3NMH
Crystal structure of the abscisic receptor PYL2 in complex with pyrabactin
Summary for 3NMH
| Entry DOI | 10.2210/pdb3nmh/pdb |
| Related | 3KAZ 3KB0 3KB3 3NMN 3NMP 3NMT 3NMV |
| Descriptor | Abscisic acid receptor PYL2, 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total) |
| Functional Keywords | pyl2, pyrabactin, plant hormone receptor, helix-grip fold, hormone binding, abscisic acid, hormone binding protein |
| Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
| Cellular location | Cytoplasm (By similarity): O80992 |
| Total number of polymer chains | 3 |
| Total formula weight | 61669.89 |
| 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: 2023-09-06) |
| 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 (1.85 Å) |
Structure validation
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