4cbc: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
'''Unreleased structure'''
==Open-form NavMS Sodium Channel Pore (with C-terminal Domain) after thallium soak==
<StructureSection load='4cbc' size='340' side='right' caption='[[4cbc]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4cbc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBC FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cal|4cal]], [[4cbd|4cbd]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbc RCSB], [http://www.ebi.ac.uk/pdbsum/4cbc PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Voltage-gated sodium channels have essential roles in electrical signalling. Prokaryotic sodium channels are tetramers consisting of transmembrane (TM) voltage-sensing and pore domains, and a cytoplasmic carboxy-terminal domain. Previous crystal structures of bacterial sodium channels revealed the nature of their TM domains but not their C-terminal domains (CTDs). Here, using electron paramagnetic resonance (EPR) spectroscopy combined with molecular dynamics, we show that the CTD of the NavMs channel from Magnetococcus marinus includes a flexible region linking the TM domains to a four-helix coiled-coil bundle. A 2.9 A resolution crystal structure of the NavMs pore indicates the position of the CTD, which is consistent with the EPR-derived structure. Functional analyses demonstrate that the coiled-coil domain couples inactivation with channel opening, and is enabled by negatively charged residues in the linker region. A mechanism for gating is proposed based on the structure, whereby splaying of the bottom of the pore is possible without requiring unravelling of the coiled-coil.


The entry 4cbc is ON HOLD  until Paper Publication
Role of the C-terminal domain in the structure and function of tetrameric sodium channels.,Bagneris C, Decaen PG, Hall BA, Naylor CE, Clapham DE, Kay CW, Wallace BA Nat Commun. 2013 Sep 20;4:2465. doi: 10.1038/ncomms3465. PMID:24051986<ref>PMID:24051986</ref>


Authors: Bagneris, C., Naylor, C.E., Wallace, B.A.
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Open-form NavMS Sodium Channel Pore (with C-terminal Domain) after thallium soak
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bagneris, C.]]
[[Category: Naylor, C E.]]
[[Category: Wallace, B A.]]
[[Category: Membrane protein]]
[[Category: Selectivity filter]]
[[Category: Sodium channel]]
[[Category: Transport protein]]
Retrieved from "https://proteopedia.org/4cbc"