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Structure. 2015 Nov 3;23(11):2143-54. doi: 10.1016/j.str.2015.07.023. Epub 2015 Oct 9.

Structural Insight into Fungal Cell Wall Recognition by a CVNH Protein with a Single LysM Domain.

Author information

1
Department of Structural Biology, University of Pittsburgh School of Medicine, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA.
2
Department of Structural Biology, University of Pittsburgh School of Medicine, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA. Electronic address: amg100@pitt.edu.

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.

KEYWORDS:

Chitin; LysM domain; NMR; Protein-carbohydrate complex; X-ray crystallography

PMID:
26455798
PMCID:
PMC4635050
DOI:
10.1016/j.str.2015.07.023
[Indexed for MEDLINE]
Free PMC Article

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