5C8O

Crystal structure of MoCVNH3 variant (Mo0v)

5C8O の概要

• エントリーDOI: 10.2210/pdb5c8o/pdb
• 関連するPDBエントリー: 5C8P 5C8Q
• 分子名称: MoCVNH3 variant (2 entities in total)
• 機能のキーワード: lectin, n-acetylglucosamine, cvnh, sugar binding protein
• 由来する生物種: Magnaporthe oryzae (Rice blast fungus)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17346.00

構造登録者

Koharudin, L.M.I.,Gronenborn, A.M. (登録日: 2015-06-25, 公開日: 2015-08-12, 最終更新日: 2023-09-27)

主引用文献

Koharudin, L.M.,Debiec, K.T.,Gronenborn, A.M.
Structural Insight into Fungal Cell Wall Recognition by a CVNH Protein with a Single LysM Domain.
Structure, 23:2143-2154, 2015

PubMed Abstract: MGG_03307 is a lectin isolated from Magnaporte oryzae, a fungus that causes devastating rice blast disease. Its function is associated with protecting M. oryzae from the host immune response in plants. To provide the structural basis of how MGG_03307 protects the fungus, crystal structures of its CVNH-LysM module were determined in the absence and presence of GlcNAc-containing cell wall chitin constituents, which can act as pathogen-associated molecular patterns. Our structures revealed that glycan binding is accompanied by a notable conformational change in the LysM domain and that GlcNAc3 and GlcNAc4 are accommodated similarly. GlcNAc5 and GlcNAc6 interact with the LysM domain in multiple conformations, as evidenced by solution nuclear magnetic resonance studies. No dimerization of MoCVNH3 via its LysM domain was observed upon binding to GlcNAc6, unlike in multiple LysM domain-containing proteins. Importantly, we define a specific consensus binding mode for the recognition of GlcNAc oligomers by single LysM domains.

PubMed: 26455798
DOI: 10.1016/j.str.2015.07.023

実験手法

X-RAY DIFFRACTION (2.09 Å)