Visualization of hydrogen atoms in a perdeuterated lectin-fucose complex reveals key details of protein-carbohydrate interactions

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Authors

GAJDOŠ Lukáš BLAKELEY Matthew P. KUMAR Atul WIMMEROVÁ Michaela HAERTLEIN Michaela FORSYTH Trevor V. IMBERTY Anne DEVOS Juliette M.

Year of publication 2021
Type Article in Periodical
Magazine / Source Structure
MU Faculty or unit

Faculty of Science

Citation
Web https://www.sciencedirect.com/science/article/pii/S0969212621000769?via%3Dihub
Doi http://dx.doi.org/10.1016/j.str.2021.03.003
Keywords lectin; neutron diffraction; X-ray
Description Carbohydrate-binding proteins from pathogenic bacteria and fungi have been shown to be implicated in various pathological processes, where they interact with glycans present on the surface of the host cells. These interactions are part of the initial processes of infection of the host and are very important to study at the atomic level. Here, we report the roomtemperature neutron structures of PLL lectin from Photorhabdus laumondii in its apo form and in complex with deuterated L-fucose, which is, to our knowledge, the first neutron structure of a carbohydrate-binding protein in complex with a fully deuterated carbohydrate ligand. A detailed structural analysis of the lectin-carbohydrate interactions provides information on the hydrogen bond network, the role of water molecules, and the extent of the CH-pi stacking interactions between fucose and the aromatic amino acids in the binding site.
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