5jce | pdb_00005jce
Crystal structure of OsCEBiP complex
Structural highlights
Function[CEBIP_ORYSJ] Chitin elicitor-binding protein involved in the perception and transduction of chitin oligosaccharide elicitor signal for defense responses.[1] [2] [3] Publication Abstract from PubMedChitin 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. Molecular Mechanism for Fungal Cell Wall Recognition by Rice Chitin Receptor OsCEBiP.,Liu S, Wang J, Han Z, Gong X, Zhang H, Chai J Structure. 2016 May 24. pii: S0969-2126(16)30075-2. doi:, 10.1016/j.str.2016.04.014. PMID:27238968[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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