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| | <StructureSection load='5hk6' size='340' side='right'caption='[[5hk6]], [[Resolution|resolution]] 5.50Å' scene=''> | | <StructureSection load='5hk6' size='340' side='right'caption='[[5hk6]], [[Resolution|resolution]] 5.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hk6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_baa-1101 Atcc baa-1101]. 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://proteopedia.org/fgij/fg.htm?mol=5HK6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hk6]] 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=5HK6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 5.5Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mlg_0322 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=351052 ATCC BAA-1101])</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=5hk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hk6 OCA], [https://pdbe.org/5hk6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hk6 RCSB], [https://www.ebi.ac.uk/pdbsum/5hk6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hk6 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hk6 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 == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc baa-1101]] | + | [[Category: Alkalilimnicola ehrlichii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Minor, D L]] | + | [[Category: Minor DL]] |
| - | [[Category: Rohaim, A]] | + | [[Category: Rohaim A]] |
| - | [[Category: Bacterial voltage gated sodium channel]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
Q0ABW0_ALKEH
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Arrigoni C, Rohaim A, Shaya D, Findeisen F, Stein RA, Nurva SR, Mishra S, Mchaourab HS, Minor DL Jr. Unfolding of a Temperature-Sensitive Domain Controls Voltage-Gated Channel Activation. Cell. 2016 Feb 25;164(5):922-36. doi: 10.1016/j.cell.2016.02.001. PMID:26919429 doi:http://dx.doi.org/10.1016/j.cell.2016.02.001
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