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PDBsum entry 6zfc
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Sugar binding protein
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PDB id
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6zfc
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PDB id:
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| Name: |
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Sugar binding protein
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Title:
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Fucose-binding lectin from burkholderia ambifaria (bambl) in complex with a fucosyl derivative
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Structure:
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Bacterial lectin from burkholderia ambifaria. Chain: a, b, c, d, e, f. Engineered: yes
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Source:
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Burkholderia ambifaria (strain atcc baa-244 / ammd). Organism_taxid: 339670. Gene: bamb_5415. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008
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Resolution:
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1.65Å
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R-factor:
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0.178
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R-free:
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0.209
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Authors:
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S.Kuhaudomlarp,E.Gillon,M.Fragai,L.Cerofolini,S.Giuntini,M.Denis, S.Santarsia,C.Valori,A.Dondoni,S.Fallarini,G.Lombardi,C.Nativi, A.Imberty
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Key ref:
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S.Kuhaudomlarp
et al.
(2020).
Fucosylated ubiquitin and orthogonally glycosylated mutant A28C: conceptually new ligands for Burkholderia ambifaria lectin (BambL).
Chem Sci,
11,
12662-12670.
PubMed id:
DOI:
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Date:
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17-Jun-20
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Release date:
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28-Oct-20
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PROCHECK
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Headers
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References
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Q0B4G1
(Q0B4G1_BURCM) -
Fucose-binding lectin protein from Burkholderia ambifaria (strain ATCC BAA-244 / DSM 16087 / CCUG 44356 / LMG 19182 / AMMD)
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Seq:
Struc:
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87 a.a.
87 a.a.
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DOI no:
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Chem Sci
11:12662-12670
(2020)
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PubMed id:
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Fucosylated ubiquitin and orthogonally glycosylated mutant A28C: conceptually new ligands for Burkholderia ambifaria lectin (BambL).
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S.Kuhaudomlarp,
L.Cerofolini,
S.Santarsia,
E.Gillon,
S.Fallarini,
G.Lombardi,
M.Denis,
S.Giuntini,
C.Valori,
M.Fragai,
A.Imberty,
A.Dondoni,
C.Nativi.
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ABSTRACT
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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 Burkholderia ambifaria. 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.
Fuc-Ub, presented several copies of the fucoside analogue, with proper
geometry for multivalent effect; Rha-A28C, displayed one thio-rhamnose,
known for its ability to tuning the immunological response; finally,
Fuc-Rha-A28C, included both multiple fucoside analogs and the rhamnose
residue. Fuc-Ub and Fuc-Rha-A28C ligands proved high affinity for
BambL and unprecedented immune modulatory properties towards macrophages
activation.
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Links
