6R8K

Complex of rice blast (Magnaporthe oryzae) effector protein AVR-PikD with an engineered HMA domain of Pikp-1 from rice (Oryza sativa)

Summary for 6R8K

• Entry DOI: 10.2210/pdb6r8k/pdb
• Descriptor: NBS-LRR class disease resistance protein Pikh-1, AVR-Pik protein (3 entities in total)
• Functional Keywords: nlr, complex, hma, rice blast, plant protein
• Biological source: Oryza sativa subsp. japonica (Japanese rice); More
• Total number of polymer chains: 2
• Total formula weight: 19216.16

Authors

De la Concepcion, J.C.,Franceschetti, M.,Banfield, M.J. (deposition date: 2019-04-02, release date: 2019-04-24, Last modification date: 2024-10-16)

Primary citation

De la Concepcion, J.C.,Franceschetti, M.,MacLean, D.,Terauchi, R.,Kamoun, S.,Banfield, M.J.
Protein engineering expands the effector recognition profile of a rice NLR immune receptor.
Elife, 8:-, 2019

PubMed Abstract: Plant nucleotide binding, leucine-rich repeat (NLR) receptors detect pathogen effectors and initiate an immune response. Since their discovery, NLRs have been the focus of protein engineering to improve disease resistance. However, this approach has proven challenging, in part due to their narrow response specificity. Previously, we revealed the structural basis of pathogen recognition by the integrated heavy metal associated (HMA) domain of the rice NLR Pikp (Maqbool et al., 2015). Here, we used structure-guided engineering to expand the response profile of Pikp to variants of the rice blast pathogen effector AVR-Pik. A mutation located within an effector-binding interface of the integrated Pikp-HMA domain increased the binding affinity for AVR-Pik variants in vitro and in vivo. This translates to an expanded cell-death response to AVR-Pik variants previously unrecognized by Pikp in planta. The structures of the engineered Pikp-HMA in complex with AVR-Pik variants revealed the mechanism of expanded recognition. These results provide a proof-of-concept that protein engineering can improve the utility of plant NLR receptors where direct interaction between effectors and NLRs is established, particularly where this interaction occurs via integrated domains.

PubMed: 31535976
DOI: 10.7554/eLife.47713

Experimental method

X-RAY DIFFRACTION (1.6 Å)