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6mwb
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NavAb Voltage-gated Sodium Channel, residues 1-239 with mutation T206A== | |
| + | <StructureSection load='6mwb' size='340' side='right'caption='[[6mwb]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6mwb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aliarcobacter_butzleri_RM4018 Aliarcobacter butzleri RM4018]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MWB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MWB 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]] 2.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=PX4:1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PX4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6mwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mwb OCA], [https://pdbe.org/6mwb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mwb RCSB], [https://www.ebi.ac.uk/pdbsum/6mwb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mwb ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A8EVM5_ALIB4 A8EVM5_ALIB4] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Homotetrameric bacterial voltage-gated sodium channels share major biophysical features with their more complex eukaryotic counterparts, including a slow-inactivation mechanism that reduces ion-conductance activity during prolonged depolarization through conformational changes in the pore. The bacterial sodium channel NaVAb activates at very negative membrane potentials and inactivates through a multiphase slow-inactivation mechanism. Early voltage-dependent inactivation during one depolarization is followed by late use-dependent inactivation during repetitive depolarization. Mutations that change the molecular volume of Thr206 in the pore-lining S6 segment can enhance or strongly block early voltage-dependent inactivation, suggesting that this residue serves as a molecular hub controlling the coupling of activation to inactivation. In contrast, truncation of the C-terminal tail enhances the early phase of inactivation yet completely blocks late use-dependent inactivation. Determination of the structure of a C-terminal tail truncation mutant and molecular modeling of conformational changes at Thr206 and the S6 activation gate led to a two-step model of these gating processes. First, bending of the S6 segment, local protein interactions dependent on the size of Thr206, and exchange of hydrogen-bonding partners at the level of Thr206 trigger pore opening followed by the early phase of voltage-dependent inactivation. Thereafter, conformational changes in the C-terminal tail lead to late use-dependent inactivation. These results have important implications for the sequence of conformational changes that lead to multiphase inactivation of NaVAb and other sodium channels. | ||
| - | + | Molecular dissection of multiphase inactivation of the bacterial sodium channel NaVAb.,Gamal El-Din TM, Lenaeus MJ, Ramanadane K, Zheng N, Catterall WA J Gen Physiol. 2018 Dec 3. pii: jgp.201711884. doi: 10.1085/jgp.201711884. PMID:30510035<ref>PMID:30510035</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Catterall | + | <div class="pdbe-citations 6mwb" style="background-color:#fffaf0;"></div> |
| - | [[Category: Lenaeus | + | |
| + | ==See Also== | ||
| + | *[[Ion channels 3D structures|Ion channels 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aliarcobacter butzleri RM4018]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Catterall WA]] | ||
| + | [[Category: Lenaeus MJ]] | ||
Current revision
NavAb Voltage-gated Sodium Channel, residues 1-239 with mutation T206A
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