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

0553202 - BC 2022 RIV GB eng J - Journal Article
Gajdos, L. - Blakeley, M. - Kumar, Atul - Wimmerová, M. - Haertlein, M. - Forsyth, V. T. - Imberty, A. - Devos, J.
Visualization of hydrogen atoms in a perdeuterated lectin-fucose complex reveals key details of protein-carbohydrate interactions.
Structure. Roč. 29, č. 9 (2021), č. článku 1003-1013.e4. ISSN 0969-2126. E-ISSN 1878-4186
Institutional support: RVO:60077344
Keywords : d-xylose isomerase * x-ray structures * concanavalin-a * neutron structure * data-collection * dynamics * binding * crystallography * photorhabdus * diffraction
OECD category: Biochemistry and molecular biology
Impact factor: 5.871, year: 2021
Method of publishing: Open access
https://www.sciencedirect.com/science/article/pii/S0969212621000769?via%3Dihub

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.
Permanent Link: http://hdl.handle.net/11104/0328203