3KL1

Crystal structure of abscisic acid receptor PYL2 at 1.55 A

3KL1 の概要

• エントリーDOI: 10.2210/pdb3kl1/pdb
• 関連するPDBエントリー: 3KLX
• 分子名称: Putative uncharacterized protein At2g26040 (2 entities in total)
• 機能のキーワード: abscisic acid receptor, crystal, high resolution, pp2c, hormone receptor
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress)
• 細胞内の位置: Cytoplasm (By similarity): O80992
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42619.88

構造登録者

Zhang, X.,Wang, G.,Chen, Z. (登録日: 2009-11-06, 公開日: 2010-11-10, 最終更新日: 2024-03-20)

主引用文献

Zhang, X.,Zhang, Q.,Xin, Q.,Yu, L.,Wang, Z.,Wu, W.,Jiang, L.,Wang, G.,Tian, W.,Deng, Z.,Wang, Y.,Liu, Z.,Long, J.,Gong, Z.,Chen, Z.
Complex Structures of the Abscisic Acid Receptor PYL3/RCAR13 Reveal a Unique Regulatory Mechanism
Structure, 20:780-790, 2012

PubMed Abstract: Abscisic acid (ABA) controls many physiological processes and mediates adaptive responses to abiotic stresses. The ABA signaling mechanisms for abscisic acid receptors PYR/PYL/RCAR (PYLs) were reported. However, it remains unclear whether the molecular mechanisms are suitable for other PYLs. Here, complex structures of PYL3 with (+)-ABA, pyrabactin and HAB1 are reported. An unexpected trans-homodimer intermediate observed in the crystal is confirmed in solution. ABA-bound PYL3 greatly promotes the generation of monomeric PYL3, which can excessively increase the efficiency of inhibiting PP2Cs. Structure-guided biochemical experiments show that Ser195 accounts for the key intermediate. Interestingly, pyrabactin binds to PYL3 in a distinct nonproductive mode with gate closure, which sheds light on the design of agonists and antagonists for abscisic acid receptors. According to different conformations of ligand-bound PYLs, the PYLs family can be divided into three subclasses, among which the trans-dimeric subclass, represented by PYL3, reveals a distinct regulatory mechanism.

PubMed: 22579247
DOI: 10.1016/j.str.2012.02.019

実験手法

X-RAY DIFFRACTION (1.55 Å)