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5JCD

Crystal structure of OsCEBiP

Summary for 5JCD
Entry DOI10.2210/pdb5jcd/pdb
Related5JCE
DescriptorChitin elicitor-binding protein, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
Functional Keywordschitin receptor, sugar binding protein
Biological sourceOryza sativa subsp. japonica (Rice)
Cellular locationCell membrane ; Single-pass membrane protein : Q8H8C7
Total number of polymer chains3
Total formula weight62922.82
Authors
Chai, J.J.,Liu, S.M.,Wang, J.Z. (deposition date: 2016-04-15, release date: 2017-02-22, Last modification date: 2024-11-13)
Primary citationLiu, S.M.,Wang, J.Z.,Han, Z.,Gong, X.,Zhang, H.,Chai, J.J.
Molecular Mechanism for Fungal Cell Wall Recognition by Rice Chitin Receptor OsCEBiP
Structure, 24:1192-1200, 2016
Cited by
PubMed Abstract: 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.
PubMed: 27238968
DOI: 10.1016/j.str.2016.04.014
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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