Parallel evolution in two homologues of phosphorylase

@article{Rath1994ParallelEI,
  title={Parallel evolution in two homologues of phosphorylase},
  author={Virginia L. Rath and Robert Fletterick},
  journal={Nature Structural Biology},
  year={1994},
  volume={1},
  pages={681-690}
}
The structure of the unphosphorylated, inactive form of yeast glycogen phosphorylase has been determined to a resolution of 2.6 Å. The structure is similar to the phosphorylated, active form of muscle phosphorylase in the orientations of the subunits and catalytic residues, but resembles the inactive muscle enzyme in the closed, or substrate excluding, orientation of the two domains. Part of the unique yeast amino-terminal extension of 40 residues binds near the catalytic site of the second… CONTINUE READING