7PRG

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

This is a non-PDB format compatible entry.

Summary for 7PRG

• Entry DOI: 10.2210/pdb7prg/pdb
• Descriptor: Fucose-binding lectin, CALCIUM ION, alpha-L-fucopyranose, ... (5 entities in total)
• Functional Keywords: lectin, complex, sugar binding protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 4
• Total formula weight: 48536.93

Authors

Gajdos, L.,Blakeley, M.P.,Haertlein, M.,Forsyth, T.V.,Devos, J.M.,Imberty, A. (deposition date: 2021-09-21, release date: 2022-01-12, Last modification date: 2024-05-01)

Primary citation

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

Experimental method

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