3NJ0
X-ray crystal structure of the PYL2-pyrabactin A complex
Summary for 3NJ0
| Entry DOI | 10.2210/pdb3nj0/pdb |
| Related | 3NJ1 3NJO |
| Descriptor | Abscisic acid receptor PYL2, 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide, DI(HYDROXYETHYL)ETHER, ... (5 entities in total) |
| Functional Keywords | start, aba, pyr/pyl/rcar, plant hormone, structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, hormone receptor |
| Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
| Cellular location | Cytoplasm : O80992 |
| Total number of polymer chains | 3 |
| Total formula weight | 66212.75 |
| Authors | Peterson, F.C.,Burgie, E.S.,Bingman, C.A.,Volkman, B.F.,Phillips Jr., G.N.,Cutler, S.R.,Jensen, D.R.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2010-06-16, release date: 2010-08-18, Last modification date: 2024-02-21) |
| Primary citation | Peterson, F.C.,Burgie, E.S.,Park, S.Y.,Jensen, D.R.,Weiner, J.J.,Bingman, C.A.,Chang, C.E.,Cutler, S.R.,Phillips, G.N.,Volkman, B.F. Structural basis for selective activation of ABA receptors. Nat.Struct.Mol.Biol., 17:1109-1113, 2010 Cited by PubMed Abstract: Changing environmental conditions and lessening fresh water supplies have sparked intense interest in understanding and manipulating abscisic acid (ABA) signaling, which controls adaptive responses to drought and other abiotic stressors. We recently discovered a selective ABA agonist, pyrabactin, and used it to discover its primary target PYR1, the founding member of the PYR/PYL family of soluble ABA receptors. To understand pyrabactin's selectivity, we have taken a combined structural, chemical and genetic approach. We show that subtle differences between receptor binding pockets control ligand orientation between productive and nonproductive modes. Nonproductive binding occurs without gate closure and prevents receptor activation. Observations in solution show that these orientations are in rapid equilibrium that can be shifted by mutations to control maximal agonist activity. Our results provide a robust framework for the design of new agonists and reveal a new mechanism for agonist selectivity. PubMed: 20729860DOI: 10.1038/nsmb.1898 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.89 Å) |
Structure validation
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