5L7S
Crystal structure of RXLR effector PexRD54 from Phytophthora infestans
Summary for 5L7S
Entry DOI | 10.2210/pdb5l7s/pdb |
Descriptor | Secreted RxLR effector peptide protein (1 entity in total) |
Functional Keywords | rxlr effector, phytophthora infestans, signaling protein |
Biological source | Phytophthora infestans (Potato late blight fungus) |
Total number of polymer chains | 1 |
Total formula weight | 34068.89 |
Authors | Maqbool, A.,Hughes, R.K.,Banfield, M.J. (deposition date: 2016-06-03, 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 Cited by 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: 27458016DOI: 10.1074/jbc.M116.744995 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
Download full validation report
