7XVI

pathogen effectors which are essential to cause plant disease by manipulating cellular processes in the host

7XVI の概要

• エントリーDOI: 10.2210/pdb7xvi/pdb
• 分子名称: PITG_15142, 1,2-ETHANEDIOL, CADMIUM ION, ... (4 entities in total)
• 機能のキーワード: plant immunology, translocation, effector, immune system
• 由来する生物種: Phytophthora infestans (potato late blight agent)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53959.91

構造登録者

Wang, J.,Wang, Y. (登録日: 2022-05-23, 公開日: 2023-07-05, 最終更新日: 2024-05-29)

主引用文献

Li, H.,Wang, J.,Kuan, T.A.,Tang, B.,Feng, L.,Wang, J.,Cheng, Z.,Sklenar, J.,Derbyshire, P.,Hulin, M.,Li, Y.,Zhai, Y.,Hou, Y.,Menke, F.L.H.,Wang, Y.,Ma, W.
Pathogen protein modularity enables elaborate mimicry of a host phosphatase.
Cell, 186:3196-3207.e17, 2023

PubMed Abstract: Pathogens produce diverse effector proteins to manipulate host cellular processes. However, how functional diversity is generated in an effector repertoire is poorly understood. Many effectors in the devastating plant pathogen Phytophthora contain tandem repeats of the "(L)WY" motif, which are structurally conserved but variable in sequences. Here, we discovered a functional module formed by a specific (L)WY-LWY combination in multiple Phytophthora effectors, which efficiently recruits the serine/threonine protein phosphatase 2A (PP2A) core enzyme in plant hosts. Crystal structure of an effector-PP2A complex shows that the (L)WY-LWY module enables hijacking of the host PP2A core enzyme to form functional holoenzymes. While sharing the PP2A-interacting module at the amino terminus, these effectors possess divergent C-terminal LWY units and regulate distinct sets of phosphoproteins in the host. Our results highlight the appropriation of an essential host phosphatase through molecular mimicry by pathogens and diversification promoted by protein modularity in an effector repertoire.

PubMed: 37369204
DOI: 10.1016/j.cell.2023.05.049

実験手法

X-RAY DIFFRACTION (3.11 Å)