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7YWF

Monocot chimeric jacalin JAC1 from Oryza sativa: dirigent domain with bound galactobiose

Summary for 7YWF
Entry DOI10.2210/pdb7ywf/pdb
Related7R5Z 7YWE 7YWG 7YWW
Related PRD IDPRD_900113
DescriptorDirigent protein, beta-D-galactopyranose-(1-4)-beta-D-galactopyranose, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (6 entities in total)
Functional Keywordsmonocot chimeric jacalin, dirigent protein, lectin, pathogen resistance, plant protein
Biological sourceOryza sativa (rice)
Total number of polymer chains3
Total formula weight53754.33
Authors
Huwa, N.,Classen, T.,Weiergraeber, O.H. (deposition date: 2022-02-13, release date: 2022-05-04, Last modification date: 2024-01-31)
Primary citationHuwa, N.,Weiergraber, O.H.,Fejzagic, A.V.,Kirsch, C.,Schaffrath, U.,Classen, T.
The Crystal Structure of the Defense Conferring Rice Protein Os JAC1 Reveals a Carbohydrate Binding Site on the Dirigent-like Domain.
Biomolecules, 12:-, 2022
Cited by
PubMed Abstract: Pesticides are routinely used to prevent severe losses in agriculture. This practice is under debate because of its potential negative environmental impact and selection of resistances in pathogens. Therefore, the development of disease resistant plants is mandatory. It was shown that the rice () protein JAC1 enhances resistance against different bacterial and fungal plant pathogens in rice, barley, and wheat. Recently we reported possible carbohydrate interaction partners for both domains of JAC1 (a jacalin-related lectin (JRL) and a dirigent (DIR) domain), however, a mechanistic understanding of its function is still lacking. Here, we report crystal structures for both individual domains and the complex of galactobiose with the DIR domain, which revealed a new carbohydrate binding motif for DIR proteins. Docking studies of the two domains led to a model of the full-length protein. Our findings offer insights into structure and binding properties of JAC1 and its possible function in pathogen resistance.
PubMed: 36009020
DOI: 10.3390/biom12081126
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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