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Structure paper

TitleSpecific recognition of two MAX effectors by integrated HMA domains in plant immune receptors involves distinct binding surfaces
Journal, issue, pagesProc. Natl. Acad. Sci. U.S.A., Vol. 115, Page 11637-11642, Year 2018
Publish dateApr 9, 2018 (structure data deposition date)
AuthorsGuo, L. / Cesari, S. / de Guillen, K. / Chalvon, V. / Mammri, L. / Ma, M. / Meusnier, I. / Bonnot, F. / Padilla, A. / Peng, Y.L. ...Guo, L. / Cesari, S. / de Guillen, K. / Chalvon, V. / Mammri, L. / Ma, M. / Meusnier, I. / Bonnot, F. / Padilla, A. / Peng, Y.L. / Liu, J. / Kroj, T.
External linksProc. Natl. Acad. Sci. U.S.A. / PubMed:30355769
MethodsX-ray diffraction
Resolution1.78 - 2.189 Å
Structure data

PDB-5zne:
The crystal structure of immune receptor RGA5A_S of resistance protein Pia from rice (Oryza sativa)
Method: X-RAY DIFFRACTION / Resolution: 1.78 Å

PDB-5zng:
The crystal complex of immune receptor RGA5A_S of Pia from rice (Oryzae sativa) with rice blast (Magnaporthe oryzae) effector protein AVR1-CO39
Method: X-RAY DIFFRACTION / Resolution: 2.189 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • oryza sativa subsp. japonica (Japanese rice)
  • magnaporthe grisea (fungus)
KeywordsPLANT PROTEIN / RGA5A_S / Resistance Protein / Rice / IMMUNE SYSTEM / rice AVR1-CO39 / effector protein / Magnaporthe oryzae

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