6KUN
Crystal structure of dioxygenase for auxin oxidation (DAO) in rice
Summary for 6KUN
| Entry DOI | 10.2210/pdb6kun/pdb |
| Descriptor | 2-oxoglutarate-dependent dioxygenase DAO, 2-OXOGLUTARIC ACID, 1H-INDOL-3-YLACETIC ACID, ... (5 entities in total) |
| Functional Keywords | jelly rolls, metal ion binding, oxygenase, biosynthetic protein |
| Biological source | Oryza sativa subsp. indica (Rice) |
| Total number of polymer chains | 2 |
| Total formula weight | 65293.58 |
| Authors | Takehara, S.,Mikami, B.,Sakuraba, S.,Matsuoka, M.,Ueguchi-Tanaka, M. (deposition date: 2019-09-02, 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 (2.002 Å) |
Structure validation
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