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3OQU

Crystal structure of native abscisic acid receptor PYL9 with ABA

Summary for 3OQU
Entry DOI10.2210/pdb3oqu/pdb
Related3KL1 3KLX
DescriptorAbscisic acid receptor PYL9, (2Z,4E)-5-[(1S)-1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl]-3-methylpenta-2,4-dienoic acid (3 entities in total)
Functional Keywordspyl9, rcar1, abscisic acid receptor, hormone receptor
Biological sourceArabidopsis thaliana (mouse-ear cress)
Cellular locationCytoplasm (By similarity): Q84MC7
Total number of polymer chains2
Total formula weight46544.86
Authors
Zhang, X.,Zhang, Q.,Chen, Z. (deposition date: 2010-09-04, release date: 2011-09-14, Last modification date: 2024-10-16)
Primary citationZhang, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.68 Å)
Structure validation

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