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TitleArchitecture and autoinhibitory mechanism of the plasma membrane Na/H antiporter SOS1 in Arabidopsis.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 4487, Year 2023
Publish dateJul 26, 2023
AuthorsYuhang Wang / Chengcai Pan / Qihao Chen / Qing Xie / Yiwei Gao / Lingli He / Yue Li / Yanli Dong / Xingyu Jiang / Yan Zhao /
PubMed AbstractSalt-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 ...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.
External linksNat Commun / PubMed:37495621 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.4 Å
Structure data

33592

7y3e

EMDB-33592, PDB-7y3e:
Cryo-EM structure of Arabidopsis thaliana SOS1 in an occluded state
Method: EM (single particle) / Resolution: 2.8 Å

35085

8hya

EMDB-35085, PDB-8hya:
Cryo-EM structure of Arabidopsis thaliana SOS1 in an occluded state, with expanded TMD
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-R16:
HEXADECANE

Source
  • arabidopsis thaliana (thale cress)
KeywordsMEMBRANE PROTEIN / Sodium/proton antiporter

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