Crystallization and initial X-ray data of abscisic acid receptor PYL3 in the presence of (-)-ABA

Abscisic acid (ABA) modulates many complicated developmental processes and responses to environmental stimuli. Recently, several (+)-ABA signalling mechanisms by the RCAR/PYR1/PYL family of proteins (PYLs) have been proposed. However, the mechanism of the recognition and binding of the unnatural ligand (-)-ABA by PYLs has not yet been elucidated. In the present study, the expression, purification and crystallization of PYL3 in complex with (-)-ABA are reported. Diffraction data were refined to 2.65 Å resolution for this complex in space group P6₅. These findings will help to explain the stereospecificity of PYLs for (-)-ABA and to explore the selective ABA agonists.