6KU3
Crystal structure of gibberellin 2-oxidase3 (GA2ox3)in rice
Summary for 6KU3
Entry DOI | 10.2210/pdb6ku3/pdb |
Descriptor | Gibberellin 2-beta-dioxygenase 3, GIBBERELLIN A4, 2-OXOGLUTARIC ACID, ... (6 entities in total) |
Functional Keywords | jelly rolls, metal ion binding, oxygenase, biosynthetic protein |
Biological source | Oryza sativa subsp. japonica (Rice) |
Total number of polymer chains | 4 |
Total formula weight | 145536.09 |
Authors | Takehara, S.,Mikami, B.,Sakuraba, S.,Matsuoka, M.,Ueguchi-Tanaka, M. (deposition date: 2019-08-30, release date: 2020-05-13, Last modification date: 2024-10-23) |
Primary citation | Takehara, S.,Sakuraba, S.,Mikami, B.,Yoshida, H.,Yoshimura, H.,Itoh, A.,Endo, M.,Watanabe, N.,Nagae, T.,Matsuoka, M.,Ueguchi-Tanaka, M. A common allosteric mechanism regulates homeostatic inactivation of auxin and gibberellin. Nat Commun, 11:2143-2143, 2020 Cited by PubMed Abstract: Allosteric regulation is protein activation by effector binding at a site other than the active site. Here, we show via X-ray structural analysis of gibberellin 2-oxidase 3 (GA2ox3), and auxin dioxygenase (DAO), that such a mechanism maintains hormonal homeostasis in plants. Both enzymes form multimers by interacting via GA and indole-3-acetic acid (IAA) at their binding interface. Via further functional analyses we reveal that multimerization of these enzymes gradually proceeds with increasing GA and IAA concentrations; multimerized enzymes have higher specific activities than monomer forms, a system that should favour the maintenance of homeostasis for these phytohormones. Molecular dynamic analysis suggests a possible mechanism underlying increased GA2ox3 activity by multimerization-GA in the interface of oligomerized GA2ox3s may be able to enter the active site with a low energy barrier. In summary, homeostatic systems for maintaining GA and IAA levels, based on a common allosteric mechanism, appear to have developed independently. PubMed: 32358569DOI: 10.1038/s41467-020-16068-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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