5hj8: Difference between revisions
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==Bacterial sodium channel neck 3G mutant== | |||
<StructureSection load='5hj8' size='340' side='right'caption='[[5hj8]], [[Resolution|resolution]] 3.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hj8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalilimnicola_ehrlichii Alkalilimnicola ehrlichii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HJ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HJ8 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]] 3.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=5hj8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hj8 OCA], [https://pdbe.org/5hj8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hj8 RCSB], [https://www.ebi.ac.uk/pdbsum/5hj8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hj8 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5hj8" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Alkalilimnicola ehrlichii]] | |||
[[Category: Large Structures]] | |||
[[Category: Minor DL]] | |||
[[Category: Rohaim A]] | |||
Latest revision as of 10:38, 9 August 2023
Bacterial sodium channel neck 3G mutantBacterial sodium channel neck 3G mutant
Structural highlights
FunctionPublication Abstract from PubMedVoltage-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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