View source for 5cbg


==Calcium activated non-selective cation channel==
<StructureSection load='5cbg' size='340' side='right'caption='[[5cbg]], [[Resolution|resolution]] 3.14&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cbg]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Tsukamurella_paurometabola_DSM_20162 Tsukamurella paurometabola DSM 20162]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CBG 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]] 3.14&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</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=5cbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cbg OCA], [https://pdbe.org/5cbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cbg RCSB], [https://www.ebi.ac.uk/pdbsum/5cbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cbg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D5UM26_TSUPD D5UM26_TSUPD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The selectivity filter is an essential functional element of K(+) channels that is highly conserved both in terms of its primary sequence and its three-dimensional structure. Here, we investigate the properties of an ion channel from the Gram-positive bacterium Tsukamurella paurometabola with a selectivity filter formed by an uncommon proline-rich sequence. Electrophysiological recordings show that it is a non-selective cation channel and that its activity depends on Ca(2+) concentration. In the crystal structure, the selectivity filter adopts a novel conformation with Ca(2+) ions bound within the filter near the pore helix where they are coordinated by backbone oxygen atoms, a recurrent motif found in multiple proteins. The binding of Ca(2+) ion in the selectivity filter controls the widening of the pore as shown in crystal structures and in molecular dynamics simulations. The structural, functional and computational data provide a characterization of this calcium-gated cationic channel.

Structural and functional characterization of a calcium-activated cation channel from Tsukamurella paurometabola.,Dhakshnamoorthy B, Rohaim A, Rui H, Blachowicz L, Roux B Nat Commun. 2016 Sep 28;7:12753. doi: 10.1038/ncomms12753. PMID:27678077<ref>PMID:27678077</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5cbg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Tsukamurella paurometabola DSM 20162]]
[[Category: Blachowicz L]]
[[Category: Dhakshnamoorthy B]]
[[Category: Rohaim A]]
[[Category: Roux B]]
[[Category: Rui H]]