Domain separation in the activation of glycogen phosphorylase a

E. J. Goldsmith, S. R. Sprang, R. Hamlin, N. H. Xuong, R. J. Fletterick

Research output: Contribution to journalArticlepeer-review

51 Scopus citations


The crystal structure of glycogen phosphorylase a complexed with its substrates, orthophosphate and maltopentaose, has been determined and refined at a resolution of 2.8 angstroms. With oligosaccaride bound at the glycogen storage site, the phosphate ion binds at the catalytic site and causes the regulatory and catalytic domains to separate with the loss of stabilizing interactions between them. Homotropic cooperativity between the active sites of the allosteric dimer results from rearrangements in isologous contacts between symmetry-related helices in the subunit interface. The conformational changes in the core of the interface are correlated with those observed on covalent activation by phosphorylation at Ser14 (phosphorylase b→a).

Original languageEnglish
Pages (from-to)528-532
Number of pages5
Issue number4917
StatePublished - 1989


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