6TO9

Crystal structure of the oligomerisation domain of the transcription factor PHOSPHATE STARVATION RESPONSE 1 from Arabidopsis (crystal form 2)

これはPDB形式変換不可エントリーです。

6TO9 の概要

• エントリーDOI: 10.2210/pdb6to9/pdb
• 関連するPDBエントリー: 6TO5
• 分子名称: Protein PHOSPHATE STARVATION RESPONSE 1, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: phosphate starvation, myb domain, coiled-coil domain, inositol pyrophosphate, plant nutrition, transcription
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18655.60

構造登録者

Hothorn, M. (登録日: 2019-12-11, 公開日: 2021-01-13, 最終更新日: 2024-01-24)

主引用文献

Ried, M.K.,Wild, R.,Zhu, J.,Pipercevic, J.,Sturm, K.,Broger, L.,Harmel, R.K.,Abriata, L.A.,Hothorn, L.A.,Fiedler, D.,Hiller, S.,Hothorn, M.
Inositol pyrophosphates promote the interaction of SPX domains with the coiled-coil motif of PHR transcription factors to regulate plant phosphate homeostasis.
Nat Commun, 12:384-384, 2021

PubMed Abstract: Phosphorus is an essential nutrient taken up by organisms in the form of inorganic phosphate (Pi). Eukaryotes have evolved sophisticated Pi sensing and signaling cascades, enabling them to stably maintain cellular Pi concentrations. Pi homeostasis is regulated by inositol pyrophosphate signaling molecules (PP-InsPs), which are sensed by SPX domain-containing proteins. In plants, PP-InsP-bound SPX receptors inactivate Myb coiled-coil (MYB-CC) Pi starvation response transcription factors (PHRs) by an unknown mechanism. Here we report that a InsP-SPX complex targets the plant-unique CC domain of PHRs. Crystal structures of the CC domain reveal an unusual four-stranded anti-parallel arrangement. Interface mutations in the CC domain yield monomeric PHR1, which is no longer able to bind DNA with high affinity. Mutation of conserved basic residues located at the surface of the CC domain disrupt interaction with the SPX receptor in vitro and in planta, resulting in constitutive Pi starvation responses. Together, our findings suggest that InsP regulates plant Pi homeostasis by controlling the oligomeric state and hence the promoter binding capability of PHRs via their SPX receptors.

PubMed: 33452263
DOI: 10.1038/s41467-020-20681-4

実験手法

X-RAY DIFFRACTION (2.45 Å)