4JDL

Crystal structure of native abscisic acid receptor PYL5 at 2.65 Angstrom

「3QRZ」から置き換えられました

4JDL の概要

• エントリーDOI: 10.2210/pdb4jdl/pdb
• 関連するPDBエントリー: 3KL1 3KLX 3OQU
• 分子名称: Abscisic acid receptor PYL5, GLYCEROL (3 entities in total)
• 機能のキーワード: abscisic acid receptor, pp2c, hormone receptor
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress)
• 細胞内の位置: Cytoplasm: Q9FLB1
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 76008.98

構造登録者

Zhang, X.,Zhang, Q.,Chen, Z. (登録日: 2013-02-25, 公開日: 2013-03-13, 最終更新日: 2023-11-08)

主引用文献

Zhang, X.,Jiang, L.,Wang, G.,Yu, L.,Zhang, Q.,Xin, Q.,Wu, W.,Gong, Z.,Chen, Z.
Structural Insights into the Abscisic Acid Stereospecificity by the ABA Receptors PYR/PYL/RCAR
Plos One, 8:e67477-e67477, 2013

PubMed Abstract: The phytohormone abscisic acid ((+)-ABA) plays a key role in many processes. The biological and biochemical activities of unnatural (-)-ABA have been extensively investigated since 1960s. However, the recognition mechanism by which only a few members among PYR/PYL/RCAR (PYLs) family can bind (-)-ABA remains largely unknown. Here we systematically characterized the affinity of PYLs binding to the (-)-ABA and reported the crystal structures of apo-PYL5, PYL3-(-)-ABA and PYL9-(+)-ABA. PYL5 showed the strongest binding affinity with (-)-ABA among all the PYLs. PYL9 is a stringently exclusive (+)-ABA receptor with interchangeable disulfide bonds shared by a subclass of PYLs. PYL3 is a dual receptor to both ABA enantiomers. The binding orientation and pocket of (-)-ABA in PYLs are obviously different from those of (+)-ABA. Steric hindrance and hydrophobic interaction are the two key factors in determining the stereospecificity of PYLs binding to (-)-ABA, which is further confirmed by gain-of-function and loss-of-function mutagenesis. Our results provide novel insights of the bioactivity of ABA enantiomers onto PYLs, and shed light on designing the selective ABA receptors agonists.

PubMed: 23844015
DOI: 10.1371/journal.pone.0067477

実験手法

X-RAY DIFFRACTION (2.65 Å)