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5GNC

Crystal structure of Phytophthora. sojae PSR2

Summary for 5GNC
Entry DOI10.2210/pdb5gnc/pdb
DescriptorAvh146 (1 entity in total)
Functional Keywordspsr2, rnai, unknown function
Biological sourcePhytophthora sojae (Soybean stem and root rot agent)
Total number of polymer chains1
Total formula weight68991.92
Authors
He, J.Q.,Wu, B.X.,Ma, J.B. (deposition date: 2016-07-20, release date: 2017-08-16, Last modification date: 2024-10-30)
Primary citationHe, J.Q.,Ye, W.W.,Choi, D.S.,Wu, B.X.,Zhai, Y.,Guo, B.D.,Duan, S.Y.,Wang, Y.C.,Gan, J.H.,Ma, W.B.,Ma, J.B.
Structural analysis ofPhytophthorasuppressor of RNA silencing 2 (PSR2) reveals a conserved modular fold contributing to virulence.
Proc. Natl. Acad. Sci. U.S.A., 2019
Cited by
PubMed Abstract: are eukaryotic pathogens that cause enormous losses in agriculture and forestry. Each species encodes hundreds of effector proteins that collectively have essential roles in manipulating host cellular processes and facilitating disease development. Here we report the crystal structure of the effector suppressor of RNA silencing 2 (PSR2). PSR2 produced by the soybean pathogen (PSR2) consists of seven tandem repeat units, including one W-Y motif and six L-W-Y motifs. Each L-W-Y motif forms a highly conserved fold consisting of five α-helices. Adjacent units are connected through stable, directional linkages between an internal loop at the C terminus of one unit and a hydrophobic pocket at the N terminus of the following unit. This unique concatenation results in an overall stick-like structure of PSR2. Genome-wide analyses reveal 293 effectors from five species that have the PSR2-like arrangement, that is, containing a W-Y motif as the "start" unit, various numbers of L-W-Y motifs as the "middle" units, and a degenerate L-W-Y as the "end" unit. Residues involved in the interunit interactions show significant conservation, suggesting that these effectors also use the conserved concatenation mechanism. Furthermore, functional analysis demonstrates differential contributions of individual units to the virulence activity of PSR2. These findings suggest that the L-W-Y fold is a basic structural and functional module that may serve as a "building block" to accelerate effector evolution in .
PubMed: 30926664
DOI: 10.1073/pnas.1819481116
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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数据于2025-08-06公开中

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