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Crystallographic studies on the activity of glycogen phosphorylase b

Nature volume 274, pages 433437 (03 August 1978) | Download Citation

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Abstract

High resolution studies on the crystal structure of glycogen phosphorylase b have identified the catalytic site to which the substrate glucose-1-phosphate binds strongly with some local conformational changes. The site is situated 8 Å (phosphate-to-phosphate distance) from pyridoxal phosphate, an essential cofactor of all glycogen phosphorylases. The catalytic site is 33 Å from the site in the N-terminal portion of the molecule to which adenine nucleotides bind. In contrast to phosphorylase a (the active form of the enzyme which is phosphorylated at Ser 14), the positions of the first 19 residues of phosphorylase b are not well defined.

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  1. Laboratory of Molecular Biophysics, South Parks Road, Oxford, UK

    • I. T. Weber
    • , L. N. Johnson
    • , K. S. Wilson
    • , D. G. R. Yeates
    • , D. L. Wild
    •  & J. A. Jenkins

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https://doi.org/10.1038/274433a0

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