View source for 7fho


==Structure of AtTPC1 D240A/D454A/E528A mutant with 50 mM Ca2+==
<StructureSection load='7fho' size='340' side='right'caption='[[7fho]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7fho]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FHO FirstGlance]. <br>
</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=7fho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fho OCA], [https://pdbe.org/7fho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fho RCSB], [https://www.ebi.ac.uk/pdbsum/7fho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fho ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/TPC1_ARATH TPC1_ARATH]] Functions as a voltage-gated inward-rectifying Ca(2+) channel (VDCC) across the vacuole membrane. Is one of the essential components of the slow vacuolar (SV) channel. Acts as the major ROS-responsive Ca(2+) channel and is the possible target of Al-dependent inhibition. Involved in the regulation of germination and stomatal movement.<ref>PMID:15464979</ref> <ref>PMID:15772667</ref>  
<div style="background-color:#fffaf0;">
== 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 7fho" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Guo, J]]
[[Category: Jiang, Y]]
[[Category: Li, X]]
[[Category: Xu, L]]
[[Category: Ye, F]]
[[Category: Dimer]]
[[Category: Non-selective cation channel]]
[[Category: Transport protein]]
[[Category: Vacuole]]