7fho: Difference between revisions
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==Structure of AtTPC1 D240A/D454A/E528A mutant with 50 mM Ca2+== | ==Structure of AtTPC1 D240A/D454A/E528A mutant with 50 mM Ca2+== | ||
<StructureSection load='7fho' size='340' side='right'caption='[[7fho]]' scene=''> | <StructureSection load='7fho' size='340' side='right'caption='[[7fho]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>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> | <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='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> | </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> | </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®/PubMed®, 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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Guo J]] | [[Category: Guo, J]] | ||
[[Category: Jiang Y]] | [[Category: Jiang, Y]] | ||
[[Category: Li X]] | [[Category: Li, X]] | ||
[[Category: Xu L]] | [[Category: Xu, L]] | ||
[[Category: Ye F]] | [[Category: Ye, F]] | ||
[[Category: Dimer]] | |||
[[Category: Non-selective cation channel]] | |||
[[Category: Transport protein]] | |||
[[Category: Vacuole]] | |||
Latest revision as of 10:15, 16 March 2022
Structure of AtTPC1 D240A/D454A/E528A mutant with 50 mM Ca2+Structure of AtTPC1 D240A/D454A/E528A mutant with 50 mM Ca2+
Structural highlights
Function[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.[1] [2] Publication Abstract from PubMedArabidopsis 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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