6cpv
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==MicroED structure of NaK ion channel reveals a process of Na+ partition into the selectivity filter== | |
| + | <StructureSection load='6cpv' size='340' side='right' caption='[[6cpv]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6cpv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CPV FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=6cpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpv OCA], [http://pdbe.org/6cpv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cpv RCSB], [http://www.ebi.ac.uk/pdbsum/6cpv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sodium (Na(+)) is a ubiquitous and important inorganic salt mediating many critical biological processes such as neuronal excitation, signaling, and facilitation of various transporters. The hydration states of Na(+) are proposed to play critical roles in determining the conductance and the selectivity of Na(+) channels, yet they are rarely captured by conventional structural biology means. Here we use the emerging cryo-electron microscopy (cryoEM) method micro-electron diffraction (MicroED) to study the structure of a prototypical tetrameric Na(+)-conducting channel, NaK, to 2.5 A resolution from nano-crystals. Two new conformations at the external site of NaK are identified, allowing us to visualize a partially hydrated Na(+) ion at the entrance of the channel pore. A process of dilation coupled with Na(+) movement is identified leading to valuable insights into the mechanism of ion conduction and gating. This study lays the ground work for future studies using MicroED in membrane protein biophysics. | ||
| - | + | MicroED structure of the NaK ion channel reveals a Na(+) partition process into the selectivity filter.,Liu S, Gonen T Commun Biol. 2018;1:38. doi: 10.1038/s42003-018-0040-8. Epub 2018 May 3. PMID:30167468<ref>PMID:30167468</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category:  | + | </div> | 
| + | <div class="pdbe-citations 6cpv" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Gonen, T]] | ||
| + | [[Category: Liu, S]] | ||
| + | [[Category: Ion channel]] | ||
| + | [[Category: Nak]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 07:35, 12 September 2018
MicroED structure of NaK ion channel reveals a process of Na+ partition into the selectivity filter
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Categories: Gonen, T | Liu, S | Ion channel | Nak | Transport protein
