3KDH

Structure of ligand-free PYL2

3KDH の概要

• エントリーDOI: 10.2210/pdb3kdh/pdb
• 関連するPDBエントリー: 3kdi 3kdj
• 分子名称: Putative uncharacterized protein At2g26040 (2 entities in total)
• 機能のキーワード: pyl2, 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: 3
• 化学式量合計: 63929.81

構造登録者

Yin, P.,Fan, H.,Hao, Q.,Yuan, X.,Yan, N. (登録日: 2009-10-22, 公開日: 2009-11-10, 最終更新日: 2024-03-20)

主引用文献

Yin, P.,Fan, H.,Hao, Q.,Yuan, X.,Wu, D.,Pang, Y.,Yan, C.,Li, W.,Wang, J.,Yan, N.
Structural insights into the mechanism of abscisic acid signaling by PYL proteins
Nat.Struct.Mol.Biol., 16:1230-1236, 2009

PubMed Abstract: Abscisic acid (ABA) is an important phytohormone that regulates plant stress responses. Proteins from the PYR-PYL-RCAR family were recently identified as ABA receptors. Upon binding to ABA, a PYL protein associates with type 2C protein phosphatases (PP2Cs) such as ABI1 and ABI2, inhibiting their activity; the molecular mechanisms by which PYLs mediate ABA signaling remain unknown, however. Here we report three crystal structures: apo-PYL2, (+)-ABA-bound PYL2 and (+)-ABA-bound PYL1 in complex with phosphatase ABI1. Apo-PYL2 contains a pocket surrounded by four highly conserved surface loops. In response to ABA binding, loop CL2 closes onto the pocket, creating a surface that recognizes ABI1. In the ternary complex, the CL2 loop is located near the active site of ABI1, blocking the entry of substrate proteins. Together, our data reveal the mechanisms by which ABA regulates PYL-mediated inhibition of PP2Cs.

PubMed: 19893533
DOI: 10.1038/nsmb.1730

実験手法

X-RAY DIFFRACTION (1.653 Å)