5JHJ

M. Oryzae effector AVR-Pia mutant H3

Summary for 5JHJ

• Entry DOI: 10.2210/pdb5jhj/pdb
• NMR Information: BMRB: 30068
• Descriptor: Antivirulence protein AVR-Pia (1 entity in total)
• Functional Keywords: avirulence effector magnaporthe oryzae, structure from molmol, rga5-binding protein, unknown function
• Biological source: Magnaporthe oryzae (Rice blast fungus)
• Total number of polymer chains: 1
• Total formula weight: 10830.05

Authors

Padilla, A.,deGuillen, K. (deposition date: 2016-04-21, release date: 2017-03-29, Last modification date: 2024-10-09)

Primary citation

Ortiz, D.,de Guillen, K.,Cesari, S.,Chalvon, V.,Gracy, J.,Padilla, A.,Kroj, T.
Recognition of the Magnaporthe oryzae Effector AVR-Pia by the Decoy Domain of the Rice NLR Immune Receptor RGA5.
Plant Cell, 29:156-168, 2017

PubMed Abstract: Nucleotide binding domain and leucine-rich repeat proteins (NLRs) are important receptors in plant immunity that allow recognition of pathogen effectors. The rice () NLR RGA5 recognizes the effector AVR-Pia through direct interaction. Here, we gained detailed insights into the molecular and structural bases of AVR-Pia-RGA5 interaction and the role of the RATX1 decoy domain of RGA5. NMR titration combined with in vitro and in vivo protein-protein interaction analyses identified the AVR-Pia interaction surface that binds to the RATX1 domain. Structure-informed AVR-Pia mutants showed that, although AVR-Pia associates with additional sites in RGA5, binding to the RATX1 domain is necessary for pathogen recognition but can be of moderate affinity. Therefore, RGA5-mediated resistance is highly resilient to mutations in the effector. We propose a model that explains such robust effector recognition as a consequence, and an advantage, of the combination of integrated decoy domains with additional independent effector-NLR interactions.

PubMed: 28087830
DOI: 10.1105/tpc.16.00435

Experimental method

SOLUTION NMR