3NMN
Crystal structure of pyrabactin-bound abscisic acid receptor PYL1 in complex with type 2C protein phosphatase ABI1
Summary for 3NMN
| Entry DOI | 10.2210/pdb3nmn/pdb |
| Related | 3KAY 3NMH 3NMP 3NMT 3NMV |
| Descriptor | Abscisic acid receptor PYL1, Protein phosphatase 2C 56, 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide, ... (5 entities in total) |
| Functional Keywords | pyl1, pyrabactin, plant hormone receptor, abscisic acid signaling, protein binding |
| Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) More |
| Cellular location | Cytoplasm (By similarity): Q8VZS8 Nucleus: P49597 |
| Total number of polymer chains | 4 |
| Total formula weight | 112258.11 |
| Authors | Zhou, X.E.,Melcher, K.,Ng, L.-M.,Soon, F.-F.,Xu, Y.,Suino-Powell, K.M.,Kovach, A.,Li, J.,Yong, E.-L.,Xu, H.E. (deposition date: 2010-06-22, release date: 2010-08-25, Last modification date: 2024-10-16) |
| Primary citation | Melcher, K.,Xu, Y.,Ng, L.M.,Zhou, X.E.,Soon, F.F.,Chinnusamy, V.,Suino-Powell, K.M.,Kovach, A.,Tham, F.S.,Cutler, S.R.,Li, J.,Yong, E.L.,Zhu, J.K.,Xu, H.E. Identification and mechanism of ABA receptor antagonism. Nat.Struct.Mol.Biol., 17:1102-1108, 2010 Cited by PubMed Abstract: The phytohormone abscisic acid (ABA) functions through a family of fourteen PYR/PYL receptors, which were identified by resistance to pyrabactin, a synthetic inhibitor of seed germination. ABA activates these receptors to inhibit type 2C protein phosphatases, such as ABI1, yet it remains unclear whether these receptors can be antagonized. Here we demonstrate that pyrabactin is an agonist of PYR1 and PYL1 but is unexpectedly an antagonist of PYL2. Crystal structures of the PYL2-pyrabactin and PYL1-pyrabactin-ABI1 complexes reveal the mechanism responsible for receptor-selective activation and inhibition, which enables us to design mutations that convert PYL1 to a pyrabactin-inhibited receptor and PYL2 to a pyrabactin-activated receptor and to identify new pyrabactin-based ABA receptor agonists. Together, our results establish a new concept of ABA receptor antagonism, illustrate its underlying mechanisms and provide a rational framework for discovering novel ABA receptor ligands. PubMed: 20729862DOI: 10.1038/nsmb.1887 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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