4cbc
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Open-form NavMS Sodium Channel Pore (with C-terminal Domain) after thallium soak== |
| + | <StructureSection load='4cbc' size='340' side='right' caption='[[4cbc]], [[Resolution|resolution]] 2.66Å' 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == 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]] | ||
Revision as of 09:44, 28 May 2014
Open-form NavMS Sodium Channel Pore (with C-terminal Domain) after thallium soak
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