3OQU: Crystal Structure Of Native Abscisic Acid Receptor Pyl9 With Aba

Citation:
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.
PDB ID: 3OQUDownload
MMDB ID: 93551
PDB Deposition Date: 2010/9/4
Updated in MMDB: 2011/09
Experimental Method:
x-ray diffraction
Resolution: 2.68  Å
Source Organism:
Similar Structures:
Biological Unit for 3OQU: dimeric; determined by author and by software (PISA)
Molecular Components in 3OQU
Label Count Molecule
Proteins (2 molecules)
2
Abscisic Acid Receptor Pyl9(Gene symbol: RCAR1)
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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