8HYA

Cryo-EM structure of Arabidopsis thaliana SOS1 in an occluded state, with expanded TMD

8HYA の概要

• エントリーDOI: 10.2210/pdb8hya/pdb
• EMDBエントリー: 35085
• 分子名称: Sodium/hydrogen exchanger 7, HEXADECANE (2 entities in total)
• 機能のキーワード: sodium/proton antiporter, membrane 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: 256014.43

構造登録者

Wang, Y.,Zhao, Y.,Gao, Y. (登録日: 2023-01-06, 公開日: 2023-08-09, 最終更新日: 2024-05-08)

主引用文献

Wang, Y.,Pan, C.,Chen, Q.,Xie, Q.,Gao, Y.,He, L.,Li, Y.,Dong, Y.,Jiang, X.,Zhao, Y.
Architecture and autoinhibitory mechanism of the plasma membrane Na + /H + antiporter SOS1 in Arabidopsis.
Nat Commun, 14:4487-4487, 2023

PubMed Abstract: Salt-overly-sensitive 1 (SOS1) is a unique electroneutral Na/H antiporter at the plasma membrane of higher plants and plays a central role in resisting salt stress. SOS1 is kept in a resting state with basal activity and activated upon phosphorylation. Here, we report the structures of SOS1. SOS1 forms a homodimer, with each monomer composed of transmembrane and intracellular domains. We find that SOS1 is locked in an occluded state by shifting of the lateral-gate TM5b toward the dimerization domain, thus shielding the Na/H binding site. We speculate that the dimerization of the intracellular domain is crucial to stabilize the transporter in this specific conformation. Moreover, two discrete fragments and a residue W1013 are important to prevent the transition of SOS1 to an alternative conformational state, as validated by functional complementation assays. Our study enriches understanding of the alternate access model of eukaryotic Na/H exchangers.

PubMed: 37495621
DOI: 10.1038/s41467-023-40215-y

実験手法

ELECTRON MICROSCOPY (3.4 Å)