5C8P
Crystal structure of MoCVNH3 variant (Mo0v) in complex with (N-GlcNAc)3
Summary for 5C8P
| Entry DOI | 10.2210/pdb5c8p/pdb |
| Related | 5C8O 5C8Q |
| Related PRD ID | PRD_900017 |
| Descriptor | MoCVNH3 variant, 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 (3 entities in total) |
| Functional Keywords | lectin, n-acetylglucosamine, cvnh, sugar binding protein |
| Biological source | Magnaporthe oryzae (Rice blast fungus) |
| Total number of polymer chains | 1 |
| Total formula weight | 17973.59 |
| Authors | Koharudin, L.M.I.,Gronenborn, A.M. (deposition date: 2015-06-25, release date: 2015-08-12, Last modification date: 2023-09-27) |
| Primary citation | 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 Cited by 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: 26455798DOI: 10.1016/j.str.2015.07.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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