8PQ7

The Potato Late Blight pathogen (Phytophthora infestans) effector protein Pi04134 in complex with potato protein phosphatase type 1c (PP1c).

8PQ7 の概要

• エントリーDOI: 10.2210/pdb8pq7/pdb
• 分子名称: Serine/threonine-protein phosphatase, RxLR effector protein PexRD24, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: protein complex, plant pathogen interactions, effector protein, phosphatase, plant protein
• 由来する生物種: Solanum tuberosum (potato); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 88507.55

構造登録者

Bentham, A.R.,Banfield, M.J. (登録日: 2023-07-10, 公開日: 2023-07-19, 最終更新日: 2024-04-17)

主引用文献

Bentham, A.R.,Wang, W.,Trusch, F.,Varden, F.A.,Birch, P.R.J.,Banfield, M.J.
The WY Domain of an RxLr Effector Drives Interactions with a Host Target Phosphatase to Mimic Host Regulatory Proteins and Promote Phytophthora infestans Infection.
Mol.Plant Microbe Interact., 37:239-249, 2024

PubMed Abstract: Plant pathogens manipulate the cellular environment of the host to facilitate infection and colonization that often lead to plant diseases. To accomplish this, many specialized pathogens secrete virulence proteins called effectors into the host cell, which subvert processes such as immune signaling, gene transcription, and host metabolism. , the causative agent of potato late blight, employs an expanded repertoire of RxLR effectors with WY domains to manipulate the host through direct interaction with protein targets. However, our understanding of the molecular mechanisms underlying the interactions between WY effectors and their host targets remains limited. In this study, we performed a structural and biophysical characterization of the WY effector Pi04314 in complex with the potato Protein Phosphatase 1-c (PP1c). We elucidate how Pi04314 uses a WY domain and a specialized C-terminal loop carrying a KVxF motif that interact with conserved surfaces on PP1c, known to be used by host regulatory proteins for guiding function. Through biophysical and in planta analyses, we demonstrate that Pi04314 WY or KVxF mutants lose their ability to bind PP1c. The loss of PP1c binding correlates with changes in PP1c nucleolar localization and a decrease in lesion size in plant infection assays. This study provides insights into the manipulation of plant hosts by pathogens, revealing how effectors exploit key regulatory interfaces in host proteins to modify their function and facilitate disease. [Formula: see text] Copyright © 2024 The Author(s). This is an open access article distributed under the CC BY 4.0 International license.

PubMed: 37921637
DOI: 10.1094/MPMI-08-23-0118-FI

実験手法

X-RAY DIFFRACTION (2.1 Å)