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| - | | + | #REDIRECT [[5iwn]] This PDB entry is obsolete and replaced by 5iwn |
| - | ==Bacterial sodium channel pore domain, high bromide==
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| - | <StructureSection load='5hkt' size='340' side='right' caption='[[5hkt]], [[Resolution|resolution]] 3.75Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[5hkt]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HKT FirstGlance]. <br>
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| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hj8|5hj8]], [[5hk6|5hk6]], [[5hk7|5hk7]], [[5hkd|5hkd]], [[5hku|5hku]]</td></tr>
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| - | <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=5hkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hkt OCA], [http://pdbe.org/5hkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hkt RCSB], [http://www.ebi.ac.uk/pdbsum/5hkt PDBsum]</span></td></tr>
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| - | </table>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | 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>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5hkt" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Findeisen, F]]
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| - | [[Category: Minor, D L]]
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| - | [[Category: Rohaim, A]]
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| - | [[Category: Shaya, D]]
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| - | [[Category: Bacterial sodium channel]]
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| - | [[Category: High br]]
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| - | [[Category: Transport protein]]
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