6mwg: Difference between revisions

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-'''Unreleased structure'''
-The entry 6mwg is ON HOLD
+==NavAb Voltage-gated Sodium Channel, residues 1-239, with mutation T206V==
+<StructureSection load='6mwg' size='340' side='right'caption='[[6mwg]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6mwg]] 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=6MWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MWG 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]] 2.501&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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></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=6mwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mwg OCA], [https://pdbe.org/6mwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mwg RCSB], [https://www.ebi.ac.uk/pdbsum/6mwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mwg 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.
-Authors: Lenaeus, M.J., Catterall, W.A.
+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>
-Description: NavAb Voltage-gated Sodium Channel, residues 1-239, with mutation T206V
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Catterall, W.A]]
+<div class="pdbe-citations 6mwg" style="background-color:#fffaf0;"></div>
-[[Category: Lenaeus, M.J]]
+==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]]