View source for 5iwo


==Bacterial sodium channel pore domain, low bromide==
<StructureSection load='5iwo' size='340' side='right'caption='[[5iwo]], [[Resolution|resolution]] 3.33&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5iwo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalilimnicola_ehrlichii Alkalilimnicola ehrlichii]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5hku 5hku]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IWO 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]] 3.33&#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></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=5iwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iwo OCA], [https://pdbe.org/5iwo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iwo RCSB], [https://www.ebi.ac.uk/pdbsum/5iwo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iwo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q0ABW0_ALKEH Q0ABW0_ALKEH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Voltage-gated ion channels (VGICs) are outfitted with diverse cytoplasmic domains that impact function. To examine how such elements may affect VGIC behavior, we addressed how the bacterial voltage-gated sodium channel (BacNaV) C-terminal cytoplasmic domain (CTD) affects function. Our studies show that the BacNaV CTD exerts a profound influence on gating through a temperature-dependent unfolding transition in a discrete cytoplasmic domain, the neck domain, proximal to the pore. Structural and functional studies establish that the BacNaV CTD comprises a bi-partite four-helix bundle that bears an unusual hydrophilic core whose integrity is central to the unfolding mechanism and that couples directly to the channel activation gate. Together, our findings define a general principle for how the widespread four-helix bundle cytoplasmic domain architecture can control VGIC responses, uncover a mechanism underlying the diverse BacNaV voltage dependencies, and demonstrate that a discrete domain can encode the temperature-dependent response of a channel.

Unfolding of a Temperature-Sensitive Domain Controls Voltage-Gated Channel Activation.,Arrigoni C, Rohaim A, Shaya D, Findeisen F, Stein RA, Nurva SR, Mishra S, Mchaourab HS, Minor DL Jr Cell. 2016 Feb 25;164(5):922-36. doi: 10.1016/j.cell.2016.02.001. PMID:26919429<ref>PMID:26919429</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5iwo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Alkalilimnicola ehrlichii]]
[[Category: Large Structures]]
[[Category: Findeisen F]]
[[Category: Minor DL]]
[[Category: Rohaim A]]
[[Category: Shaya D]]