5L83

Complex of potato ATG8 protein with a peptide from Irish potato famine pathogen effector protein PexRD54

Summary for 5L83

• Entry DOI: 10.2210/pdb5l83/pdb
• Descriptor: ASP-TRP-GLU-ILE-VAL, Autophagy-related protein, SULFATE ION, ... (5 entities in total)
• Functional Keywords: autophagy-related protein 8, atg8 interacting moif, effector protein, immune system
• Biological source: Solanum tuberosum (Potato); More
• Total number of polymer chains: 4
• Total formula weight: 28106.07

Authors

Maqbool, A.,Hughes, R.K.,Banfield, M.J. (deposition date: 2016-06-06, release date: 2016-08-03, Last modification date: 2024-05-08)

Primary citation

Maqbool, A.,Hughes, R.K.,Dagdas, Y.F.,Tregidgo, N.,Zess, E.,Belhaj, K.,Round, A.,Bozkurt, T.O.,Kamoun, S.,Banfield, M.J.
Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54.
J.Biol.Chem., 291:20270-20282, 2016

PubMed Abstract: Filamentous plant pathogens deliver effector proteins to host cells to promote infection. The Phytophthora infestans RXLR-type effector PexRD54 binds potato ATG8 via its ATG8 family-interacting motif (AIM) and perturbs host-selective autophagy. However, the structural basis of this interaction remains unknown. Here, we define the crystal structure of PexRD54, which includes a modular architecture, including five tandem repeat domains, with the AIM sequence presented at the disordered C terminus. To determine the interface between PexRD54 and ATG8, we solved the crystal structure of potato ATG8CL in complex with a peptide comprising the effector's AIM sequence, and we established a model of the full-length PexRD54-ATG8CL complex using small angle x-ray scattering. Structure-informed deletion of the PexRD54 tandem domains reveals retention of ATG8CL binding in vitro and in planta This study offers new insights into structure/function relationships of oomycete RXLR effectors and how these proteins engage with host cell targets to promote disease.

PubMed: 27458016
DOI: 10.1074/jbc.M116.744995

Experimental method

X-RAY DIFFRACTION (1.9 Å)