6mwb: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 6mwb is ~~ON HOLD until Paper~~ Publication

==NavAb Voltage-gated Sodium Channel, residues 1-239 with mutation T206A==

== Structural highlights ==

<table><tr><td colspan='2'>[[6mwb]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MWB FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6mwa|6mwa]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mwb OCA], [http://pdbe.org/6mwb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mwb RCSB], [http://www.ebi.ac.uk/pdbsum/6mwb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mwb ProSAT]</span></td></tr>

</table>

== 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 T206A~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

~~[[Category: Unreleased Structures]]~~

</div>

[[Category: Catterall, W.A]]

[[Category: Lenaeus, M.J]]

== References ==

__TOC__

</StructureSection>

[[Category: Catterall, W A]]

[[Category: Lenaeus, M J]]

[[Category: Ion channel voltage-gated sodium channel]]

[[Category: Membrane protein]]

[[Category: Metal transport]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6mwb is ON HOLD  until Paper Publication
+==NavAb Voltage-gated Sodium Channel, residues 1-239 with mutation T206A==
+<StructureSection load='6mwb' size='340' side='right' caption='[[6mwb]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6mwb]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MWB FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6mwa|6mwa]]</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mwb OCA], [http://pdbe.org/6mwb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mwb RCSB], [http://www.ebi.ac.uk/pdbsum/6mwb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mwb ProSAT]</span></td></tr>
+</table>
+<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 T206A
+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 6mwb" style="background-color:#fffaf0;"></div>
-[[Category: Lenaeus, M.J]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Catterall, W A]]
+[[Category: Lenaeus, M J]]
+[[Category: Ion channel voltage-gated sodium channel]]
+[[Category: Membrane protein]]
+[[Category: Metal transport]]