4x8a
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==NavMS pore and C-terminal domain grown from protein purified in LiCl== | |
| + | <StructureSection load='4x8a' size='340' side='right' caption='[[4x8a]], [[Resolution|resolution]] 3.02Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4x8a]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X8A FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x87|4x87]], [[3zjz|3zjz]], [[4cbc|4cbc]], [[4x89|4x89]], [[4x88|4x88]]</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=4x8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x8a OCA], [http://pdbe.org/4x8a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x8a RCSB], [http://www.ebi.ac.uk/pdbsum/4x8a 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> | |
| - | + | <div class="pdbe-citations 4x8a" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bagneris, C]] | [[Category: Bagneris, C]] | ||
| - | [[Category: Naylor, C | + | [[Category: Naylor, C E]] |
| + | [[Category: Wallace, B A]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Selectivity filter]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 03:37, 10 March 2016
NavMS pore and C-terminal domain grown from protein purified in LiCl
| |||||||||||
