6FUD

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

6FUD の概要

• エントリーDOI: 10.2210/pdb6fud/pdb
• 関連するPDBエントリー: 6FU9 6FUB 6G10 6G11
• 分子名称: NBS-LRR class disease resistance protein, AVR-Pik protein (3 entities in total)
• 機能のキーワード: plant nlr, fungal effector, plant immunity, complex, antifungal protein
• 由来する生物種: Oryza sativa subsp. japonica (Rice); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19383.26

構造登録者

Franceschetti, M.,De la Concepcion, J.C.,Banfield, M.J. (登録日: 2018-02-26, 公開日: 2018-06-13, 最終更新日: 2024-11-20)

主引用文献

De 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

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

実験手法

X-RAY DIFFRACTION (1.3 Å)