View source for 5wuf


==Structural basis for conductance through TRIC cation channels==
<StructureSection load='5wuf' size='340' side='right'caption='[[5wuf]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5wuf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Colwellia_psychrerythraea_34H Colwellia psychrerythraea 34H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WUF 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]] 2.401&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5wuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wuf OCA], [https://pdbe.org/5wuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wuf RCSB], [https://www.ebi.ac.uk/pdbsum/5wuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wuf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q47UY7_COLP3 Q47UY7_COLP3] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mammalian TRICs function as K+-permeable cation channels that provide counter ions for Ca2+ handling in intracellular stores. Here we describe the structures of two prokaryotic homologues, archaeal SaTRIC and bacterial CpTRIC, showing that TRIC channels are symmetrical trimers with transmembrane pores through each protomer. Each pore holds a string of water molecules centred at kinked helices in two inverted-repeat triple-helix bundles (THBs). The pores are locked in a closed state by a hydrogen bond network at the C terminus of the THBs, which is lost when the pores assume an open conformation. The transition between the open and close states seems to be mediated by cation binding to conserved residues along the three-fold axis. Electrophysiology and mutagenesis studies show that prokaryotic TRICs have similar functional properties to those of mammalian TRICs and implicate the three-fold axis in the allosteric regulation of the channel.

Structural basis for conductance through TRIC cation channels.,Su M, Gao F, Yuan Q, Mao Y, Li DL, Guo Y, Yang C, Wang XH, Bruni R, Kloss B, Zhao H, Zeng Y, Zhang FB, Marks AR, Hendrickson WA, Chen YH Nat Commun. 2017 May 19;8:15103. doi: 10.1038/ncomms15103. PMID:28524849<ref>PMID:28524849</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5wuf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Colwellia psychrerythraea 34H]]
[[Category: Large Structures]]
[[Category: Bruni R]]
[[Category: Chen YH]]
[[Category: Gao F]]
[[Category: Hendrickson WA]]
[[Category: Kloss B]]
[[Category: Mao Y]]
[[Category: Su M]]
[[Category: Wang XH]]
[[Category: Zeng Y]]