8B97

N-terminal beta-trefoil lectin domain of the Laccaria bicolor lectin in complex with N-acetyl-lactosamine

Summary for 8B97

• Entry DOI: 10.2210/pdb8b97/pdb
• Related PRD ID: PRD_900019
• Descriptor: Beta-trefoil domain of the LBL lectin, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: atomic resolution, beta-trefoil, fruiting-body lectin, sugar-specificity, sugar binding protein
• Biological source: Laccaria bicolor S238N-H53
• Total number of polymer chains: 1
• Total formula weight: 18782.59

Authors

Acebron, I.,Campanero-Rhodes, M.A.,Solis, D.,Menendez, M.,Garcia, C.,Lillo, M.P.,Mancheno, J.M. (deposition date: 2022-10-05, release date: 2023-02-22, Last modification date: 2024-02-07)

Primary citation

Acebron, I.,Campanero-Rhodes, M.A.,Solis, D.,Menendez, M.,Garcia, C.,Lillo, M.P.,Mancheno, J.M.
Atomic crystal structure and sugar specificity of a beta-trefoil lectin domain from the ectomycorrhizal basidiomycete Laccaria bicolor.
Int.J.Biol.Macromol., 233:123507-123507, 2023

PubMed Abstract: Lectins from fruiting bodies are a diverse group of sugar-binding proteins from mushrooms that face the biologically relevant challenge of discriminating self- from non-self carbohydrate structures, therefore providing a basis for an innate defence system. Such a system entails both detection and destruction of invaders and/or feeders, and in contrast to more complex organisms with immense immune systems, these two functions normally rely on multitasking lectins, namely, lectins with different functional modules. Here, we present a novel fungal lectin, LBL, from the basidiomycete Laccaria bicolor. Using a diverse set of biophysical techniques, we unveil the fine details of the sugar-binding specificity of the N-terminal β-trefoil of LBL (LBL), whose structure has been determined at the highest resolution so far reported for such a fold. LBL binds complex poly-N-Acetyllactosamine polysaccharides and also robust LBL binding to Caenorhabditis elegans and Drosophila melanogaster cellular extracts was detected in microarray assays, with a seeming preference for the fruit fly adult and pupa stages over the larva stage. Prediction of the structure of the C-terminal part of LBL with AlphaFold reveals a tandem repeat of two structurally almost identical domains of around 110 amino acids each, despite sharing low sequence conservation.

PubMed: 36754262
DOI: 10.1016/j.ijbiomac.2023.123507

Experimental method

X-RAY DIFFRACTION (0.97 Å)