5A6W
Complex of rice blast (Magnaporthe oryzae) effector protein AVR-PikD with the HMA domain of Pikp1 from rice (Oryza sativa)
Summary for 5A6W
| Entry DOI | 10.2210/pdb5a6w/pdb |
| Related | 5A6P |
| Descriptor | RESISTANCE PROTEIN PIKP-1, AVR-PIK PROTEIN, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | antiviral protein, rice blast disease, plant disease resistance, effector protein, integrated hma domain |
| Biological source | ORYZA SATIVA (RICE) More |
| Total number of polymer chains | 3 |
| Total formula weight | 26804.14 |
| Authors | Maqbool, A.,Saitoh, H.,Franceschetti, M.,Stevenson, C.E.,Uemura, A.,Kanzaki, H.,Kamoun, S.,Terauchi, R.,Banfield, M.J. (deposition date: 2015-07-01, release date: 2015-08-26, Last modification date: 2024-11-06) |
| Primary citation | Maqbool, A.,Saitoh, H.,Franceschetti, M.,Stevenson, C.E.,Uemura, A.,Kanzaki, H.,Kamoun, S.,Terauchi, R.,Banfield, M.J. Structural basis of pathogen recognition by an integrated HMA domain in a plant NLR immune receptor. Elife, 4:-, 2015 Cited by PubMed Abstract: Plants have evolved intracellular immune receptors to detect pathogen proteins known as effectors. How these immune receptors detect effectors remains poorly understood. Here we describe the structural basis for direct recognition of AVR-Pik, an effector from the rice blast pathogen, by the rice intracellular NLR immune receptor Pik. AVR-PikD binds a dimer of the Pikp-1 HMA integrated domain with nanomolar affinity. The crystal structure of the Pikp-HMA/AVR-PikD complex enabled design of mutations to alter protein interaction in yeast and in vitro, and perturb effector-mediated response both in a rice cultivar containing Pikp and upon expression of AVR-PikD and Pikp in the model plant Nicotiana benthamiana. These data reveal the molecular details of a recognition event, mediated by a novel integrated domain in an NLR, which initiates a plant immune response and resistance to rice blast disease. Such studies underpin novel opportunities for engineering disease resistance to plant pathogens in staple food crops. PubMed: 26304198DOI: 10.7554/eLife.08709 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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