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==Crystal structure of voltage-gated sodium channel NavAb E32Q mutant== | ==Crystal structure of voltage-gated sodium channel NavAb E32Q mutant== | ||
<StructureSection load='5yub' size='340' side='right' caption='[[5yub]], [[Resolution|resolution]] 3.40Å' scene=''> | <StructureSection load='5yub' size='340' side='right'caption='[[5yub]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5yub]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YUB OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5yub]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aliarcobacter_butzleri Aliarcobacter butzleri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YUB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1N7:CHAPSO'>1N7</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</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]] 3.40004Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1N7:CHAPSO'>1N7</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</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=5yub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yub OCA], [https://pdbe.org/5yub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yub RCSB], [https://www.ebi.ac.uk/pdbsum/5yub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yub ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A8EVM5_ALIB4 A8EVM5_ALIB4] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Voltage-gated sodium channels are crucial for electro-signalling in living systems. Analysis of the molecular mechanism requires both fine electrophysiological evaluation and high-resolution channel structures. Here, we optimized a dual expression system of NavAb, which is a well-established standard of prokaryotic voltage-gated sodium channels, for E. coli and insect cells using a single plasmid vector to analyse high-resolution protein structures and measure large ionic currents. Using this expression system, we evaluated the voltage dependence and determined the crystal structures of NavAb wild-type and two mutants, E32Q and N49K, whose voltage dependence were positively shifted and essential interactions were lost in voltage sensor domain. The structural and functional comparison elucidated the molecular mechanisms of the voltage dependence of prokaryotic voltage-gated sodium channels. | |||
Optimized expression and purification of NavAb provide the structural insight into the voltage dependence.,Irie K, Haga Y, Shimomura T, Fujiyoshi Y FEBS Lett. 2017 Dec 22. doi: 10.1002/1873-3468.12955. PMID:29274127<ref>PMID:29274127</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5yub" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aliarcobacter butzleri]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Fujiyoshi Y]] | ||
[[Category: | [[Category: Irie K]] | ||
[[Category: | [[Category: Shimomura T]] | ||
Latest revision as of 11:37, 22 November 2023
Structural highlights
FunctionPublication Abstract from PubMedVoltage-gated sodium channels are crucial for electro-signalling in living systems. Analysis of the molecular mechanism requires both fine electrophysiological evaluation and high-resolution channel structures. Here, we optimized a dual expression system of NavAb, which is a well-established standard of prokaryotic voltage-gated sodium channels, for E. coli and insect cells using a single plasmid vector to analyse high-resolution protein structures and measure large ionic currents. Using this expression system, we evaluated the voltage dependence and determined the crystal structures of NavAb wild-type and two mutants, E32Q and N49K, whose voltage dependence were positively shifted and essential interactions were lost in voltage sensor domain. The structural and functional comparison elucidated the molecular mechanisms of the voltage dependence of prokaryotic voltage-gated sodium channels. Optimized expression and purification of NavAb provide the structural insight into the voltage dependence.,Irie K, Haga Y, Shimomura T, Fujiyoshi Y FEBS Lett. 2017 Dec 22. doi: 10.1002/1873-3468.12955. PMID:29274127[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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