5OD4
Avr2 effector protein from the fungal plant pathogen Fusarium oxysporum
Summary for 5OD4
| Entry DOI | 10.2210/pdb5od4/pdb |
| Descriptor | Secreted in xylem 3, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | effector, protein-protein interaction, beta-sandwich, unknown function |
| Biological source | Fusarium oxysporum |
| Total number of polymer chains | 1 |
| Total formula weight | 14379.85 |
| Authors | Hughes, R.K.,Banfield, M.J. (deposition date: 2017-07-04, release date: 2017-08-16, Last modification date: 2024-10-16) |
| Primary citation | Di, X.,Cao, L.,Hughes, R.K.,Tintor, N.,Banfield, M.J.,Takken, F.L.W. Structure-function analysis of the Fusarium oxysporum Avr2 effector allows uncoupling of its immune-suppressing activity from recognition. New Phytol., 216:897-914, 2017 Cited by PubMed Abstract: Plant pathogens employ effector proteins to manipulate their hosts. Fusarium oxysporum f. sp. lycopersici (Fol), the causal agent of tomato wilt disease, produces effector protein Avr2. Besides being a virulence factor, Avr2 triggers immunity in I-2 carrying tomato (Solanum lycopersicum). Fol strains that evade I-2 recognition carry point mutations in Avr2 (e.g. Avr2 ), but retain full virulence. Here we investigate the virulence function of Avr2 and determine its crystal structure. Transgenic tomato and Arabidopsis expressing either wild-type ΔspAvr2 (deleted signal-peptide) or the ΔspAvr2 variant become hypersusceptible to fungal, and even bacterial infections, suggesting that Avr2 targets a conserved defense mechanism. Indeed, Avr2 transgenic plants are attenuated in immunity-related readouts, including flg22-induced growth inhibition, ROS production and callose deposition. The crystal structure of Avr2 reveals that the protein shares intriguing structural similarity to ToxA from the wheat pathogen Pyrenophora tritici-repentis and to TRAF proteins. The I-2 resistance-breaking Avr2 , Avr2 and Avr2 variants cluster on a surface-presented loop. Structure-guided mutagenesis enabled uncoupling of virulence from I-2-mediated recognition. We conclude that I-2-mediated recognition is not based on monitoring Avr2 virulence activity, which includes suppression of immune responses via an evolutionarily conserved effector target, but by recognition of a distinct epitope. PubMed: 28857169DOI: 10.1111/nph.14733 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.1 Å) |
Structure validation
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