5TUA

structure of a Na+-selective mutant of two-pore channel from Arabidopsis thaliana AtTPC1

5TUA の概要

• エントリーDOI: 10.2210/pdb5tua/pdb
• 分子名称: Two pore calcium channel protein 1, CALCIUM ION, BARIUM ION, ... (4 entities in total)
• 機能のキーワード: two-pore channel, na+-selective, metal transport, membrane protein
• 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: 86817.50

構造登録者

Guo, J.,Zeng, W.,Jiang, Y. (登録日: 2016-11-05, 公開日: 2017-01-18, 最終更新日: 2023-10-04)

主引用文献

Guo, J.,Zeng, W.,Jiang, Y.
Tuning the ion selectivity of two-pore channels.
Proc. Natl. Acad. Sci. U.S.A., 114:1009-1014, 2017

PubMed Abstract: Organellar two-pore channels (TPCs) contain two copies of a Shaker-like six-transmembrane (6-TM) domain in each subunit and are ubiquitously expressed in plants and animals. Interestingly, plant and animal TPCs share high sequence similarity in the filter region, yet exhibit drastically different ion selectivity. Plant TPC1 functions as a nonselective cation channel on the vacuole membrane, whereas mammalian TPC channels have been shown to be endo/lysosomal Na-selective or Ca-release channels. In this study, we performed systematic characterization of the ion selectivity of TPC1 from Arabidopsis thaliana (AtTPC1) and compared its selectivity with the selectivity of human TPC2 (HsTPC2). We demonstrate that AtTPC1 is selective for Ca over Na, but nonselective among monovalent cations (Li, Na, and K). Our results also confirm that HsTPC2 is a Na-selective channel activated by phosphatidylinositol 3,5-bisphosphate. Guided by our recent structure of AtTPC1, we converted AtTPC1 to a Na-selective channel by mimicking the selectivity filter of HsTPC2 and identified key residues in the TPC filters that differentiate the selectivity between AtTPC1 and HsTPC2. Furthermore, the structure of the Na-selective AtTPC1 mutant elucidates the structural basis for Na selectivity in mammalian TPCs.

PubMed: 28096396
DOI: 10.1073/pnas.1616191114

実験手法

X-RAY DIFFRACTION (3.3 Å)