5NWJ

14-3-3c in complex with CPP7

5NWJ の概要

• エントリーDOI: 10.2210/pdb5nwj/pdb
• 分子名称: 14-3-3-like protein C, Potassium channel KAT1, TRIETHYLENE GLYCOL, ... (7 entities in total)
• 機能のキーワード: 14-3-3, complex, fusicoccin, channel, signaling protein
• 由来する生物種: Nicotiana tabacum (Common tobacco); 詳細
• 細胞内の位置: Membrane; Multi-pass membrane protein: Q39128
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31059.65

構造登録者

Saponaro, A.,Porro, A.,Chaves-Sanjuan, A.,Nardini, M.,Thiel, G.,Moroni, A. (登録日: 2017-05-06, 公開日: 2017-11-22, 最終更新日: 2024-11-20)

主引用文献

Saponaro, A.,Porro, A.,Chaves-Sanjuan, A.,Nardini, M.,Rauh, O.,Thiel, G.,Moroni, A.
Fusicoccin Activates KAT1 Channels by Stabilizing Their Interaction with 14-3-3 Proteins.
Plant Cell, 29:2570-2580, 2017

PubMed Abstract: Plants acquire potassium (K) ions for cell growth and movement via regulated diffusion through K channels. Here, we present crystallographic and functional data showing that the K inward rectifier KAT1 (K 1) channel is regulated by 14-3-3 proteins and further modulated by the phytotoxin fusicoccin, in analogy to the H-ATPase. We identified a 14-3-3 mode III binding site at the very C terminus of KAT1 and cocrystallized it with tobacco () 14-3-3 proteins to describe the protein complex at atomic detail. Validation of this interaction by electrophysiology shows that 14-3-3 binding augments KAT1 conductance by increasing the maximal current and by positively shifting the voltage dependency of gating. Fusicoccin potentiates the 14-3-3 effect on KAT1 activity by stabilizing their interaction. Crystal structure of the ternary complex reveals a noncanonical binding site for the toxin that adopts a novel conformation. The structural insights underscore the adaptability of fusicoccin, predicting more potential targets than so far anticipated. The data further advocate a common mechanism of regulation of the proton pump and a potassium channel, two essential elements in K uptake in plant cells.

PubMed: 28970335
DOI: 10.1105/tpc.17.00375

実験手法

X-RAY DIFFRACTION (2.07 Å)