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Crystallographic studies on the activity of glycogen phosphorylase b

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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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Authors and Affiliations

  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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  1. I. T. Weber
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  2. L. N. Johnson
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  3. K. S. Wilson
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  4. D. G. R. Yeates
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  5. D. L. Wild
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Weber, I., Johnson, L., Wilson, K. et al. Crystallographic studies on the activity of glycogen phosphorylase b. Nature 274, 433–437 (1978). https://doi.org/10.1038/274433a0

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