4JDA

Complex structure of abscisic acid receptor PYL3 with (-)-ABA

Summary for 4JDA

• Entry DOI: 10.2210/pdb4jda/pdb
• Related: 3KL1 4DSC
• Descriptor: Abscisic acid receptor PYL3, (2Z,4E)-5-[(1R)-1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl]-3-methylpenta-2,4-dienoic acid (3 entities in total)
• Functional Keywords: abscisic acid receptor, pp2c, hormone receptor
• Biological source: Arabidopsis thaliana (mouse-ear cress)
• Cellular location: Cytoplasm (By similarity): Q9SSM7
• Total number of polymer chains: 4
• Total formula weight: 87639.99

Authors

Zhang, X.,Wang, G.,Chen, Z. (deposition date: 2013-02-24, release date: 2013-07-24, Last modification date: 2023-11-08)

Primary citation

Zhang, X.,Jiang, L.,Wang, G.,Yu, L.,Zhang, Q.,Xin, Q.,Wu, W.,Gong, Z.,Chen, Z.
Structural Insights into the Abscisic Acid Stereospecificity by the ABA Receptors PYR/PYL/RCAR
Plos One, 8:e67477-e67477, 2013

PubMed Abstract: The phytohormone abscisic acid ((+)-ABA) plays a key role in many processes. The biological and biochemical activities of unnatural (-)-ABA have been extensively investigated since 1960s. However, the recognition mechanism by which only a few members among PYR/PYL/RCAR (PYLs) family can bind (-)-ABA remains largely unknown. Here we systematically characterized the affinity of PYLs binding to the (-)-ABA and reported the crystal structures of apo-PYL5, PYL3-(-)-ABA and PYL9-(+)-ABA. PYL5 showed the strongest binding affinity with (-)-ABA among all the PYLs. PYL9 is a stringently exclusive (+)-ABA receptor with interchangeable disulfide bonds shared by a subclass of PYLs. PYL3 is a dual receptor to both ABA enantiomers. The binding orientation and pocket of (-)-ABA in PYLs are obviously different from those of (+)-ABA. Steric hindrance and hydrophobic interaction are the two key factors in determining the stereospecificity of PYLs binding to (-)-ABA, which is further confirmed by gain-of-function and loss-of-function mutagenesis. Our results provide novel insights of the bioactivity of ABA enantiomers onto PYLs, and shed light on designing the selective ABA receptors agonists.

PubMed: 23844015
DOI: 10.1371/journal.pone.0067477

Experimental method

X-RAY DIFFRACTION (2.65 Å)