3NEF

High-resolution pyrabactin-bound PYL1 structure

3NEF の概要

• エントリーDOI: 10.2210/pdb3nef/pdb
• 関連するPDBエントリー: 3KDH 3KDI 3KDJ 3NEG
• 分子名称: Abscisic acid receptor PYL1, 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide (3 entities in total)
• 機能のキーワード: pyl1, pyrabactin, hormone receptor, hydrolase
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress)
• 細胞内の位置: Cytoplasm (By similarity): Q8VZS8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47033.05

構造登録者

Yan, N. (登録日: 2010-06-08, 公開日: 2010-06-16, 最終更新日: 2023-11-01)

主引用文献

Hao, Q.,Yin, P.,Yan, C.,Yuan, X.,Li, W.,Zhang, Z.,Liu, L.,Wang, J.,Yan, N.
Functional mechanism of the ABA agonist pyrabactin
J.Biol.Chem., 285:28946-28952, 2010

PubMed Abstract: Pyrabactin is a synthetic abscisic acid (ABA) agonist that selectively inhibits seed germination. The use of pyrabactin was pivotal in the identification of the PYR1/PYL/RCAR family (PYL) of proteins as the ABA receptor. Although they both act through PYL proteins, pyrabactin and ABA share no apparent chemical or structural similarity. It remains unclear how pyrabactin functions as an ABA agonist. Here, we report the crystal structure of pyrabactin in complex with PYL1 at 2.4 A resolution. Structural and biochemical analyses revealed that recognition of pyrabactin by the pocket residues precedes the closure of switch loop CL2. Structural comparison between pyrabactin- and ABA-bound PYL1 reveals a general principle in the arrangements of function groups of the two distinct ligands. The study provides a framework for the development of novel ABA agonists that may have applicable potentials in agriculture.

PubMed: 20554531
DOI: 10.1074/jbc.M110.149005

実験手法

X-RAY DIFFRACTION (2.4 Å)