7XVK

Modularity of Phytophthora effectors enables host mimicry of a principal phosphatase

Summary for 7XVK

• Entry DOI: 10.2210/pdb7xvk/pdb
• Descriptor: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform, RxLR effector protein PSR2, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: plant immunology, translocation, effector, phosphatase, immune system
• Biological source: Arabidopsis thaliana (thale cress); More
• Total number of polymer chains: 2
• Total formula weight: 112053.59

Authors

Wang, J.,Wang, Y. (deposition date: 2022-05-24, release date: 2023-07-05, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.29 Å)