5hk6: Difference between revisions

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-'''Unreleased structure'''
-The entry 5hk6 is ON HOLD
+==Bacterial sodium channel neck 3G mutant, SAD==
+<StructureSection load='5hk6' size='340' side='right' caption='[[5hk6]], [[Resolution|resolution]] 5.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5hk6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HK6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HK6 FirstGlance]. <br>
+</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">[[5hj8|5hj8]], [[5hk7|5hk7]], [[5hkd|5hkd]], [[5hkt|5hkt]], [[5hku|5hku]]</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=5hk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hk6 OCA], [http://pdbe.org/5hk6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hk6 RCSB], [http://www.ebi.ac.uk/pdbsum/5hk6 PDBsum]</span></td></tr>
+</table>
+<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.
-Authors: Rohaim, A., Minor, D.L.
+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>
-Description: Bacterial sodium channel neck 3G mutant, SAD
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5hk6" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Minor, D L]]
 [[Category: Rohaim, A]]
-[[Category: Minor, D.L]]
+[[Category: Bacterial voltage gated sodium channel]]
+[[Category: Transport protein]]