7TDF

AtTPC1 D454N with 1 mM EDTA state I

7TDF の概要

• エントリーDOI: 10.2210/pdb7tdf/pdb
• EMDBエントリー: 25825 25826 25827
• 分子名称: Two pore calcium channel protein 1 (1 entity in total)
• 機能のキーワード: ion channel, voltage activation, vgic, transport protein
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 169879.69

構造登録者

Dickinson, M.S.,Stroud, R.M. (登録日: 2021-12-31, 公開日: 2022-02-02, 最終更新日: 2024-11-13)

主引用文献

Dickinson, M.S.,Lu, J.,Gupta, M.,Marten, I.,Hedrich, R.,Stroud, R.M.
Molecular basis of multistep voltage activation in plant two-pore channel 1.
Proc.Natl.Acad.Sci.USA, 119:-, 2022

PubMed Abstract: Voltage-gated ion channels confer excitability to biological membranes, initiating and propagating electrical signals across large distances on short timescales. Membrane excitation requires channels that respond to changes in electric field and couple the transmembrane voltage to gating of a central pore. To address the mechanism of this process in a voltage-gated ion channel, we determined structures of the plant two-pore channel 1 at different stages along its activation coordinate. These high-resolution structures of activation intermediates, when compared with the resting-state structure, portray a mechanism in which the voltage-sensing domain undergoes dilation and in-membrane plane rotation about the gating charge-bearing helix, followed by charge translocation across the charge transfer seal. These structures, in concert with patch-clamp electrophysiology, show that residues in the pore mouth sense inhibitory Ca and are allosterically coupled to the voltage sensor. These conformational changes provide insight into the mechanism of voltage-sensor domain activation in which activation occurs vectorially over a series of elementary steps.

PubMed: 35210362
DOI: 10.1073/pnas.2110936119

実験手法

ELECTRON MICROSCOPY (2.7 Å)