2LAI

Hyaloperonospora arabidopsidis Effector Protein ATR13

Summary for 2LAI

• Entry DOI: 10.2210/pdb2lai/pdb
• NMR Information: BMRB: 17525
• Descriptor: Avirulence protein ATR13 (1 entity in total)
• Functional Keywords: nucleolar localization, signaling protein
• Biological source: Hyaloperonospora parasitica
• Total number of polymer chains: 1
• Total formula weight: 11305.88

Authors

Leonelli, L.,Pelton, J.G.,Wemmer, D.E.,Staskawicz, B.J. (deposition date: 2011-03-15, release date: 2012-01-18, Last modification date: 2024-05-01)

Primary citation

Leonelli, L.,Pelton, J.,Schoeffler, A.,Dahlbeck, D.,Berger, J.,Wemmer, D.E.,Staskawicz, B.
Structural Elucidation and Functional Characterization of the Hyaloperonospora arabidopsidis Effector Protein ATR13.
Plos Pathog., 7:e1002428-e1002428, 2011

PubMed Abstract: The oomycete Hyaloperonospora arabidopsidis (Hpa) is the causal agent of downy mildew on the model plant Arabidopsis thaliana and has been adapted as a model system to investigate pathogen virulence strategies and plant disease resistance mechanisms. Recognition of Hpa infection occurs when plant resistance proteins (R-genes) detect the presence or activity of pathogen-derived protein effectors delivered to the plant host. This study examines the Hpa effector ATR13 Emco5 and its recognition by RPP13-Nd, the cognate R-gene that triggers programmed cell death (HR) in the presence of recognized ATR13 variants. Herein, we use NMR to solve the backbone structure of ATR13 Emco5, revealing both a helical domain and a disordered internal loop. Additionally, we use site-directed and random mutagenesis to identify several amino acid residues involved in the recognition response conferred by RPP13-Nd. Using our structure as a scaffold, we map these residues to one of two surface-exposed patches of residues under diversifying selection. Exploring possible roles of the disordered region within the ATR13 structure, we perform domain swapping experiments and identify a peptide sequence involved in nucleolar localization. We conclude that ATR13 is a highly dynamic protein with no clear structural homologues that contains two surface-exposed patches of polymorphism, only one of which is involved in RPP13-Nd recognition specificity.

PubMed: 22194684
DOI: 10.1371/journal.ppat.1002428

Experimental method

SOLUTION NMR