6UH8

Crystal structure of DAD2 N242I mutant

6UH8 の概要

• エントリーDOI: 10.2210/pdb6uh8/pdb
• 分子名称: Decreased Apical Dominance 2, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: strigolactone receptor, hydrolase
• 由来する生物種: Petunia hybrida (Petunia)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60803.42

構造登録者

Sharma, P.,Hamiaux, C.,Snowden, K.C. (登録日: 2019-09-27, 公開日: 2020-02-26, 最終更新日: 2023-10-11)

主引用文献

Lee, H.W.,Sharma, P.,Janssen, B.J.,Drummond, R.S.M.,Luo, Z.,Hamiaux, C.,Collier, T.,Allison, J.R.,Newcomb, R.D.,Snowden, K.C.
Flexibility of the petunia strigolactone receptor DAD2 promotes its interaction with signaling partners.
J.Biol.Chem., 295:4181-4193, 2020

PubMed Abstract: Strigolactones (SLs) are terpenoid-derived plant hormones that regulate various developmental processes, particularly shoot branching, root development, and leaf senescence. The SL receptor has an unusual mode of action. Upon binding SL, it hydrolyzes the hormone, and then covalently binds one of the hydrolytic products. These initial events enable the SL receptor DAD2 (in petunia) to interact with the F-box protein PhMAX2A of the Skp-Cullin-F-box (SCF) complex and/or a repressor of SL signaling, PhD53A. However, it remains unclear how binding and hydrolysis structurally alters the SL receptor to enable its engagement with signaling partners. Here, we used mutagenesis to alter DAD2 and affect SL hydrolysis or DAD2's ability to interact with its signaling partners. We identified three DAD2 variants whose hydrolytic activity had been separated from the receptor's interactions with PhMAX2A or PhD53A. Two variants, DAD2 and DAD2, having substitutions in the core α/β hydrolase-fold domain and the hairpin, exhibited hormone-independent interactions with PhMAX2A and PhD53A, respectively. Conversely, the DAD2 variant could not interact with PhMAX2A in the presence of SL, but its interaction with PhD53A remained unaffected. Structural analyses of DAD2 and DAD2 revealed only small differences compared with the structure of the WT receptor. Results of molecular dynamics simulations of the DAD2 structure suggested that increased flexibility is a likely cause for its SL-independent interaction with PhMAX2A. Our results suggest that PhMAX2A and PhD53A have distinct binding sites on the SL receptor and that its flexibility is a major determinant of its interactions with these two downstream regulators.

PubMed: 32071083
DOI: 10.1074/jbc.RA119.011509

実験手法

X-RAY DIFFRACTION (1.58 Å)