8J1E

AtSLAC1 in open state

8J1E の概要

• エントリーDOI: 10.2210/pdb8j1e/pdb
• EMDBエントリー: 35920
• 分子名称: Guard cell S-type anion channel SLAC1,Green fluorescent protein, CHOLESTEROL HEMISUCCINATE, CHLORIDE ION (3 entities in total)
• 機能のキーワード: stomatal closure, anion channel, phosphorylation-dependent activation, membrane protein
• 由来する生物種: Arabidopsis thaliana (thale cress); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 283261.76

構造登録者

Lee, Y.,Lee, S. (登録日: 2023-04-12, 公開日: 2023-11-22, 最終更新日: 2023-11-29)

主引用文献

Lee, Y.,Jeong, H.S.,Jung, S.,Hwang, J.,Le, C.T.H.,Jun, S.H.,Du, E.J.,Kang, K.,Kim, B.G.,Lim, H.H.,Lee, S.
Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model.
Nat Commun, 14:7345-7345, 2023

PubMed Abstract: The anion channel SLAC1 functions as a crucial effector in the ABA signaling, leading to stomata closure. SLAC1 is activated by phosphorylation in its intracellular domains. Both a binding-activation model and an inhibition-release model for activation have been proposed based on only the closed structures of SLAC1, rendering the structure-based activation mechanism controversial. Here we report cryo-EM structures of Arabidopsis SLAC1 WT and its phosphomimetic mutants in open and closed states. Comparison of the open structure with the closed ones reveals the structural basis for opening of the conductance pore. Multiple phosphorylation of an intracellular domain (ICD) causes dissociation of ICD from the transmembrane domain. A conserved, positively-charged sequence motif in the intracellular loop 2 (ICL2) seems to be capable of sensing of the negatively charged phosphorylated ICD. Interactions between ICL2 and ICD drive drastic conformational changes, thereby widening the pore. From our results we propose that SLAC1 operates by a mechanism combining the binding-activation and inhibition-release models.

PubMed: 37963863
DOI: 10.1038/s41467-023-43193-3

実験手法

ELECTRON MICROSCOPY (3.84 Å)