3ED1
Crystal Structure of Rice GID1 complexed with GA3
Summary for 3ED1
| Entry DOI | 10.2210/pdb3ed1/pdb |
| Related | 3EBL |
| Descriptor | Gibberellin receptor GID1, (4S)-2-METHYL-2,4-PENTANEDIOL, NITRATE ION, ... (6 entities in total) |
| Functional Keywords | alpha/beta hydrolase, lipase, gibberellin signaling pathway, hydrolase, nucleus, receptor, hydrolase receptor |
| Biological source | Oryza sativa subsp. japonica (Rice) |
| Cellular location | Nucleus : Q6L545 |
| Total number of polymer chains | 6 |
| Total formula weight | 249125.48 |
| Authors | Shimada, A.,Nakatsu, T.,Ueguchi-Tanaka, M.,Kato, H.,Matsuoka, M. (deposition date: 2008-09-02, release date: 2008-11-25, Last modification date: 2023-11-01) |
| Primary citation | Shimada, A.,Ueguchi-Tanaka, M.,Nakatsu, T.,Nakajima, M.,Naoe, Y.,Ohmiya, H.,Kato, H.,Matsuoka, M. Structural basis for gibberellin recognition by its receptor GID1. Nature, 456:520-523, 2008 Cited by PubMed Abstract: Gibberellins (GAs) are phytohormones essential for many developmental processes in plants. A nuclear GA receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), has a primary structure similar to that of the hormone-sensitive lipases (HSLs). Here we analyse the crystal structure of Oryza sativa GID1 (OsGID1) bound with GA(4) and GA(3) at 1.9 A resolution. The overall structure of both complexes shows an alpha/beta-hydrolase fold similar to that of HSLs except for an amino-terminal lid. The GA-binding pocket corresponds to the substrate-binding site of HSLs. On the basis of the OsGID1 structure, we mutagenized important residues for GA binding and examined their binding activities. Almost all of them showed very little or no activity, confirming that the residues revealed by structural analysis are important for GA binding. The replacement of Ile 133 with Leu or Val-residues corresponding to those of the lycophyte Selaginella moellendorffii GID1s-caused an increase in the binding affinity for GA(34), a 2beta-hydroxylated GA(4). These observations indicate that GID1 originated from HSL and was further modified to have higher affinity and more strict selectivity for bioactive GAs by adapting the amino acids involved in GA binding in the course of plant evolution. PubMed: 19037316DOI: 10.1038/nature07546 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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