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Significance Effectors are essential virulence proteins. The notoriousPhytophthora pathogens use a large arsenal of effectors to manipulate cellular processes in plant hosts. An overall understanding of effector function and the mechanisms underlying their diversification and adaptation is critical to implementing durable resistance. We analyze the protein structure ofPhytophthora suppressor of RNA silencing 2 (PSR2), which allows the discovery of a conserved structural and functional module that tolerates sequence flexibility. Importantly, this module, often arranged as highly organized tandem repeats that are concatenated through a conserved mechanism, is present in hundreds ofPhytophthora effectors. This study provides insight into effector evolution and offers new opportunities to combat severePhytophthora diseases.

Structural analysis of Phytophthora suppressor of RNA silencing 2 (PSR2) reveals a conserved modular fold contributing to virulence