View source for 7fhk


==Structure of AtTPC1 with 1 mM Ca2+==
<StructureSection load='7fhk' size='340' side='right'caption='[[7fhk]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7fhk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [https://en.wikipedia.org/wiki/Human_orthopneumovirus Human orthopneumovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FHK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#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></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=7fhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fhk OCA], [https://pdbe.org/7fhk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fhk RCSB], [https://www.ebi.ac.uk/pdbsum/7fhk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fhk ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Arabidopsis thaliana two-pore channel AtTPC1 is a voltage-gated, Ca(2+)-modulated, nonselective cation channel that is localized in the vacuolar membrane and responsible for generating slow vacuolar (SV) current. Under depolarizing membrane potential, cytosolic Ca(2+) activates AtTPC1 by binding at the EF-hand domain, whereas luminal Ca(2+) inhibits the channel by stabilizing the voltage-sensing domain II (VSDII) in the resting state. Here, we present 2.8 to 3.3 A cryoelectron microscopy (cryo-EM) structures of AtTPC1 in two conformations, one in closed conformation with unbound EF-hand domain and resting VSDII and the other in a partially open conformation with Ca(2+)-bound EF-hand domain and activated VSDII. Structural comparison between the two different conformations allows us to elucidate the structural mechanisms of voltage gating, cytosolic Ca(2+) activation, and their coupling in AtTPC1. This study also provides structural insight into the general voltage-gating mechanism among voltage-gated ion channels.

Voltage-gating and cytosolic Ca(2+) activation mechanisms of Arabidopsis two-pore channel AtTPC1.,Ye F, Xu L, Li X, Zeng W, Gan N, Zhao C, Yang W, Jiang Y, Guo J Proc Natl Acad Sci U S A. 2021 Dec 7;118(49). pii: 2113946118. doi:, 10.1073/pnas.2113946118. PMID:34845029<ref>PMID:34845029</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7fhk" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ion channels 3D structures|Ion channels 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Human orthopneumovirus]]
[[Category: Large Structures]]
[[Category: Guo J]]
[[Category: Jiang Y]]
[[Category: Li X]]
[[Category: Xu L]]
[[Category: Ye F]]