2L9Y

Solution structure of the MoCVNH-LysM module from the rice blast fungus Magnaporthe oryzae protein (MGG_03307)

2L9Y の概要

• エントリーDOI: 10.2210/pdb2l9y/pdb
• NMR情報: BMRB: 17493
• 分子名称: CVNH-LysM lectin (1 entity in total)
• 機能のキーワード: cvnh, lectin, carbohydrate, sugar binding protein
• 由来する生物種: Magnaporthe oryzae 70-15 (Rice blast fungus)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18176.84

構造登録者

Koharudin, L.M.I.,Viscomi, A.R.,Montanini, B.,Kershaw, M.J.,Talbot, N.J.,Ottonello, S.,Gronenborn, A.M. (登録日: 2011-02-26, 公開日: 2011-03-23, 最終更新日: 2024-05-01)

主引用文献

Koharudin, L.M.,Viscomi, A.R.,Montanini, B.,Kershaw, M.J.,Talbot, N.J.,Ottonello, S.,Gronenborn, A.M.
Structure-Function Analysis of a CVNH-LysM Lectin Expressed during Plant Infection by the Rice Blast Fungus Magnaporthe oryzae.
Structure, 19:662-674, 2011

PubMed Abstract: The rice blast fungus Magnaporthe oryzae's genome encodes a hypothetical protein (MGG_03307) containing a type III CVNH lectin, in which a LysM domain is inserted between individual repeats of a single CVNH domain. At present, no structural or ligand binding data are available for any type III CVNH and functional studies in natural source organisms are scarce. Here, we report NMR solution structure and functional data on MGG_03307. The structure of the CVNH/LysM module revealed that intact and functionally competent CVNH and LysM domains are present. Using NMR titrations, carbohydrate specificities for both domains were determined, and it was found that each domain behaves as an isolated unit without any interdomain communication. Furthermore, live-cell imaging revealed a predominant localization of MGG_03307 within the appressorium, the specialized fungal cell for gaining entry into rice tissue. Our results suggest that MGG_03307 plays a role in the early stages of plant infection.

PubMed: 21565701
DOI: 10.1016/j.str.2011.03.004

実験手法

SOLUTION NMR