15_EC8_00123, pO103_22, SK78_04822 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5kom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kom OCA], [http://pdbe.org/5kom PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kom RCSB], [http://www.ebi.ac.uk/pdbsum/5kom PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kom ProSAT]</span></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 ==
-[[http://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]
+[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 ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Kolmakova-Partensky, L]]
+[[Category: Kolmakova-Partensky L]]
-[[Category: Last, N B]]
+[[Category: Last NB]]
-[[Category: Miller, C]]
+[[Category: Miller C]]
-[[Category: Shane, T]]
+[[Category: Shane T]]
-[[Category: Alpha helix]]
-[[Category: Ion channel]]
-[[Category: Membrane protein]]
-[[Category: Transport protein]]

5kom

From Proteopedia

Current revision

The crystal structure of fluoride channel Fluc Ec2 F83I Mutant

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox