3K3K

Crystal structure of dimeric abscisic acid (ABA) receptor pyrabactin resistance 1 (PYR1) with ABA-bound closed-lid and ABA-free open-lid subunits

3K3K の概要

• エントリーDOI: 10.2210/pdb3k3k/pdb
• 分子名称: Abscisic acid receptor PYR1, (2Z,4E)-5-[(1S)-1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl]-3-methylpenta-2,4-dienoic acid (3 entities in total)
• 機能のキーワード: pyr1, abscisic acid, aba receptor, plant hormone receptor, aba, aba sensor, drought tolerance, plant development, seed dormancy, alpha/beta helix-grip fold, start protein, cluster a type 2c protein phosphatase (pp2c) inhibitor, pyrabactin resistance 1, pyrabactin, pyl, phytohormone, hormone receptor, signaling protein
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress)
• 細胞内の位置: Cytoplasm (By similarity): O49686
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47813.54

構造登録者

Arvai, A.S.,Hitomi, K.,Getzoff, E.D. (登録日: 2009-10-02, 公開日: 2009-11-17, 最終更新日: 2023-09-06)

主引用文献

Nishimura, N.,Hitomi, K.,Arvai, A.S.,Rambo, R.P.,Hitomi, C.,Cutler, S.R.,Schroeder, J.I.,Getzoff, E.D.
Structural mechanism of abscisic acid binding and signaling by dimeric PYR1.
Science, 326:1373-1379, 2009

PubMed Abstract: The phytohormone abscisic acid (ABA) acts in seed dormancy, plant development, drought tolerance, and adaptive responses to environmental stresses. Structural mechanisms mediating ABA receptor recognition and signaling remain unknown but are essential for understanding and manipulating abiotic stress resistance. Here, we report structures of pyrabactin resistance 1 (PYR1), a prototypical PYR/PYR1-like (PYL)/regulatory component of ABA receptor (RCAR) protein that functions in early ABA signaling. The crystallographic structure reveals an alpha/beta helix-grip fold and homodimeric assembly, verified in vivo by coimmunoprecipitation. ABA binding within a large internal cavity switches structural motifs distinguishing ABA-free "open-lid" from ABA-bound "closed-lid" conformations. Small-angle x-ray scattering suggests that ABA signals by converting PYR1 to a more compact, symmetric closed-lid dimer. Site-directed PYR1 mutants designed to disrupt hormone binding lose ABA-triggered interactions with type 2C protein phosphatase partners in planta.

PubMed: 19933100
DOI: 10.1126/science.1181829

実験手法

X-RAY DIFFRACTION (1.7 Å)