TY  - JOUR
AU  - Huwa, Nikolai
AU  - Weiergräber, Oliver H.
AU  - Fejzagić, Alexander V.
AU  - Kirsch, Christian
AU  - Schaffrath, Ulrich
AU  - Classen, Thomas
TI  - The Crystal Structure of the Defense Conferring Rice Protein OsJAC1 Reveals a Carbohydrate Binding Site on the Dirigent-like Domain
JO  - Biomolecules
VL  - 12
IS  - 8
SN  - 2218-273X
CY  - Basel
PB  - MDPI
M1  - FZJ-2022-03510
SP  - 1126 -
PY  - 2022
AB  - 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 (Oryza sativa) protein OsJAC1 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 OsJAC1 (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 OsJAC1 and its possible function in pathogen resistance.
LB  - PUB:(DE-HGF)16
C6  - 36009020
UR  - <Go to ISI:>//WOS:000847001000001
DO  - DOI:10.3390/biom12081126
UR  - https://juser.fz-juelich.de/record/909907
ER  -