What are the Structural Features of Phosphoglycerate Kinase?
PGK is a monomeric enzyme with a two-domain structure, each domain contributing to the binding of either 1,3-bisphosphoglycerate or ADP. The N-terminal domain binds to 1,3-bisphosphoglycerate, while the C-terminal domain binds to ADP. The hinge region between these two domains allows for the necessary conformational changes during the catalytic cycle. This structural arrangement ensures that the substrates are optimally positioned to facilitate the transfer of the phosphate group.
