3NMP

Crystal structure of the abscisic receptor PYL2 mutant A93F in complex with pyrabactin

3NMP の概要

• エントリーDOI: 10.2210/pdb3nmp/pdb
• 関連するPDBエントリー: 3KAZ 3KB0 3MNH 3NMN 3NMT 3NMV
• 分子名称: Abscisic acid receptor PYL2, 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide (3 entities in total)
• 機能のキーワード: pyl2, pyrabactin, plant hormone receptor, helix-grip fold, hormone binding protein
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• 細胞内の位置: Cytoplasm : O80992
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 61421.57

構造登録者

Zhou, X.E.,Melcher, K.,Ng, L.-M.,Soon, F.-F.,Xu, Y.,Suino-Powell, K.M.,Kovach, A.,Li, J.,Yong, E.-L.,Xu, H.E. (登録日: 2010-06-22, 公開日: 2010-08-25, 最終更新日: 2023-09-06)

主引用文献

Melcher, K.,Xu, Y.,Ng, L.M.,Zhou, X.E.,Soon, F.F.,Chinnusamy, V.,Suino-Powell, K.M.,Kovach, A.,Tham, F.S.,Cutler, S.R.,Li, J.,Yong, E.L.,Zhu, J.K.,Xu, H.E.
Identification and mechanism of ABA receptor antagonism.
Nat.Struct.Mol.Biol., 17:1102-1108, 2010

PubMed Abstract: The phytohormone abscisic acid (ABA) functions through a family of fourteen PYR/PYL receptors, which were identified by resistance to pyrabactin, a synthetic inhibitor of seed germination. ABA activates these receptors to inhibit type 2C protein phosphatases, such as ABI1, yet it remains unclear whether these receptors can be antagonized. Here we demonstrate that pyrabactin is an agonist of PYR1 and PYL1 but is unexpectedly an antagonist of PYL2. Crystal structures of the PYL2-pyrabactin and PYL1-pyrabactin-ABI1 complexes reveal the mechanism responsible for receptor-selective activation and inhibition, which enables us to design mutations that convert PYL1 to a pyrabactin-inhibited receptor and PYL2 to a pyrabactin-activated receptor and to identify new pyrabactin-based ABA receptor agonists. Together, our results establish a new concept of ABA receptor antagonism, illustrate its underlying mechanisms and provide a rational framework for discovering novel ABA receptor ligands.

PubMed: 20729862
DOI: 10.1038/nsmb.1887

実験手法

X-RAY DIFFRACTION (2.1 Å)