3K90
The Abscisic acid receptor PYR1 in complex with Abscisic Acid
Summary for 3K90
| Entry DOI | 10.2210/pdb3k90/pdb |
| Descriptor | Putative uncharacterized protein, (2Z,4E)-5-[(1S)-1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl]-3-methylpenta-2,4-dienoic acid, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | gene regulator, hormone, plant protein, signaling protein, start domain, bet v i domain, hormone-receptor complex, regulator of protein phosphatase type 2c, hormone receptor, hydrolase regulator |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Cellular location | Cytoplasm (By similarity): O49686 |
| Total number of polymer chains | 4 |
| Total formula weight | 87686.33 |
| Authors | Dupeux, F.D.,Santiago, J.,Rodriguez, P.L.,Marquez, J.A. (deposition date: 2009-10-15, release date: 2009-11-10, Last modification date: 2023-11-01) |
| Primary citation | Santiago, J.,Dupeux, F.,Round, A.,Antoni, R.,Park, S.Y.,Jamin, M.,Cutler, S.R.,Rodriguez, P.L.,Marquez, J.A. The abscisic acid receptor PYR1 in complex with abscisic acid. Nature, 462:665-668, 2009 Cited by PubMed Abstract: The plant hormone abscisic acid (ABA) has a central role in coordinating the adaptive response in situations of decreased water availability as well as the regulation of plant growth and development. Recently, a 14-member family of intracellular ABA receptors, named PYR/PYL/RCAR, has been identified. These proteins inhibit in an ABA-dependent manner the activity of a family of key negative regulators of the ABA signalling pathway: the group-A protein phosphatases type 2C (PP2Cs). Here we present the crystal structure of Arabidopsis thaliana PYR1, which consists of a dimer in which one of the subunits is bound to ABA. In the ligand-bound subunit, the loops surrounding the entry to the binding cavity fold over the ABA molecule, enclosing it inside, whereas in the empty subunit they form a channel leaving an open access to the cavity, indicating that conformational changes in these loops have a critical role in the stabilization of the hormone-receptor complex. By providing structural details on the ABA-binding pocket, this work paves the way for the development of new small molecules able to activate the plant stress response. PubMed: 19898494DOI: 10.1038/nature08591 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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