7BBI

Joint X-ray/neutron room temperature structure of H/D-exchanged PLL lectin

Summary for 7BBI

• Entry DOI: 10.2210/pdb7bbi/pdb
• Descriptor: PLL lectin (2 entities in total)
• Functional Keywords: propeller, sugar binding protein
• Biological source: Photorhabdus laumondii
• Total number of polymer chains: 1
• Total formula weight: 41944.95

Authors

Gajdos, L.,Blakeley, M.P.,Kumar, A.,Wimmerova, M.,Haertlein, M.,Forsyth, V.T.,Imberty, A.,Devos, J.M. (deposition date: 2020-12-17, release date: 2021-03-17, Last modification date: 2024-10-09)

Primary citation

Gajdos, L.,Blakeley, M.P.,Kumar, A.,Wimmerova, M.,Haertlein, M.,Forsyth, V.T.,Imberty, A.,Devos, J.M.
Visualization of hydrogen atoms in a perdeuterated lectin-fucose complex reveals key details of protein-carbohydrate interactions.
Structure, 29:1003-1013.e4, 2021

PubMed Abstract: 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 room temperature 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-π stacking interactions between fucose and the aromatic amino acids in the binding site.

PubMed: 33765407
DOI: 10.1016/j.str.2021.03.003

Experimental method

NEUTRON DIFFRACTION (2.2 Å)
X-RAY DIFFRACTION (1.7 Å)