2L9Y

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

Summary for 2L9Y

• Entry DOI: 10.2210/pdb2l9y/pdb
• NMR Information: BMRB: 17493
• Descriptor: CVNH-LysM lectin (1 entity in total)
• Functional Keywords: cvnh, lectin, carbohydrate, sugar binding protein
• Biological source: Magnaporthe oryzae 70-15 (Rice blast fungus)
• Total number of polymer chains: 1
• Total formula weight: 18176.84

Authors

Koharudin, L.M.I.,Viscomi, A.R.,Montanini, B.,Kershaw, M.J.,Talbot, N.J.,Ottonello, S.,Gronenborn, A.M. (deposition date: 2011-02-26, release date: 2011-03-23, Last modification date: 2024-05-01)

Primary citation

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

Experimental method

SOLUTION NMR