PDBsum entry 5c8q

Sugar binding protein

PDB id

5c8q

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Contents

			Protein chain

					151 a.a.

			Ligands

					NAG-NAG-NAG-NAG

			Waters ×94

PDB id:

5c8q

Links

Name:

Sugar binding protein

Title:

Crystal structure of mocvnh3 variant (mo0v) in complex with (n- glcnac)4

Structure:

Mocvnh3 variant. Chain: b. Fragment: unp residues 175-341. Engineered: yes

Source:

Magnaporthe oryzae. Rice blast fungus. Organism_taxid: 318829. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.90Å

R-factor:

0.227

R-free:

0.256

Authors:

L.M.I.Koharudin,A.M.Gronenborn

Key ref:

L.M.Koharudin et al. (2015). Structural Insight into Fungal Cell Wall Recognition by a CVNH Protein with a Single LysM Domain. Structure, 23, 2143-2154. PubMed id: 26455798 DOI: 10.1016/j.str.2015.07.023

Date:

25-Jun-15

Release date:

12-Aug-15

PROCHECK

	Headers

	References

Protein chain

G4N991 (G4N991_MAGO7) - LysM domain-containing protein from Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)

Seq: Struc:					340 a.a. 151 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1016/j.str.2015.07.023	Structure 23:2143-2154 (2015)
PubMed id: 26455798

Structural Insight into Fungal Cell Wall Recognition by a CVNH Protein with a Single LysM Domain.
L.M.Koharudin, K.T.Debiec, A.M.Gronenborn.

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.