3vou: Difference between revisions
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== | ==The crystal structure of NaK-NavSulP chimera channel== | ||
[[3vou]] is a 2 chain structure with sequence from [ | <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 [https://en.wikipedia.org/wiki/Bacillus_mycoides_KBAB4 Bacillus mycoides KBAB4] and [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3VOU FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</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'>[https://proteopedia.org/fgij/fg.htm?mol=3vou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vou OCA], [https://pdbe.org/3vou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vou RCSB], [https://www.ebi.ac.uk/pdbsum/3vou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vou ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A3SUL8_SULSN A3SUL8_SULSN] [https://www.uniprot.org/uniprot/A9VEV6_BACMK A9VEV6_BACMK] | |||
<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> | |||
<ref | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 3vou" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Bacillus mycoides KBAB4]] | ||
[[Category: Large Structures]] | |||
[[Category: Sulfitobacter sp. NAS-14 1]] | |||
[[Category: Fujiyoshi Y]] | |||
[[Category: Irie K]] | |||
[[Category: Shimomura T]] | |||
