2ZSI
Structural basis of gibberellin(GA4)-induced DELLA recognition by the gibberellin receptor
Summary for 2ZSI
| Entry DOI | 10.2210/pdb2zsi/pdb |
| Related | 2ZSH |
| Descriptor | Probable gibberellin receptor GID1L1, DELLA protein GAI, GIBBERELLIN A4, ... (4 entities in total) |
| Functional Keywords | plant hormone receptor, alpha/beta-hydrolase fold, carboxyesterase family, gibberellin signaling pathway, hydrolase, nucleus, receptor, developmental protein, phosphoprotein, repressor, transcription, transcription regulation, ubl conjugation, hormone receptor |
| Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) More |
| Cellular location | Nucleus (By similarity): Q9MAA7 Nucleus: Q9LQT8 |
| Total number of polymer chains | 2 |
| Total formula weight | 51888.31 |
| Authors | Murase, K.,Hirano, Y.,Sun, T.P.,Hakoshima, T. (deposition date: 2008-09-10, release date: 2008-11-25, Last modification date: 2023-11-01) |
| Primary citation | Murase, K.,Hirano, Y.,Sun, T.-P.,Hakoshima, T. Gibberellin-induced DELLA recognition by the gibberellin receptor GID1 Nature, 456:459-463, 2008 Cited by PubMed Abstract: Gibberellins control a range of growth and developmental processes in higher plants and have been widely used in the agricultural industry. By binding to a nuclear receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), gibberellins regulate gene expression by promoting degradation of the transcriptional regulator DELLA proteins, including GIBBERELLIN INSENSITIVE (GAI). The precise manner in which GID1 discriminates and becomes activated by bioactive gibberellins for specific binding to DELLA proteins remains unclear. Here we present the crystal structure of a ternary complex of Arabidopsis thaliana GID1A, a bioactive gibberellin and the amino-terminal DELLA domain of GAI. In this complex, GID1A occludes gibberellin in a deep binding pocket covered by its N-terminal helical switch region, which in turn interacts with the DELLA domain containing DELLA, VHYNP and LExLE motifs. Our results establish a structural model of a plant hormone receptor that is distinct from the mechanism of the hormone perception and effector recognition of the known auxin receptors. PubMed: 19037309DOI: 10.1038/nature07519 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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