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6KU3

Crystal structure of gibberellin 2-oxidase3 (GA2ox3)in rice

Summary for 6KU3
Entry DOI10.2210/pdb6ku3/pdb
DescriptorGibberellin 2-beta-dioxygenase 3, GIBBERELLIN A4, 2-OXOGLUTARIC ACID, ... (6 entities in total)
Functional Keywordsjelly rolls, metal ion binding, oxygenase, biosynthetic protein
Biological sourceOryza sativa subsp. japonica (Rice)
Total number of polymer chains4
Total formula weight145536.09
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 citationTakehara, 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: 32358569
DOI: 10.1038/s41467-020-16068-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

239492

数据于2025-07-30公开中

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