The allosteric transition of glycogen phosphorylase

Nature. 1989 Aug 24;340(6235):609-16. doi: 10.1038/340609a0.


The crystal structure of R-state glycogen phosphorylase b has been determined at 2.9 A resolution. A comparison of T-state and R-state structures of the enzyme explains its cooperative behaviour on ligand binding and the allosteric regulation of its activity. Communication between catalytic sites of the dimer is provided by a change in packing geometry of two helices linking each site with the subunit interface. Activation by AMP or by phosphorylation results in a quaternary conformational change that switches these two helices into the R-state conformation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allosteric Regulation*
  • Animals
  • Binding Sites
  • Catalysis
  • Computer Simulation
  • Hydrogen Bonding
  • Muscles / enzymology
  • Phosphorylases / physiology*
  • Protein Conformation
  • Rabbits
  • Structure-Activity Relationship


  • Phosphorylases