Journal
STRUCTURE
Volume 24, Issue 7, Pages 1192-1200Publisher
CELL PRESS
DOI: 10.1016/j.str.2016.04.014
Keywords
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Funding
- Projects of International Cooperation and Exchanges NSFC [31420103906]
- Chinese Ministry of Science and Technology [2015CB910200]
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Chitin is the major component of fungal cell wall and serves as a molecular pattern that can be recognized by the receptor OsCEBiP in rice, a lysine motif (LysM) receptor-like protein (RLP), to trigger immune responses. The molecular mechanisms underlying chitin recognition remain elusive. Here we report the crystal structures of the ectodomain of OsCEBiP (OsCEBiP-ECD) in free and chitin-bound forms. The structures reveal that OsCEBiP-ECD contains three tandem LysMs followed by a novel structure fold of cysteine-rich domain. The structures showed that chitin binding induces no striking conformational changes in OsCEBiP. Structural comparison among N-acetylglucosamine (NAG) oligomer-bound LysMs revealed a highly conserved recognition mechanism, which is expected to facilitate study of other LysM-containing proteins for their NAG binding. Modeling study showed that chitin induces OsCEBiP homodimerization in a sliding mode. Our data provide insights into rice chitin receptor-mediated immunity triggered by fungal cell wall.
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