5hk7: Difference between revisions
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==Bacterial sodium channel pore, 2.95 Angstrom resolution== | ==Bacterial sodium channel pore, 2.95 Angstrom resolution== | ||
<StructureSection load='5hk7' size='340' side='right' caption='[[5hk7]], [[Resolution|resolution]] 2.95Å' scene=''> | <StructureSection load='5hk7' size='340' side='right'caption='[[5hk7]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5hk7]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HK7 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5hk7]] 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=5HK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HK7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=VVA:2-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}ETHYL+HEPTADECANOATE'>VVA</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=VVA:2-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}ETHYL+HEPTADECANOATE'>VVA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hk7 OCA], [https://pdbe.org/5hk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hk7 RCSB], [https://www.ebi.ac.uk/pdbsum/5hk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hk7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q0ABW0_ALKEH Q0ABW0_ALKEH] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 17: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5hk7" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5hk7" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Alkalilimnicola ehrlichii]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Findeisen F]] | ||
[[Category: | [[Category: Minor DL]] | ||
[[Category: | [[Category: Rohaim A]] | ||
[[Category: | [[Category: Shaya D]] | ||
Latest revision as of 10:39, 9 August 2023
Bacterial sodium channel pore, 2.95 Angstrom resolutionBacterial sodium channel pore, 2.95 Angstrom resolution
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. See AlsoReferences
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