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TitleAllelic compatibility in plant immune receptors facilitates engineering of new effector recognition specificities.
Journal, issue, pagesPlant Cell, Vol. 35, Page 3809-3827, Year 2023
Publish dateSep 14, 2022 (structure data deposition date)
AuthorsBentham, A.R. / De la Concepcion, J.C. / Benjumea, J.V. / Kourelis, J. / Jones, S. / Mendel, M. / Stubbs, J. / Stevenson, C.E.M. / Maidment, J.H.R. / Youles, M. ...Bentham, A.R. / De la Concepcion, J.C. / Benjumea, J.V. / Kourelis, J. / Jones, S. / Mendel, M. / Stubbs, J. / Stevenson, C.E.M. / Maidment, J.H.R. / Youles, M. / Zdrzalek, R. / Kamoun, S. / Banfield, M.J.
External linksPlant Cell / PubMed:37486356
MethodsX-ray diffraction
Resolution1.22 Å
Structure data

PDB-8b2r:
Complex of rice blast (Magnaporthe oryzae) effector protein AVR-PikF with a rice (Oryza sativa) RGA5 HMA domain mutant.
Method: X-RAY DIFFRACTION / Resolution: 1.22 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-CL:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • oryza sativa (Asian cultivated rice)
  • pyricularia oryzae (rice blast fungus)
KeywordsANTIFUNGAL PROTEIN / heavy-metal associated domain / plant immunity / fungal pathogen / Magnaporthe oryzae / rice blast / rice / NLR / MAX effector

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