6cpv

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'''Unreleased structure'''
 
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The entry 6cpv is ON HOLD until Paper Publication
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==MicroED structure of NaK ion channel reveals a process of Na+ partition into the selectivity filter==
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<StructureSection load='6cpv' size='340' side='right' caption='[[6cpv]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6cpv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gonen, T]]
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[[Category: Liu, S]]
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[[Category: Ion channel]]
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[[Category: Nak]]
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[[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

6cpv, resolution 2.50Å

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