3NS2

High-resolution structure of pyrabactin-bound PYL2

3NS2 の概要

• エントリーDOI: 10.2210/pdb3ns2/pdb
• 関連するPDBエントリー: 3KDH 3NEF 3NEG 3NR4
• 分子名称: Abscisic acid receptor PYL2, 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide (3 entities in total)
• 機能のキーワード: abscisic acid, aba receptor, pyl2, pyrabactin, 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: 65061.58

構造登録者

Hao, Q.,Yin, P.,Yan, C.,Yuan, X.,Wang, J.,Yan, N. (登録日: 2010-07-01, 公開日: 2010-07-21, 最終更新日: 2023-11-01)

主引用文献

Yuan, X.,Yin, P.,Hao, Q.,Yan, C.,Wang, J.,Yan, N.
Single amino acid alteration between Valine and Isoleucine determines the distinct pyrabactin selectivity by PYL1 and PYL2
J.Biol.Chem., 285:28953-28958, 2010

PubMed Abstract: Abscisic acid (ABA) is one of the most important phytohormones in plant. PYL proteins were identified to be ABA receptors in Arabidopsis thaliana. Despite the remarkably high degree of sequence similarity, PYL1 and PYL2 exhibit distinct responses toward pyrabactin, an ABA agonist. PYL1 inhibits protein phosphatase type 2C upon binding of pyrabactin. In contrast, PYL2 appears relatively insensitive to this compound. The crystal structure of pyrabactin-bound PYL1 revealed that most of the PYL1 residues involved in pyrabactin binding are conserved, hence failing to explain the selectivity of pyrabactin for PYL1 over PYL2. To understand the molecular basis of pyrabactin selectivity, we determined the crystal structure of PYL2 in complex with pyrabactin at 1.64 A resolution. Structural comparison and biochemical analyses demonstrated that one single amino acid alteration between a corresponding valine and isoleucine determines the distinct pyrabactin selectivity by PYL1 and PYL2. These characterizations provide an important clue to dissecting the redundancy of PYL proteins.

PubMed: 20630864
DOI: 10.1074/jbc.M110.160192

実験手法

X-RAY DIFFRACTION (1.634 Å)