3W9R
Crystal structure of the high-affinity abscisic acid receptor PYL9/RCAR9 bound to ABA
Summary for 3W9R
| Entry DOI | 10.2210/pdb3w9r/pdb |
| Descriptor | Abscisic 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, HEXAETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | abscisic acid receptor, drought tolerance, protein phosphatase inhibitor, start/bet v1 family, hormone receptor |
| Biological source | Arabidopsis thaliana (mouse-ear cress, thale-cress) |
| Cellular location | Cytoplasm (By similarity): Q84MC7 |
| Total number of polymer chains | 1 |
| Total formula weight | 21629.73 |
| Authors | Nakagawa, M.,Hirano, Y.,Kagiyama, M.,Shibata, N.,Hakoshima, T. (deposition date: 2013-04-13, release date: 2014-04-09, Last modification date: 2023-11-08) |
| Primary citation | Nakagawa, M.,Kagiyama, M.,Shibata, N.,Hirano, Y.,Hakoshima, T. Mechanism of high-affinity abscisic acid binding to PYL9/RCAR1. Genes Cells, 19:386-404, 2014 Cited by PubMed Abstract: Arabidopsis receptors of abscisic acid (ABA), the key plant hormone for adaptation to water stress, comprise 14 PYR/PYLs/RCARs proteins classified into three subfamilies I, II, and III, which suggests functional differentiation. Although their monomer-dimer equilibria may be correlated with differences in their ABA-binding affinities, how the dimerization decreases the affinity is unclear. Comparative structural and binding studies between PYL9, which is a representative of high-affinity subfamily I, and low-affinity members of subfamily III reveals that the nonpolar triplet (Ile110, Val162, and Leu165) and Pro64 contribute to enhance ABA-binding affinity by inducing a shift of the ABA carboxyl group to form additional direct hydrogen bonds with conserved Asn169. Our mutation studies of PYL1 successfully produced a monomeric mutant PYL1 exhibiting low ABA affinity and also a dimeric mutant PYL1 exhibiting high ABA-binding affinity, suggesting that dimer formation of ABA receptors is not essential for their low ABA-binding affinity. Our study contributes toward establishing the structural basis for the higher ABA-binding affinity of the subfamily receptors and provides a clue for understanding the broad spectrum of hormone actions in plants manifested by the different hormone-binding affinity of multiple receptors. PubMed: 24645846DOI: 10.1111/gtc.12140 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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