5ZNE

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


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.78 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.218 
  • R-Value Observed: 0.219 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Specific recognition of two MAX effectors by integrated HMA domains in plant immune receptors involves distinct binding surfaces

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.

(2018) Proc Natl Acad Sci U S A 115: 11637-11642

  • DOI: https://doi.org/10.1073/pnas.1810705115
  • Primary Citation of Related Structures:  
    5ZNE, 5ZNG

  • PubMed Abstract: 

    The structurally conserved but sequence-unrelated MAX ( Magnaporthe oryzae avirulence and ToxB-like) effectors AVR1-CO39 and AVR-PikD from the blast fungus M. oryzae 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 HMA /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 HMA and RGA5 HMA , 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 HMA overlaps with the surface that mediates RGA5 HMA self-interaction. Mutations in the HMA-binding interface of AVR1-CO39 perturb RGA5 HMA -binding, in vitro and in vivo, and affect the recognition of M. oryzae in a rice cultivar containing Pi-CO39 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.


  • Organizational Affiliation

    State Key Laboratory of Agrobiotechnology, China Agricultural University, 100083 Beijing, People's Republic of China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NBS-LRR type protein137Oryza sativa Japonica GroupMutation(s): 0 
Gene Names: Os11gRGA5
UniProt
Find proteins for F7J0N2 (Oryza sativa subsp. japonica)
Explore F7J0N2 
Go to UniProtKB:  F7J0N2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupF7J0N2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.78 Å
  • R-Value Free: 0.238 
  • R-Value Work: 0.218 
  • R-Value Observed: 0.219 
  • Space Group: P 43 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 55.619α = 90
b = 55.619β = 90
c = 78.335γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Science Foundation (China)China3157110057

Revision History  (Full details and data files)

  • Version 1.0: 2018-10-24
    Type: Initial release
  • Version 1.1: 2018-11-28
    Changes: Data collection, Database references
  • Version 1.2: 2023-11-22
    Changes: Data collection, Database references, Refinement description