Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase

@article{OReilly1997OligosaccharideSB,
  title={Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase},
  author={M A R O'Reilly and Kim A. Watson and Reinhard Schinzel and Dieter Palm and Louise N. Johnson},
  journal={Nature Structural Biology},
  year={1997},
  volume={4},
  pages={405-412}
}
The crystal structure of E. coli maltodextrin phosphorylase co-crystallized with an oligosaccharide has been solved at 3.0 Å resolution, providing the first structure of an oligosaccharide bound at the catalytic site of an α-glucan phosphorylase. An induced fit mechanism brings together two domains across the catalytic site tunnel. A stacking interaction between the glucosyl residue and the aromatic group of a tyrosine residue at a sub-site remote (8 Å) from the catalytic site provides a key… CONTINUE READING

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