7PRG

Joint X-ray/neutron room temperature structure of perdeuterated LecB lectin in complex with perdeuterated fucose

これはPDB形式変換不可エントリーです。

7PRG の概要

• エントリーDOI: 10.2210/pdb7prg/pdb
• 分子名称: Fucose-binding lectin, CALCIUM ION, alpha-L-fucopyranose, ... (5 entities in total)
• 機能のキーワード: lectin, complex, sugar binding protein
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 48536.93

構造登録者

Gajdos, L.,Blakeley, M.P.,Haertlein, M.,Forsyth, T.V.,Devos, J.M.,Imberty, A. (登録日: 2021-09-21, 公開日: 2022-01-12, 最終更新日: 2024-05-01)

主引用文献

Gajdos, L.,Blakeley, M.P.,Haertlein, M.,Forsyth, V.T.,Devos, J.M.,Imberty, A.
Neutron crystallography reveals mechanisms used by Pseudomonas aeruginosa for host-cell binding.
Nat Commun, 13:194-194, 2022

PubMed Abstract: The opportunistic pathogen Pseudomonas aeruginosa, a major cause of nosocomial infections, uses carbohydrate-binding proteins (lectins) as part of its binding to host cells. The fucose-binding lectin, LecB, displays a unique carbohydrate-binding site that incorporates two closely located calcium ions bridging between the ligand and protein, providing specificity and unusually high affinity. Here, we investigate the mechanisms involved in binding based on neutron crystallography studies of a fully deuterated LecB/fucose/calcium complex. The neutron structure, which includes the positions of all the hydrogen atoms, reveals that the high affinity of binding may be related to the occurrence of a low-barrier hydrogen bond induced by the proximity of the two calcium ions, the presence of coordination rings between the sugar, calcium and LecB, and the dynamic behaviour of bridging water molecules at room temperature. These key structural details may assist in the design of anti-adhesive compounds to combat multi-resistance bacterial infections.

PubMed: 35017516
DOI: 10.1038/s41467-021-27871-8

実験手法

NEUTRON DIFFRACTION (1.9 Å)
X-RAY DIFFRACTION (1.85 Å)