Allostery through Covalent Modification

 

Glycogen phosphorylase catalyzes the release of a glucose from glycogen, while transfering a phosphate group to generate Glucose-1-phosphate. The enzyme is a homodimer, colored red and blue. The phosphorylation (green) of Ser14, colored yellow, determines whether the enzyme is active or inactive. Phosphorylation causes a change in how the two monomers interact and opens up the catalytic site. The active sites are at a distance, and are marked by a cofactor PLP colored cyan.

This enzyme is also regulated by allosteric effector molecules, including inhibitors ATP and Glucose-6-phosphate, and activator AMP.


The allosteric transition of glycogen phosphorylase.
Barford D, Johnson LN.
Nature. 1989 Aug 24;340(6235):609-16. (PubMed)

9gpb (PDB)