5E1J

Structure of voltage-gated two-pore channel TPC1 from Arabidopsis thaliana

5E1J の概要

• エントリーDOI: 10.2210/pdb5e1j/pdb
• 分子名称: Two pore calcium channel protein 1, BARIUM ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: two-pore channel, voltage-gated, calcium modulation, metal transport
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 86902.51

構造登録者

Guo, J.,Zeng, W.,Chen, Q.,Lee, C.,Chen, L.,Yang, Y.,Jiang, Y. (登録日: 2015-09-29, 公開日: 2015-12-16, 最終更新日: 2024-03-06)

主引用文献

Guo, J.,Zeng, W.,Chen, Q.,Lee, C.,Chen, L.,Yang, Y.,Cang, C.,Ren, D.,Jiang, Y.
Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana.
Nature, 531:196-201, 2016

PubMed Abstract: Two-pore channels (TPCs) contain two copies of a Shaker-like six-transmembrane (6-TM) domain in each subunit and are ubiquitously expressed in both animals and plants as organellar cation channels. Here we present the crystal structure of a vacuolar two-pore channel from Arabidopsis thaliana, AtTPC1, which functions as a homodimer. AtTPC1 activation requires both voltage and cytosolic Ca(2+). Ca(2+) binding to the cytosolic EF-hand domain triggers conformational changes coupled to the pair of pore-lining inner helices from the first 6-TM domains, whereas membrane potential only activates the second voltage-sensing domain, the conformational changes of which are coupled to the pair of inner helices from the second 6-TM domains. Luminal Ca(2+) or Ba(2+) can modulate voltage activation by stabilizing the second voltage-sensing domain in the resting state and shift voltage activation towards more positive potentials. Our Ba(2+)-bound AtTPC1 structure reveals a voltage sensor in the resting state, providing hitherto unseen structural insight into the general voltage-gating mechanism among voltage-gated channels.

PubMed: 26689363
DOI: 10.1038/nature16446

実験手法

X-RAY DIFFRACTION (3.308 Å)