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Review the three-dimensional crystal structures and conformational changes of glycogen phosphorylase to explain how allosteric ligands and covalent modifications regulate enzymatic activity.

November 1, 1982Accounts of Chemical Research

Glycogen phosphorylase structures and function

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Authors

RFRobert J. FletterickUniversity of California, San Francisco SSStephen R. SprangCenter for Environmental Health

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Implication

Review describes the crystallographic structure and regulatory mechanisms of glycogen phosphorylase, highlighting how conformational shifts govern cellular glycogen breakdown.

Key Points

Review the three-dimensional crystal structures and conformational changes of glycogen phosphorylase to explain how allosteric ligands and covalent modifications regulate enzymatic activity.
Synthesis of structural data obtained from high-resolution X-ray crystallography of glycogen phosphorylase.
Comparative analysis of structural transitions between active and inactive conformations in response to allosteric effectors and reversible phosphorylation.
X-ray crystallographic analyses show that glycogen phosphorylase transitions between active and inactive states via coordinated quaternary structural rearrangements at the dimer interface.
Enzyme activation is mediated cooperatively by phosphorylation of Ser-14 or binding of allosteric activators such as AMP, which reposition catalytic residues relative to the pyridoxal phosphate cofactor.

Cite This Study

Fletterick et al. (1982) studied this question.

synapsesocial.com/papers/6a7162f55671bbf00bc2e13d https://doi.org/10.1021/ar00083a004

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Implication

Review describes the crystallographic structure and regulatory mechanisms of glycogen phosphorylase, highlighting how conformational shifts govern cellular glycogen breakdown.

Glycogen phosphorylase structures and function

Discussion

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Implication

Key Points

Cite This Study

Glycogen phosphorylase structures and function

Discussion

Member takes

Implication

Key Points

Cite This Study

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