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Träfflista för sökning "WFRF:(Brosens E.) srt2:(2003-2004)"

Sökning: WFRF:(Brosens E.) > (2003-2004)

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1.
  • Buts, L, et al. (författare)
  • Solving the phase problem for carbohydrate-binding proteins using selenium derivatives of their ligands : a case study involving the bacterial F17-G adhesin
  • 2003
  • Ingår i: Acta Crystallographica Section D. - : International Union of Crystallography (IUCr). - 2059-7983. ; 59:6, s. 1012-1015
  • Tidskriftsartikel (refereegranskat)abstract
    • The Escherichia coli adhesin F17-G is a carbohydrate-binding protein that allows the bacterium to attach to the intestinal epithelium of young ruminants. The structure of the 17 kDa lectin domain of F17-G was determined using the anomalous dispersion signal of a selenium-containing analogue of the monosaccharide ligand N-acetyl-D-glucosamine in which the anomeric oxygen was replaced by an Se atom. A three-wavelength MAD data set yielded good experimental phases to 2.6 Angstrom resolution. The structure was refined to 1.75 Angstrom resolution and was used to solve the structures of the ligand-free protein and the F17-G-N-acetyl-D-glucosamine complex. This selenium-carbohydrate phasing method could be of general use for determining the structures of carbohydrate-binding proteins.
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2.
  • Buts, L, et al. (författare)
  • The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine
  • 2003
  • Ingår i: Molecular Microbiology. - : Wiley. - 0950-382X .- 1365-2958. ; 49:3, s. 705-715
  • Tidskriftsartikel (refereegranskat)abstract
    • The F17-G adhesin at the tip of flexible F17 fimbriae of enterotoxigenic Escherichia coli mediates binding to N-acetyl-beta-D-glucosamine-presenting receptors on the microvilli of the intestinal epithelium of ruminants. We report the 1.7 Angstrom resolution crystal structure of the lectin domain of F17-G, both free and in complex with N-acetylglucosamine. The monosaccharide is bound on the side of the ellipsoid-shaped protein in a conserved site around which all natural variations of F17-G are clustered. A model is proposed for the interaction between F17-fimbriated E. coli and microvilli with enhanced affinity compared with the binding constant we determined for F17-G binding to N-acetylglucosamine (0.85 mM(-1)). Unexpectedly, the F17-G structure reveals that the lectin domains of the F17-G, PapGII and FimH fimbrial adhesins all share the immunoglobulin-like fold of the structural components (pilins) of their fimbriae, despite lack of any sequence identity. Fold comparisons with pilin and chaperone structures of the chaperone/usher pathway highlight the central role of the C-terminal beta-strand G of the immunoglobulin-like fold and provides new insights into pilus assembly, function and adhesion.
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  • Resultat 1-2 av 2
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refereegranskat (2)
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Oscarson, S (2)
Buts, L (2)
Loris, R (2)
De Genst, E (2)
Lahmann, Martina, Do ... (2)
Messens, J (2)
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Brosens, E (2)
Wyns, L (2)
De Greve, H (2)
Bouckaert, J (2)
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2003 (2)

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