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6FUB

Complex of rice blast (Magnaporthe oryzae) effector protein AVR-PikE with the HMA domain of Pikm-1 from rice (Oryza sativa)

Summary for 6FUB
Entry DOI10.2210/pdb6fub/pdb
Related6FU9
DescriptorAVR-Pik protein, NBS-LRR class disease resistance protein (3 entities in total)
Functional Keywordsplant nlr, fungal effector, plant immunity, complex, antifungal protein
Biological sourceMagnaporthe oryzae (Rice blast fungus)
More
Total number of polymer chains2
Total formula weight19351.26
Authors
Franceschetti, M.,De la Concepcion, J.C.,Banfield, M.J. (deposition date: 2018-02-26, release date: 2018-06-13, Last modification date: 2024-10-09)
Primary citationDe la Concepcion, J.C.,Franceschetti, M.,Maqbool, A.,Saitoh, H.,Terauchi, R.,Kamoun, S.,Banfield, M.J.
Polymorphic residues in rice NLRs expand binding and response to effectors of the blast pathogen.
Nat Plants, 4:576-585, 2018
Cited by
PubMed Abstract: Accelerated adaptive evolution is a hallmark of plant-pathogen interactions. Plant intracellular immune receptors (NLRs) often occur as allelic series with differential pathogen specificities. The determinants of this specificity remain largely unknown. Here, we unravelled the biophysical and structural basis of expanded specificity in the allelic rice NLR Pik, which responds to the effector AVR-Pik from the rice blast pathogen Magnaporthe oryzae. Rice plants expressing the Pikm allele resist infection by blast strains expressing any of three AVR-Pik effector variants, whereas those expressing Pikp only respond to one. Unlike Pikp, the integrated heavy metal-associated (HMA) domain of Pikm binds with high affinity to each of the three recognized effector variants, and variation at binding interfaces between effectors and Pikp-HMA or Pikm-HMA domains encodes specificity. By understanding how co-evolution has shaped the response profile of an allelic NLR, we highlight how natural selection drove the emergence of new receptor specificities. This work has implications for the engineering of NLRs with improved utility in agriculture.
PubMed: 29988155
DOI: 10.1038/s41477-018-0194-x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.3 Å)
Structure validation

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