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The allosteric transition of glycogen phosphorylase

Nature volume 340, pages 609–616 (1989)Cite this article

Abstract

The crystal structure of R-state glycogen phosphorylase b has been determined at 2.9 Å 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 con-formational change that switches these two helices into the R-state conformation.

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Authors and Affiliations

  1. Laboratory of Molecular Biophysics, University of Oxford, The Rex Richards Building, South Parks Road, Oxford, 0X1 3QU, UK

    D. Barford & L. N. Johnson

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  1. D. Barford
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  2. L. N. Johnson
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Barford, D., Johnson, L. The allosteric transition of glycogen phosphorylase. Nature 340, 609–616 (1989). https://doi.org/10.1038/340609a0

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