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5L7S

Crystal structure of RXLR effector PexRD54 from Phytophthora infestans

Summary for 5L7S
Entry DOI10.2210/pdb5l7s/pdb
DescriptorSecreted RxLR effector peptide protein (1 entity in total)
Functional Keywordsrxlr effector, phytophthora infestans, signaling protein
Biological sourcePhytophthora infestans (Potato late blight fungus)
Total number of polymer chains1
Total formula weight34068.89
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 citationMaqbool, 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: 27458016
DOI: 10.1074/jbc.M116.744995
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

240971

數據於2025-08-27公開中

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