7prg | pdb_00007prg

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

spinqualitylabelsall models 7prg, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7prg is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, FUC, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Neutron crystallography reveals mechanisms used by Pseudomonas aeruginosa for host-cell binding.,Gajdos L, Blakeley MP, Haertlein M, Forsyth VT, Devos JM, Imberty A Nat Commun. 2022 Jan 11;13(1):194. doi: 10.1038/s41467-021-27871-8. PMID:35017516 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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