3vou: Difference between revisions
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==The crystal structure of NaK-NavSulP chimera channel== | |||
===The crystal structure of NaK-NavSulP | <StructureSection load='3vou' size='340' side='right' caption='[[3vou]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vou]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfitobacter_sp._nas-14.1 Sulfitobacter sp. nas-14.1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VOU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VOU FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BcerKBAB4_0590, NAS141_12386 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=314267 Sulfitobacter sp. NAS-14.1])</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=3vou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vou OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vou RCSB], [http://www.ebi.ac.uk/pdbsum/3vou PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Most tetrameric channels have cytosolic domains to regulate their functions, including channel inactivation. Here we show that the cytosolic C-terminal region of NavSulP, a prokaryotic voltage-gated sodium channel cloned from Sulfitobacter pontiacus, accelerates channel inactivation. The crystal structure of the C-terminal region of NavSulP grafted into the C-terminus of a NaK channel revealed that the NavSulP C-terminal region forms a four-helix bundle. Point mutations of the residues involved in the intersubunit interactions of the four-helix bundle destabilized the tetramer of the channel and reduced the inactivation rate. The four-helix bundle was directly connected to the inner helix of the pore domain, and a mutation increasing the rigidity of the inner helix also reduced the inactivation rate. These findings suggest that the NavSulP four-helix bundle has important roles not only in stabilizing the tetramer, but also in accelerating the inactivation rate, through promotion of the conformational change of the inner helix. | |||
The C-terminal helical bundle of the tetrameric prokaryotic sodium channel accelerates the inactivation rate.,Irie K, Shimomura T, Fujiyoshi Y Nat Commun. 2012 Apr 24;3:793. doi: 10.1038/ncomms1797. PMID:22531178<ref>PMID:22531178</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Sulfitobacter sp. nas-14 1]] | [[Category: Sulfitobacter sp. nas-14 1]] | ||
[[Category: Fujiyoshi, Y | [[Category: Fujiyoshi, Y]] | ||
[[Category: Irie, K | [[Category: Irie, K]] | ||
[[Category: Shimomura, T | [[Category: Shimomura, T]] | ||
[[Category: 4-helical bundle]] | [[Category: 4-helical bundle]] | ||
[[Category: Ion channel]] | [[Category: Ion channel]] | ||
[[Category: Membrane]] | [[Category: Membrane]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
