5ZNE

The crystal structure of immune receptor RGA5A_S of resistance protein Pia from rice (Oryza sativa)

5ZNE の概要

• エントリーDOI: 10.2210/pdb5zne/pdb
• 分子名称: NBS-LRR type protein (2 entities in total)
• 機能のキーワード: rga5a_s, resistance protein, rice, plant protein
• 由来する生物種: Oryza sativa subsp. japonica (Rice)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14895.40

構造登録者

Guo, L.W.,Huang, D.,Liu, J.F.,Peng, Y.L. (登録日: 2018-04-09, 公開日: 2018-10-24, 最終更新日: 2023-11-22)

主引用文献

Guo, L.,Cesari, S.,de Guillen, K.,Chalvon, V.,Mammri, L.,Ma, M.,Meusnier, I.,Bonnot, F.,Padilla, A.,Peng, Y.L.,Liu, J.,Kroj, T.
Specific recognition of two MAX effectors by integrated HMA domains in plant immune receptors involves distinct binding surfaces
Proc. Natl. Acad. Sci. U.S.A., 115:11637-11642, 2018

PubMed Abstract: The structurally conserved but sequence-unrelated MAX ( avirulence and ToxB-like) effectors AVR1-CO39 and AVR-PikD from the blast fungus are recognized by the rice nucleotide-binding domain and leucine-rich repeat proteins (NLRs) RGA5 and Pikp-1, respectively. This involves, in both cases, direct interaction of the effector with a heavy metal-associated (HMA) integrated domain (ID) in the NLR. Here, we solved the crystal structures of a C-terminal fragment of RGA5 carrying the HMA ID (RGA5_S), alone, and in complex with AVR1-CO39 and compared it to the structure of the Pikp1/AVR-PikD complex. In both complexes, HMA ID/MAX effector interactions involve antiparallel alignment of β-sheets from each partner. However, effector-binding occurs at different surfaces in Pikp1 and RGA5, indicating that these interactions evolved independently by convergence of these two MAX effectors to the same type of plant target proteins. Interestingly, the effector-binding surface in RGA5 overlaps with the surface that mediates RGA5 self-interaction. Mutations in the HMA-binding interface of AVR1-CO39 perturb RGA5-binding, in vitro and in vivo, and affect the recognition of in a rice cultivar containing Our study provides detailed insight into the mechanisms of effector recognition by NLRs, which has substantial implications for future engineering of NLRs to expand their recognition specificities. In addition, we propose, as a hypothesis for the understanding of effector diversity, that in the structurally conserved MAX effectors the molecular mechanism of host target protein-binding is conserved rather than the host target proteins themselves.

PubMed: 30355769
DOI: 10.1073/pnas.1810705115

実験手法

X-RAY DIFFRACTION (1.78 Å)