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Protein Science, Vol 3, Issue 10 1726-1730, Copyright © 1994 by Cold Spring Harbor Laboratory Press

INVITED PAPER, SPECIAL SECTION IN HONOR OF MAX PERUTZ

Electrostatic effects in the control of glycogen phosphorylase by phosphorylation

L. N. JOHNSON and D. BARFORD
Laboratory of Molecular Biophysics, University of Oxford, Rex Richards Building, South Parks Road, Oxford OX1 3QU, United Kingdom

Electrostatic effects are important in the initial activation mechanism of glycogen phosphorylase by phosphorylation. Analysis of the electrostatic surface potential of glycogen phosphorylase with the program GRASP shows that in the unphosphorylated state, the N-terminal 20 residues, which include a number of basic amino acids, are located close to a position on the surface of the molecule that is highly acidic. Upon phosphorylation by phosphorylase kinase at Ser 14, the N-terminal residues change their position and conformation so that the Ser-P is directed away from the acidic patch and to an intersubunit site where 2 arginines bind the phosphate. This recognition site is created through tertiary and quaternary structural changes that accompany the activation mechanism.
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Copyright © 1994 by The Protein Society.