3K3K
Crystal structure of dimeric abscisic acid (ABA) receptor pyrabactin resistance 1 (PYR1) with ABA-bound closed-lid and ABA-free open-lid subunits
Summary for 3K3K
| Entry DOI | 10.2210/pdb3k3k/pdb |
| Descriptor | Abscisic acid receptor PYR1, (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 Keywords | pyr1, abscisic acid, aba receptor, plant hormone receptor, aba, aba sensor, drought tolerance, plant development, seed dormancy, alpha/beta helix-grip fold, start protein, cluster a type 2c protein phosphatase (pp2c) inhibitor, pyrabactin resistance 1, pyrabactin, pyl, phytohormone, hormone receptor, signaling protein |
| Biological source | Arabidopsis thaliana (mouse-ear cress) |
| Cellular location | Cytoplasm (By similarity): O49686 |
| Total number of polymer chains | 2 |
| Total formula weight | 47813.54 |
| Authors | Arvai, A.S.,Hitomi, K.,Getzoff, E.D. (deposition date: 2009-10-02, release date: 2009-11-17, Last modification date: 2023-09-06) |
| Primary citation | Nishimura, N.,Hitomi, K.,Arvai, A.S.,Rambo, R.P.,Hitomi, C.,Cutler, S.R.,Schroeder, J.I.,Getzoff, E.D. Structural mechanism of abscisic acid binding and signaling by dimeric PYR1. Science, 326:1373-1379, 2009 Cited by PubMed Abstract: The phytohormone abscisic acid (ABA) acts in seed dormancy, plant development, drought tolerance, and adaptive responses to environmental stresses. Structural mechanisms mediating ABA receptor recognition and signaling remain unknown but are essential for understanding and manipulating abiotic stress resistance. Here, we report structures of pyrabactin resistance 1 (PYR1), a prototypical PYR/PYR1-like (PYL)/regulatory component of ABA receptor (RCAR) protein that functions in early ABA signaling. The crystallographic structure reveals an alpha/beta helix-grip fold and homodimeric assembly, verified in vivo by coimmunoprecipitation. ABA binding within a large internal cavity switches structural motifs distinguishing ABA-free "open-lid" from ABA-bound "closed-lid" conformations. Small-angle x-ray scattering suggests that ABA signals by converting PYR1 to a more compact, symmetric closed-lid dimer. Site-directed PYR1 mutants designed to disrupt hormone binding lose ABA-triggered interactions with type 2C protein phosphatase partners in planta. PubMed: 19933100DOI: 10.1126/science.1181829 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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