6FHY
Photorhabdus asymbiotica lectin (PHL) in complex with synthetic C-fucoside
Summary for 6FHY
| Entry DOI | 10.2210/pdb6fhy/pdb |
| Descriptor | Lectin PHL, (2~{S},3~{S},4~{R},5~{S},6~{S})-2-[[(2~{S},4~{R},6~{R})-2-(hydroxymethyl)-6-oxidanyl-oxan-4-yl]methyl]-6-methyl-oxane-3,4,5-triol, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | lectin, seven-bladed beta-propeller, sugar binding protein, c-fucoside, 4.6. 4(s)-2-hydroxy-1-phenylethyl 2, 3, 4-trideoxy-3-c-[(a-l- fucopyranosyl)methyl]-b-d-threo-hexopyranoside |
| Biological source | Photorhabdus asymbiotica |
| Total number of polymer chains | 2 |
| Total formula weight | 84137.74 |
| Authors | Houser, J.,Jancarikova, G.,Wimmerova, M. (deposition date: 2018-01-16, release date: 2019-01-30, Last modification date: 2024-11-20) |
| Primary citation | Paulikova, G.,Houser, J.,Kasakova, M.,Oroszova, B.,Bertolotti, B.,Parkan, K.,Moravcova, J.,Wimmerova, M. Fucosylated inhibitors of recently identified bangle lectin from Photorhabdus asymbiotica. Sci Rep, 9:14904-14904, 2019 Cited by PubMed Abstract: A recently described bangle lectin (PHL) from the bacterium Photorhabdus asymbiotica was identified as a mainly fucose-binding protein that could play an important role in the host-pathogen interaction and in the modulation of host immune response. Structural studies showed that PHL is a homo-dimer that contains up to seven L-fucose-specific binding sites per monomer. For these reasons, potential ligands of the PHL lectin: α-L-fucopyranosyl-containing mono-, di-, tetra-, hexa- and dodecavalent ligands were tested. Two types of polyvalent structures were investigated - calix[4]arenes and dendrimers. The shared feature of all these structures was a C-glycosidic bond instead of the more common but physiologically unstable O-glycosidic bond. The inhibition potential of the tested structures was assessed using different techniques - hemagglutination, surface plasmon resonance, isothermal titration calorimetry, and cell cross-linking. All the ligands proved to be better than free L-fucose. The most active hexavalent dendrimer exhibited affinity three orders of magnitude higher than that of standard L-fucose. To determine the binding mode of some ligands, crystal complex PHL/fucosides 2 - 4 were prepared and studied using X-ray crystallography. The electron density in complexes proved the presence of the compounds in 6 out of 7 fucose-binding sites. PubMed: 31624296DOI: 10.1038/s41598-019-51357-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
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