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5JCE

Crystal structure of OsCEBiP complex

5JCE の概要
エントリーDOI10.2210/pdb5jce/pdb
関連するPDBエントリー5JCD
関連するBIRD辞書のPRD_IDPRD_900017
分子名称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)
機能のキーワードrice chitin receptor, sugar binding protein
由来する生物種Oryza sativa subsp. japonica (Rice)
細胞内の位置Cell membrane ; Single-pass membrane protein : Q8H8C7
タンパク質・核酸の鎖数2
化学式量合計63834.28
構造登録者
Chai, J.J.,Liu, S.M.,Wang, J.Z. (登録日: 2016-04-15, 公開日: 2016-06-08, 最終更新日: 2024-10-16)
主引用文献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
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.51 Å)
構造検証レポート
Validation report summary of 5jce
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-24に公開中

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