8JDA

Cyro-EM structure of the Na+/H+ antipoter SOS1 from Arabidopsis thaliana,class2

8JDA の概要

• エントリーDOI: 10.2210/pdb8jda/pdb
• EMDBエントリー: 36076
• 分子名称: Sodium/hydrogen exchanger 7 (1 entity in total)
• 機能のキーワード: sodium, proton, 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: 258030.95

構造登録者

Yang, G.H.,Zhang, Y.M.,Zhou, J.Q.,Jia, Y.T.,Xu, X.,Fu, P.,Wu, H.Y. (登録日: 2023-05-13, 公開日: 2023-11-08, 最終更新日: 2023-11-29)

主引用文献

Zhang, Y.,Zhou, J.,Ni, X.,Wang, Q.,Jia, Y.,Xu, X.,Wu, H.,Fu, P.,Wen, H.,Guo, Y.,Yang, G.
Structural basis for the activity regulation of Salt Overly Sensitive 1 in Arabidopsis salt tolerance.
Nat.Plants, 9:1915-1923, 2023

PubMed Abstract: The plasma membrane Na/H exchanger Salt Overly Sensitive 1 (SOS1) is crucial for plant salt tolerance. Unlike typical sodium/proton exchangers, SOS1 contains a large cytoplasmic domain (CPD) that regulates Na/H exchange activity. However, the underlying modulation mechanism remains unclear. Here we report the structures of SOS1 from Arabidopsis thaliana in two conformations, primarily differing in CPD flexibility. The CPD comprises an interfacial domain, a cyclic nucleotide-binding domain-like domain (CNBD-like domain) and an autoinhibition domain. Through yeast cell-based Na tolerance test, we reveal the regulatory role of the interfacial domain and the activation role of the CNBD-like domain. The CPD forms a negatively charged cavity that is connected to the ion binding site. The transport of Na may be coupled with the conformational change of CPD. These findings provide structural and functional insight into SOS1 activity regulation.

PubMed: 37884652
DOI: 10.1038/s41477-023-01550-6

実験手法

ELECTRON MICROSCOPY (3.67 Å)