6INR

The crystal structure of phytoplasmal effector causing phyllody symptoms 1 (PHYL1)

6INR の概要

• エントリーDOI: 10.2210/pdb6inr/pdb
• 分子名称: Putative effector, AYWB SAP54-like protein, CADMIUM ION (3 entities in total)
• 機能のキーワード: phytoplasma, phytoplasmal effector causing phyllody 1, gene regulation
• 由来する生物種: 'Echinacea purpurea' witches'-broom phytoplasma
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22049.56

構造登録者

Liao, Y.T.,Lin, S.S.,Ko, T.P.,Wang, H.C. (登録日: 2018-10-26, 公開日: 2019-07-31, 最終更新日: 2024-03-27)

主引用文献

Liao, Y.T.,Lin, S.S.,Lin, S.J.,Sun, W.T.,Shen, B.N.,Cheng, H.P.,Lin, C.P.,Ko, T.P.,Chen, Y.F.,Wang, H.C.
Structural insights into the interaction between phytoplasmal effector causing phyllody 1 and MADS transcription factors.
Plant J., 100:706-719, 2019

PubMed Abstract: Phytoplasmas are bacterial plant pathogens which can induce severe symptoms including dwarfism, phyllody and virescence in an infected plant. Because phytoplasmas infect many important crops such as peanut and papaya they have caused serious agricultural losses. The phytoplasmal effector causing phyllody 1 (PHYL1) is an important phytoplasmal pathogenic factor which affects the biological function of MADS transcription factors by interacting with their K (keratin-like) domain, thus resulting in abnormal plant developments such as phyllody. Until now, lack of information on the structure of PHYL1 has prevented a detailed understanding of the binding mechanism between PHYL1 and the MADS transcription factors. Here, we present the crystal structure of PHYL1 from peanut witches'-broom phytoplasma (PHYL1 ). This protein was found to fold into a unique α-helical hairpin with exposed hydrophobic residues on its surface that may play an important role in its biological function. Using proteomics approaches, we propose a binding mode of PHYL1 with the K domain of the MADS transcription factor SEPALLATA3 (SEP3_K) and identify the residues of PHYL1 that are important for this interaction. Furthermore, using surface plasmon resonance we measure the binding strength of PHYL1 proteins to SEP3_K. Lastly, based on confocal images, we found that α-helix 2 of PHYL1 plays an important role in PHYL1-mediated degradation of SEP3. Taken together, these results provide a structural understanding of the specific binding mechanism between PHYL1 and SEP3_K.

PubMed: 31323156
DOI: 10.1111/tpj.14463

実験手法

X-RAY DIFFRACTION (2.34 Å)