5JCE

Crystal structure of OsCEBiP complex

Summary for 5JCE

• Entry DOI: 10.2210/pdb5jce/pdb
• Related: 5JCD
• Related PRD ID: PRD_900017
• Descriptor: Chitin elicitor-binding protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: rice chitin receptor, sugar binding protein
• Biological source: Oryza sativa subsp. japonica (Rice)
• Cellular location: Cell membrane ; Single-pass membrane protein : Q8H8C7
• Total number of polymer chains: 2
• Total formula weight: 63834.28

Authors

Chai, J.J.,Liu, S.M.,Wang, J.Z. (deposition date: 2016-04-15, release date: 2016-06-08, Last modification date: 2024-10-16)

Primary citation

Liu, 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

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

Experimental method

X-RAY DIFFRACTION (2.51 Å)