8SXS
Crystal structure of a Nudix hydrolase effector from Magnaporthe oryzae
Summary for 8SXS
| Entry DOI | 10.2210/pdb8sxs/pdb |
| Descriptor | Nudix hydrolase domain-containing protein (2 entities in total) |
| Functional Keywords | nudix hydrolase, effector, inositol pyrophosphate hydrolase, hydrolase |
| Biological source | Pyricularia oryzae 70-15 |
| Total number of polymer chains | 2 |
| Total formula weight | 27384.82 |
| Authors | McCombe, C.L.,Ericsson, D.J.,Williams, S.J. (deposition date: 2023-05-23, release date: 2023-11-22, Last modification date: 2025-03-12) |
| Primary citation | McCombe, C.L.,Wegner, A.,Wirtz, L.,Zamora, C.S.,Casanova, F.,Aditya, S.,Greenwood, J.R.,de Paula, S.,England, E.,Shang, S.,Ericsson, D.J.,Oliveira-Garcia, E.,Williams, S.J.,Schaffrath, U. Plant pathogenic fungi hijack phosphate signaling with conserved enzymatic effectors. Science, 387:955-962, 2025 Cited by PubMed Abstract: Inorganic phosphate (Pi) is essential for life, and plant cells monitor Pi availability by sensing inositol pyrophosphate (PP-InsP) levels. In this work, we describe the hijacking of plant phosphate sensing by a conserved family of Nudix hydrolase effectors from pathogenic and fungi. Structural and enzymatic analyses of the Nudix effector family demonstrate that they selectively hydrolyze PP-InsP. Gene deletion experiments of Nudix effectors in , , and indicate that PP-InsP hydrolysis substantially enhances disease symptoms in diverse pathosystems. Further, we show that this conserved effector family induces phosphate starvation signaling in plants. Our study elucidates a molecular mechanism, used by multiple phytopathogenic fungi, that manipulates the highly conserved plant phosphate sensing pathway to exacerbate disease. PubMed: 40014726DOI: 10.1126/science.adl5764 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.57 Å) |
Structure validation
Download full validation report
