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PDBsum entry 4z3j
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Sugar binding protein
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PDB id
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4z3j
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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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Crystal structure of the lectin domain of papg from e. Coli bi47 in space group p1
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Structure:
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Papg, lectin domain. Chain: a, b, c, d. Fragment: residues 20-216. Engineered: yes
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Source:
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Escherichia coli. Organism_taxid: 562. Gene: g801_04654, g801_04690. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: 494.
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Resolution:
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2.50Å
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R-factor:
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0.221
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R-free:
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0.246
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Authors:
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R.P.Jakob,G.Navarra,P.Zihlmann,K.Stangier,R.C.Preston,S.Rabbani, T.Maier,B.Ernst
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Key ref:
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G.Navarra
et al.
(2017).
Carbohydrate-Lectin Interactions: An Unexpected Contribution to Affinity.
Chembiochem,
18,
539-544.
PubMed id:
DOI:
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Date:
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31-Mar-15
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Release date:
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13-Apr-16
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PROCHECK
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Headers
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References
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A0A182DW20
(A0A182DW20_ECOLX) -
PapG, lectin domain from Escherichia coli
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Seq:
Struc:
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198 a.a.
196 a.a.
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Key: |
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Secondary structure |
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CATH domain |
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DOI no:
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Chembiochem
18:539-544
(2017)
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PubMed id:
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Carbohydrate-Lectin Interactions: An Unexpected Contribution to Affinity.
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G.Navarra,
P.Zihlmann,
R.P.Jakob,
K.Stangier,
R.C.Preston,
S.Rabbani,
M.Smiesko,
B.Wagner,
T.Maier,
B.Ernst.
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ABSTRACT
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Uropathogenic E. coli exploit PapG-II adhesin for infecting host cells of the
kidney; the expression of PapG-II at the tip of bacterial pili correlates with
the onset of pyelonephritis in humans, a potentially life-threatening condition.
It was envisaged that blocking PapG-II (and thus bacterial adhesion) would
provide a viable therapeutic alternative to conventional antibiotic treatment.
In our search for potent PapG-II antagonists, we observed an increase in
affinity when tetrasaccharide 1, the natural ligand of PapG-II in human kidneys,
was elongated to hexasaccharide 2, even though the additional Siaα(2-3)Gal
extension is not in direct contact with the lectin. ITC studies suggest that the
increased affinity results from partial desolvation of nonbinding regions of the
hexasaccharide; this is ultimately responsible for perturbation of the outer
hydration layers. Our results are in agreement with previous observations and
suggest a general mechanism for modulating carbohydrate-protein interactions
based on nonbinding regions of the ligand.
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