7B7C

Room temperature X-ray structure of perdeuterated PLL lectin in complex with L-fucose

7B7C の概要

• エントリーDOI: 10.2210/pdb7b7c/pdb
• 分子名称: PLL lectin, beta-L-fucopyranose, alpha-L-fucopyranose, ... (4 entities in total)
• 機能のキーワード: complex, propeller, sugar binding protein
• 由来する生物種: Photorhabdus laumondii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42929.89

構造登録者

Gajdos, L.,Blakeley, M.P.,Kumar, A.,Wimmerova, M.,Haertlein, M.,Forsyth, V.T.,Imberty, A.,Devos, J.M. (登録日: 2020-12-10, 公開日: 2021-03-17, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.55 Å)