Open AccessCrystallization and preliminary X‐ray diffraction studies of the abscisic acid receptor PYL3 and its complex with pyrabactin
Author(s) -
Zhang Xingliang,
Wu Wei,
Chen Zhongzhou
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112007506
Subject(s) - abscisic acid , crystallization , x ray , receptor , x ray crystallography , crystallography , materials science , chemistry , diffraction , biochemistry , optics , physics , organic chemistry , gene
Abscisic acid (ABA) modulates many developmental processes and responses to environmental stress. Recently, a family of pyrabactin resistance‐like proteins (PYLs) in Arabidopsis thaliana were identified to be abscisic acid receptors. Although the 14 PYLs members share a similar sequence identity, they exhibit different responses toward pyrabactin. Apo‐PYL3 is a dimer; however, its oligomeric state changes greatly on the addition of pyrabactin. Moreover, pyrabactin binds dimeric PYL3 in a nonproductive mode which prevents receptor activation and inhibition of PP2Cs. Here, the expression, purification and crystallization of apo‐PYL3 and of PYL3 complexed with pyrabactin are reported. Diffraction data were optimized to 2.5 Å resolution for apo‐PYL3 and to 1.83 Å resolution for PYL3–pyrabactin. The crystals of apo‐PYL3 and PYL3–pyrabactin belonged to space groups P 4 1 2 1 2 and P 2 1 2 1 2 1 , respectively.