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3vou
From Proteopedia
(Difference between revisions)
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| - | + | ==The crystal structure of NaK-NavSulP chimera channel== | |
| - | ===The crystal structure of | + | <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]] | ||
Revision as of 10:48, 4 January 2015
The crystal structure of NaK-NavSulP chimera channel
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