The effect of substrates on the inter-domain interactions of the hinge-bending enzyme 3-phosphoglycerate kinase.
A hinge-bending mechanism has been proposed for phosphoglycerate kinase, in which the two domains bend about the connecting 'waist' region. In partially denaturing concentrations of guanidinium chloride the substrate 3-phosphoglycerate stabilises one domain against denaturation and destabilises the other. The reduction of mutual stabilisation of the two domains on binding substrate indicates a freeing of the hinge to allow the protein to take up other states rather than a directive mechanism. The stabilisation of both domains at higher concentrations of ATP at which the enzyme is inhibited supports this mechanism.
D000255:Adenosine Triphosphate; D001665:Binding Sites; D005988:Glyceric Acids; D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology; D010735:Phosphoglycerate Kinase / Q000378:metabolism*; D011487:Protein Conformation / Q000187:drug effects; D011489:Protein Denaturation / Q000187:drug effects; D012441:Saccharomyces cerevisiae / Q000201:enzymology
D005988:Glyceric Acids; D006146:Guanidines; C005156:3-phosphoglycerate; D000255:Adenosine Triphosphate; D010735:Phosphoglycerate Kinase; D019791:Guanidine