Survey of the folding pathway of a two-domain protein phosphoglycerate kinase.

Abstract The role of structural domains as folding units in the folding process which generates an active enzyme, is considered through several studies on phosphoglycerate kinase, a two-domain enzyme which catalyzes the first step of ATP production in glycolysis. The folding pathway was found to be a complex multi-step process, the C-terminal domain being more stable folding first. Inactive species originating from an intermediate in the folding pathway have been identified. Isolated domains recently obtained using genetic engineering are under investigation in our laboratory; this might probably allow to understand the way by which the N-terminal domain reaches its final native conformation and interacts with the other domain.