8JDA

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

Summary for 8JDA

• Entry DOI: 10.2210/pdb8jda/pdb
• EMDB information: 36076
• Descriptor: Sodium/hydrogen exchanger 7 (1 entity in total)
• Functional Keywords: sodium, proton, membrane protein
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 2
• Total formula weight: 258030.95

Authors

Yang, G.H.,Zhang, Y.M.,Zhou, J.Q.,Jia, Y.T.,Xu, X.,Fu, P.,Wu, H.Y. (deposition date: 2023-05-13, release date: 2023-11-08, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.67 Å)