Structure and mechanism of Helicobacter pylori fucosyltransferase. A basis for lipopolysaccharide variation and inhibitor design.

@article{Sun2007StructureAM,
  title={Structure and mechanism of Helicobacter pylori fucosyltransferase. A basis for lipopolysaccharide variation and inhibitor design.},
  author={H Sun and Sheng-Wei Lin and Tzu-Ping Ko and J Pan and C Liu and Chun-Nan Lin and Andrew H-J Wang and C. A. Lin},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 13},
  pages={9973-82}
}
Helicobacter pylori alpha1,3-fucosyltransferase (FucT) is involved in catalysis to produce the Lewis x trisaccharide, the major component of the bacteria's lipopolysaccharides, which has been suggested to mimic the surface sugars in gastric epithelium to escape host immune surveillance. We report here three x-ray crystal structures of FucT, including the FucT.GDP-fucose and FucT.GDP complexes. The protein structure is typical of the glycosyltransferase-B family despite little sequence homology… CONTINUE READING
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