7DV8

The crystal structure of rice immune receptor RGA5-HMA2.

Summary for 7DV8

• Entry DOI: 10.2210/pdb7dv8/pdb
• Descriptor: Disease resistance protein RGA5 (2 entities in total)
• Functional Keywords: immune receptor, plant protein
• Biological source: Oryza sativa subsp. japonica (Rice)
• Total number of polymer chains: 14
• Total formula weight: 110719.10

Authors

Zhang, X.,Liu, J.F. (deposition date: 2021-01-12, release date: 2021-10-20, Last modification date: 2023-11-29)

Primary citation

Liu, Y.,Zhang, X.,Yuan, G.,Wang, D.,Zheng, Y.,Ma, M.,Guo, L.,Bhadauria, V.,Peng, Y.L.,Liu, J.
A designer rice NLR immune receptor confers resistance to the rice blast fungus carrying noncorresponding avirulence effectors.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: Plant nucleotide-binding and leucine-rich repeat (NLR) receptors recognize avirulence effectors directly through their integrated domains (IDs) or indirectly via the effector-targeted proteins. Previous studies have succeeded in generating designer NLR receptors with new recognition profiles by engineering IDs or targeted proteins based on prior knowledge of their interactions with the effectors. However, it is yet a challenge to design a new plant receptor capable of recognizing effectors that function by unknown mechanisms. Several rice NLR immune receptors, including RGA5, possess an integrated heavy metal-associated (HMA) domain that recognizes corresponding Avrs and ToxB-like (MAX) effectors in the rice blast fungus. Here, we report a designer rice NLR receptor RGA5 carrying an engineered, integrated HMA domain (RGA5-HMA2) that can recognize the noncorresponding MAX effector AvrPib and confers the RGA4-dependent resistance to the isolates expressing AvrPib, which originally triggers the Pib-mediated blast resistance via unknown mechanisms. The RGA5-HMA2 domain is contrived based on the high structural similarity of AvrPib with two MAX effectors, AVR-Pia and AVR1-CO39, recognized by cognate RGA5-HMA, the binding interface between AVR1-CO39 and RGA5-HMA, and the distinct surface charge of AvrPib and RAG5-HMA. This work demonstrates that rice NLR receptors with the HMA domain can be engineered to confer resistance to the isolates noncorresponding but structurally similar MAX effectors, which manifest cognate NLR receptor-mediated resistance with unknown mechanisms. Our study also provides a practical approach for developing rice multilines and broad race spectrum-resistant cultivars by introducing a series of engineered NLR receptors.

PubMed: 34702740
DOI: 10.1073/pnas.2110751118

Experimental method

X-RAY DIFFRACTION (2.447 Å)