 |
PDBsum entry 4b9h
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Sugar binding protein
|
PDB id
|
|
|
|
4b9h
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Fungal effector ecp6 outcompetes host immune receptor for chitin binding through intrachain lysm dimerization.
|
|
|
Authors
|
|
A.Sánchez-Vallet,
R.Saleem-Batcha,
A.Kombrink,
G.Hansen,
D.J.Valkenburg,
B.P.Thomma,
J.R.Mesters.
|
|
|
Ref.
|
|
Elife, 2013,
2,
e00790.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Conserved fungal lysm effector ecp6 prevents chitin-Triggered immunity in plants.
|
|
|
Authors
|
|
R.De jonge,
H.P.Van esse,
A.Kombrink,
T.Shinya,
Y.Desaki,
R.Bours,
S.Van der krol,
N.Shibuya,
M.H.Joosten,
B.P.Thomma.
|
|
|
Ref.
|
|
Science, 2010,
329,
953-955.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
