7FHK

Structure of AtTPC1 with 1 mM Ca2+

7FHK の概要

• エントリーDOI: 10.2210/pdb7fhk/pdb
• EMDBエントリー: 31585
• 分子名称: Two pore calcium channel protein 1,GFP, AtTPC1-Cter, CALCIUM ION (3 entities in total)
• 機能のキーワード: non-selective cation channel, dimer, vacuole, transport protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 231527.45

構造登録者

Ye, F.,Xu, L.,Li, X.,Jiang, Y.,Guo, J. (登録日: 2021-07-29, 公開日: 2021-12-01, 最終更新日: 2024-06-12)

主引用文献

Ye, F.,Xu, L.,Li, X.,Zeng, W.,Gan, N.,Zhao, C.,Yang, W.,Jiang, Y.,Guo, J.
Voltage-gating and cytosolic Ca 2+ activation mechanisms of Arabidopsis two-pore channel AtTPC1.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: two-pore channel AtTPC1 is a voltage-gated, Ca-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 activates AtTPC1 by binding at the EF-hand domain, whereas luminal Ca inhibits the channel by stabilizing the voltage-sensing domain II (VSDII) in the resting state. Here, we present 2.8 to 3.3 Å 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-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 activation, and their coupling in AtTPC1. This study also provides structural insight into the general voltage-gating mechanism among voltage-gated ion channels.

PubMed: 34845029
DOI: 10.1073/pnas.2113946118

実験手法

ELECTRON MICROSCOPY (3.3 Å)