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6ZFC

Fucose-binding lectin from Burkholderia ambifaria (BamBL) in complex with a fucosyl derivative

Summary for 6ZFC
Entry DOI10.2210/pdb6zfc/pdb
Descriptorbacterial lectin from Burkholderia ambifaria, 2-[(2~{S},3~{S},4~{R},4~{a}~{S},10~{a}~{S})-2-methyl-3,4-bis(oxidanyl)-3,4,4~{a},10~{a}-tetrahydro-2~{H}-pyrano[2,3-b][1,4]benzoxathiin-7-yl]-~{N}-(3-oxidanylpropyl)ethanamide (3 entities in total)
Functional Keywordsfucose-binding lectin, glycomimetics, sugar binding protein
Biological sourceBurkholderia ambifaria (strain ATCC BAA-244 / AMMD)
Total number of polymer chains6
Total formula weight60756.19
Authors
Kuhaudomlarp, S.,Gillon, E.,Fragai, M.,Cerofolini, L.,Giuntini, S.,Denis, M.,Santarsia, S.,Valori, C.,Dondoni, A.,Fallarini, S.,Lombardi, G.,Nativi, C.,Imberty, A. (deposition date: 2020-06-17, release date: 2020-10-28, Last modification date: 2024-01-24)
Primary citationKuhaudomlarp, S.,Cerofolini, L.,Santarsia, S.,Gillon, E.,Fallarini, S.,Lombardi, G.,Denis, M.,Giuntini, S.,Valori, C.,Fragai, M.,Imberty, A.,Dondoni, A.,Nativi, C.
Fucosylated ubiquitin and orthogonally glycosylated mutant A28C: conceptually new ligands for Burkholderia ambifaria lectin (BambL).
Chem Sci, 11:12662-12670, 2020
Cited by
PubMed Abstract: Two orthogonal, metal free click reactions, enabled to glycosylate ubiquitin and its mutant A28C forming two protein scaffolds with high affinity for BambL, a lectin from the human pathogen . A new fucoside analogue, with high affinity with BambL, firstly synthetized and co-crystallized with the protein target, provided the insights for sugar determinants grafting onto ubiquitin. Three ubiquitin-based glycosides were thus assembled. , presented several copies of the fucoside analogue, with proper geometry for multivalent effect; , displayed one thio-rhamnose, known for its ability to tuning the immunological response; finally, , included both multiple fucoside analogs and the rhamnose residue. and ligands proved high affinity for BambL and unprecedented immune modulatory properties towards macrophages activation.
PubMed: 34094460
DOI: 10.1039/d0sc03741a
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

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数据于2025-06-18公开中

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