6KUN

Crystal structure of dioxygenase for auxin oxidation (DAO) in rice

6KUN の概要

• エントリーDOI: 10.2210/pdb6kun/pdb
• 分子名称: 2-oxoglutarate-dependent dioxygenase DAO, 2-OXOGLUTARIC ACID, 1H-INDOL-3-YLACETIC ACID, ... (5 entities in total)
• 機能のキーワード: jelly rolls, metal ion binding, oxygenase, biosynthetic protein
• 由来する生物種: Oryza sativa subsp. indica (Rice)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65293.58

構造登録者

Takehara, S.,Mikami, B.,Sakuraba, S.,Matsuoka, M.,Ueguchi-Tanaka, M. (登録日: 2019-09-02, 公開日: 2020-05-13, 最終更新日: 2024-10-23)

主引用文献

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

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: 32358569
DOI: 10.1038/s41467-020-16068-0

実験手法

X-RAY DIFFRACTION (2.002 Å)