3RT0

Crystal structure of PYL10-HAB1 complex in the absence of abscisic acid (ABA)

3RT0 の概要

• エントリーDOI: 10.2210/pdb3rt0/pdb
• 関連するPDBエントリー: 3RT2
• 分子名称: Protein phosphatase 2C 16, Abscisic acid receptor PYL10, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: pyl10-hab1 binary complex, apo-pyl10 inhibits hab1 dephosphorylation activity, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Arabidopsis thaliana (thale-cress); 詳細
• 細胞内の位置: Cytoplasm: Q9CAJ0; Cytoplasm (By similarity): Q8H1R0
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 116872.14

構造登録者

Hao, Q.,Yin, P.,Li, W.,Wang, L.,Yan, C.,Wang, J.,Yan, N. (登録日: 2011-05-02, 公開日: 2011-06-22, 最終更新日: 2023-11-01)

主引用文献

Hao, Q.,Yin, P.,Li, W.,Wang, L.,Yan, C.,Lin, Z.,Wu, J.Z.,Wang, J.,Yan, S.F.,Yan, N.
The Molecular Basis of ABA-Independent Inhibition of PP2Cs by a Subclass of PYL Proteins
Mol.Cell, 42:662-672, 2011

PubMed Abstract: PYR1/PYL/RCAR proteins (PYLs) are confirmed abscisic acid (ABA) receptors, which inhibit protein phosphatase 2C (PP2C) upon binding to ABA. Arabidopsis thaliana has 14 PYLs, yet their functional distinction remains unclear. Here, we report systematic biochemical characterization of PYLs. A subclass of PYLs, represented by PYL10, inhibited PP2C in the absence of any ligand. Crystal structures of PYL10, both in the free form and in the HAB1 (PP2C)-bound state, revealed the structural basis for its constitutive activity. Structural-guided biochemical analyses revealed that ABA-independent inhibition of PP2C requires the PYLs to exist in a monomeric state. In addition, the residues guarding the entrance to the ligand-binding pocket of these PYLs should be bulky and hydrophobic. Based on these principles, we were able to generate monomeric PYL2 variants that gained constitutive inhibitory effect on PP2Cs. These findings provide an important framework for understanding the complex regulation of ABA signaling by PYL proteins.

PubMed: 21658606
DOI: 10.1016/j.molcel.2011.05.011

実験手法

X-RAY DIFFRACTION (2.113 Å)