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TitleStructural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 5682, Year 2022
Publish dateSep 27, 2022
AuthorsYaming Lu / Miao Yu / Yutian Jia / Fan Yang / Yanming Zhang / Xia Xu / Xiaomin Li / Fan Yang / Jianlin Lei / Yi Wang / Guanghui Yang /
PubMed AbstractThe voltage-gated potassium channel AKT1 is responsible for primary K uptake in Arabidopsis roots. AKT1 is functionally activated through phosphorylation and negatively regulated by a potassium ...The voltage-gated potassium channel AKT1 is responsible for primary K uptake in Arabidopsis roots. AKT1 is functionally activated through phosphorylation and negatively regulated by a potassium channel α-subunit AtKC1. However, the molecular basis for the modulation mechanism remains unclear. Here we report the structures of AKT1, phosphorylated-AKT1, a constitutively-active variant, and AKT1-AtKC1 complex. AKT1 is assembled in 2-fold symmetry at the cytoplasmic domain. Such organization appears to sterically hinder the reorientation of C-linkers during ion permeation. Phosphorylated-AKT1 adopts an alternate 4-fold symmetric conformation at cytoplasmic domain, which indicates conformational changes associated with symmetry switch during channel activation. To corroborate this finding, we perform structure-guided mutagenesis to disrupt the dimeric interface and identify a constitutively-active variant Asp379Ala mediates K permeation independently of phosphorylation. This variant predominantly adopts a 4-fold symmetric conformation. Furthermore, the AKT1-AtKC1 complex assembles in 2-fold symmetry. Together, our work reveals structural insight into the regulatory mechanism for AKT1.
External linksNat Commun / PubMed:36167696 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.4 Å
Structure data

EMDB-31532, PDB-7fcv:
Cryo-EM structure of the Potassium channel AKT1 mutant from Arabidopsis thaliana
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-32769, PDB-7wsw:
Cryo-EM structure of the Potassium channel AKT1 from Arabidopsis thaliana
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-33467, PDB-7xuf:
Cryo-EM structure of the AKT1-AtKC1 complex from Arabidopsis thaliana
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM / Phosphatidylethanolamine

ChemComp-K:
Unknown entry

Source
  • arabidopsis thaliana (thale cress)
KeywordsPLANT PROTEIN / Complex / Potassium channel / Membrane protein

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