The active site of the Escherichia coli glycogen synthase is similar to the active site of retaining GT-B glycosyltransferases.

@article{Yep2004TheAS,
  title={The active site of the Escherichia coli glycogen synthase is similar to the active site of retaining GT-B glycosyltransferases.},
  author={Alejandra Yep and Miguel Angel Ballicora and Jack Preiss},
  journal={Biochemical and biophysical research communications},
  year={2004},
  volume={316 3},
  pages={960-6}
}
Bacterial glycogen synthases transfer a glucosyl unit, retaining the anomeric configuration, from ADP-glucose to the non-reducing end of glycogen. We modeled the Escherichia coli glycogen synthase based on three glycosyltransferases with a GT-B fold. Comparison between the model and the structure of the active site of crystallized retaining GT-B glycosyltransferases identified conserved residues with the same topology. To confirm the importance of these residues predicted by the model, we… CONTINUE READING