PDBsum entry 4b9h

Sugar binding protein

PDB id: 4b9h

Contents

Protein chain

189 a.a.

Ligands

NAG-NAG

NDG-NAG-NAG-NAG

NAG

I3C

Waters ×53

PDB id:

4b9h

Name:

Sugar binding protein

Title:

Cladosporium fulvum lysm effector ecp6 in complex with a beta-1,4- linked n-acetyl-d-glucosamine tetramer: i3c heavy atom derivative

Structure:

Extracellular protein 6. Chain: a. Synonym: fungal effector ecp6. Engineered: yes. Other_details: cladosporium fulvum lysm effector ecp6 in complex with a beta-1,4-linked n-acetyl-d-glucosamine tetramer (chitin)

Source:

Passalora fulva. Tomato leaf mold. Organism_taxid: 5499. Expressed in: komagataella pastoris. Expression_system_taxid: 4922.

Resolution:

2.10Å R-factor: 0.213 R-free: 0.266

Authors:

R.Saleem-Batcha,A.Sanchez-Vallet,G.Hansen,B.P.H.J.Thomma,J.R.Mesters

Key ref:

A.Sánchez-Vallet et al. (2013). Fungal effector Ecp6 outcompetes host immune receptor for chitin binding through intrachain LysM dimerization. Elife, 2, e00790. PubMed id: 23840930 DOI: 10.7554/eLife.00790

Date:

04-Sep-12 Release date: 17-Jul-13

Protein chain

B3VBK9  (LYSM_PASFU) -  Secreted LysM effector ECP6 from Passalora fulva

Seq: 228 a.a.

Struc: 189 a.a.

DOI no: 10.7554/eLife.00790

Elife 2:e00790 (2013)

PubMed id: 23840930

Fungal effector Ecp6 outcompetes host immune receptor for chitin binding through intrachain LysM dimerization.

A.Sánchez-Vallet, R.Saleem-Batcha, A.Kombrink, G.Hansen, D.J.Valkenburg, B.P.Thomma, J.R.Mesters.

ABSTRACT

While host immune receptors detect pathogen-associated molecular patterns to activate immunity, pathogens attempt to deregulate host immunity through secreted effectors. Fungi employ LysM effectors to prevent recognition of cell wall-derived chitin by host immune receptors, although the mechanism to compete for chitin binding remained unclear. Structural analysis of the LysM effector Ecp6 of the fungal tomato pathogen Cladosporium fulvum reveals a novel mechanism for chitin binding, mediated by intrachain LysM dimerization, leading to a chitin-binding groove that is deeply buried in the effector protein. This composite binding site involves two of the three LysMs of Ecp6 and mediates chitin binding with ultra-high (pM) affinity. Intriguingly, the remaining singular LysM domain of Ecp6 binds chitin with low micromolar affinity but can nevertheless still perturb chitin-triggered immunity. Conceivably, the perturbation by this LysM domain is not established through chitin sequestration but possibly through interference with the host immune receptor complex. DOI:http://dx.doi.org/10.7554/eLife.00790.001.