- EMDB-31532: Cryo-EM structure of the Potassium channel AKT1 mutant from Arabi... -
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基本情報
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データベース: EMDB / ID: EMD-31532
タイトル
Cryo-EM structure of the Potassium channel AKT1 mutant from Arabidopsis thaliana
マップデータ
試料
複合体: Arabidopsis thaliana Potassium channel AKT1
タンパク質・ペプチド: Potassium channel AKT1
リガンド: PHOSPHATIDYLETHANOLAMINE
リガンド: POTASSIUM ION
キーワード
Complex / Potassium channel / Membrane protein / PLANT PROTEIN
機能・相同性
機能・相同性情報
root hair elongation / regulation of stomatal closure / response to water deprivation / inward rectifier potassium channel activity / monoatomic ion channel complex / potassium ion import across plasma membrane / response to salt stress / potassium ion transport / identical protein binding / plasma membrane 類似検索 - 分子機能
ジャーナル: Nat Commun / 年: 2022 タイトル: Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis. 著者: Yaming Lu / Miao Yu / Yutian Jia / Fan Yang / Yanming Zhang / Xia Xu / Xiaomin Li / Fan Yang / Jianlin Lei / Yi Wang / Guanghui Yang / 要旨: 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 ...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.