3JRQ
Crystal structure of (+)-ABA-bound PYL1 in complex with ABI1
Summary for 3JRQ
| Entry DOI | 10.2210/pdb3jrq/pdb |
| Related | 3JRS |
| Descriptor | Protein phosphatase 2C 56, Putative uncharacterized protein At5g46790, (2Z,4E)-5-[(1S)-1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl]-3-methylpenta-2,4-dienoic acid, ... (4 entities in total) |
| Functional Keywords | plant hormone receptor, abscisic acid, pyl1, abi1, type 2c protein phosphatase, abscisic acid signaling pathway, cell membrane, hydrolase, magnesium, manganese, membrane, metal-binding, nucleus, protein phosphatase, hydrolase-hormone receptor complex, hydrolase/hormone receptor |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
| Cellular location | Nucleus: P49597 Cytoplasm (By similarity): Q8VZS8 |
| Total number of polymer chains | 2 |
| Total formula weight | 57587.24 |
| Authors | Miyazono, K.,Miyakawa, T.,Sawano, Y.,Kubota, K.,Tanokura, M. (deposition date: 2009-09-08, release date: 2009-11-03, Last modification date: 2023-11-01) |
| Primary citation | Miyazono, K.,Miyakawa, T.,Sawano, Y.,Kubota, K.,Kang, H.J.,Asano, A.,Miyauchi, Y.,Takahashi, M.,Zhi, Y.,Fujita, Y.,Yoshida, T.,Kodaira, K.,Yamaguchi-Shinozaki, K.,Tanokura, M. Structural basis of abscisic acid signalling Nature, 462:609-614, 2009 Cited by PubMed Abstract: The phytohormone abscisic acid (ABA) mediates the adaptation of plants to environmental stresses such as drought and regulates developmental signals such as seed maturation. Within plants, the PYR/PYL/RCAR family of START proteins receives ABA to inhibit the phosphatase activity of the group-A protein phosphatases 2C (PP2Cs), which are major negative regulators in ABA signalling. Here we present the crystal structures of the ABA receptor PYL1 bound with (+)-ABA, and the complex formed by the further binding of (+)-ABA-bound PYL1 with the PP2C protein ABI1. PYL1 binds (+)-ABA using the START-protein-specific ligand-binding site, thereby forming a hydrophobic pocket on the surface of the closed lid. (+)-ABA-bound PYL1 tightly interacts with a PP2C domain of ABI1 by using the hydrophobic pocket to cover the active site of ABI1 like a plug. Our results reveal the structural basis of the mechanism of (+)-ABA-dependent inhibition of ABI1 by PYL1 in ABA signalling. PubMed: 19855379DOI: 10.1038/nature08583 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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