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Structure paper

TitleBioengineering a plant NLR immune receptor with a robust binding interface toward a conserved fungal pathogen effector.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 121, Page e2402872121-e2402872121, Year 2024
Publish dateNov 24, 2023 (structure data deposition date)
AuthorsZdrzalek, R. / Xi, Y. / Langner, T. / Bentham, A.R. / Petit-Houdenot, Y. / De la Concepcion, J.C. / Harant, A. / Shimizu, M. / Were, V. / Talbot, N.J. ...Zdrzalek, R. / Xi, Y. / Langner, T. / Bentham, A.R. / Petit-Houdenot, Y. / De la Concepcion, J.C. / Harant, A. / Shimizu, M. / Were, V. / Talbot, N.J. / Terauchi, R. / Kamoun, S. / Banfield, M.J.
External linksProc. Natl. Acad. Sci. USA / PubMed:38968126
MethodsX-ray diffraction
Resolution1.8 - 2.5 Å
Structure data

PDB-8r7a:
Complex of rice blast (Magnaporthe oryzae) effector protein PWL2 with the HMA domain of OsHIPP43 from rice (Oryza sativa)
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-8r7d:
Complex of rice blast (Magnaporthe oryzae) mutant effector protein PWL2-SNDE with the HMA domain of OsHIPP43 from rice (Oryza sativa)
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • oryza sativa (Asian cultivated rice)
  • pyricularia oryzae (rice blast fungus)
KeywordsPLANT PROTEIN / Pathogen effector / host target protein / rice blast / disease resistance

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