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-Structure paper
タイトル | Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis. |
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ジャーナル・号・ページ | Nat Commun, Vol. 13, Issue 1, Page 5682, Year 2022 |
掲載日 | 2022年9月27日 |
![]() | Yaming Lu / Miao Yu / Yutian Jia / Fan Yang / Yanming Zhang / Xia Xu / Xiaomin Li / Fan Yang / Jianlin Lei / Yi Wang / Guanghui Yang / ![]() |
PubMed 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. |
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手法 | EM (単粒子) |
解像度 | 2.9 - 3.4 Å |
構造データ | EMDB-31532, PDB-7fcv: EMDB-32769, PDB-7wsw: EMDB-33467, PDB-7xuf: |
化合物 | ![]() ChemComp-PTY: ![]() ChemComp-K: |
由来 |
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![]() | PLANT PROTEIN / Complex / Potassium channel / Membrane protein |