7BNT
Complex of rice blast (Magnaporthe oryzae) effector protein AVR-PikD with a predicted ancestral HMA domain of Pik-1 from Oryza spp.
Summary for 7BNT
| Entry DOI | 10.2210/pdb7bnt/pdb |
| Descriptor | Predicted ancestral HMA domain of Pik-1 from Oryza spp., AVR-Pik protein, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | rice blast disease, plant disease resistance, effector protein, integrated hma domain, protein binding |
| Biological source | synthetic construct More |
| Total number of polymer chains | 3 |
| Total formula weight | 26572.99 |
| Authors | Bialas, A.,Langner, T.,Harant, A.,Contreras, M.P.,Stevenson, C.E.M.,Lawson, D.M.,Sklenar, J.,Kellner, R.,Moscou, M.J.,Terauchi, R.,Banfield, M.J.,Kamoun, S. (deposition date: 2021-01-22, release date: 2021-02-17, Last modification date: 2024-10-09) |
| Primary citation | Bialas, A.,Langner, T.,Harant, A.,Contreras, M.P.,Stevenson, C.E.,Lawson, D.M.,Sklenar, J.,Kellner, R.,Moscou, M.J.,Terauchi, R.,Banfield, M.J.,Kamoun, S. Two NLR immune receptors acquired high-affinity binding to a fungal effector through convergent evolution of their integrated domain. Elife, 10:-, 2021 Cited by PubMed Abstract: A subset of plant NLR immune receptors carry unconventional integrated domains in addition to their canonical domain architecture. One example is rice Pik-1 that comprises an integrated heavy metal-associated (HMA) domain. Here, we reconstructed the evolutionary history of Pik-1 and its NLR partner, Pik-2, and tested hypotheses about adaptive evolution of the HMA domain. Phylogenetic analyses revealed that the HMA domain integrated into Pik-1 before Oryzinae speciation over 15 million years ago and has been under diversifying selection. Ancestral sequence reconstruction coupled with functional studies showed that two Pik-1 allelic variants independently evolved from a weakly binding ancestral state to high-affinity binding of the blast fungus effector AVR-PikD. We conclude that for most of its evolutionary history the Pik-1 HMA domain did not sense AVR-PikD, and that different Pik-1 receptors have recently evolved through distinct biochemical paths to produce similar phenotypic outcomes. These findings highlight the dynamic nature of the evolutionary mechanisms underpinning NLR adaptation to plant pathogens. PubMed: 34288868DOI: 10.7554/eLife.66961 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.32 Å) |
Structure validation
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