Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering. Signal transmission following effector binding.
The result of binding the effectors ATP and CTP to aspartate transcarbamylase was studied by X-ray solution scattering. Binding of substrate analogues produces a substantial change in the solution scattering curve, allowing us to monitor the proportion of the different quaternary structure states present in solution. In the initial solution this ratio was made roughly unity by adding either carbamyl phosphate and succinate, or N-(phosphonacetyl)-L-aspartate (PALA). ATP or CTP were then added, and their effect on the proportion of the different quaternary structure states was followed. When using carbamyl phosphate and succinate (weakly bound), ATP or CTP had a clear effect, as observed previously by monitoring the sedimentation rate (Changeux et al., 1968). However, when PALA (strongly bound) was used, the effect of CTP was very much smaller, and that of ATP was undetectable. This result supports the explanation by Tauc et al. (1982), that nucleotides act mostly through changing the affinity of the active sites for substrate, and only to a small extent by directly modifying the quaternary structure equilibrium in the case of CTP.
D000255:Adenosine Triphosphate; D000495:Allosteric Site; D001221:Aspartate Carbamoyltransferase; D001224:Aspartic Acid / Q000031:analogs & derivatives; D001665:Binding Sites; D002221:Carbamyl Phosphate; D003570:Cytidine Triphosphate; D004926:Escherichia coli / Q000201:enzymology; D046911:Macromolecular Substances; D010746:Phosphonoacetic Acid / Q000031:analogs & derivatives; D014965:X-Rays
D046911:Macromolecular Substances; D001224:Aspartic Acid; D002221:Carbamyl Phosphate; D003570:Cytidine Triphosphate; C013195:sparfosic acid; D000255:Adenosine Triphosphate; D001221:Aspartate Carbamoyltransferase; D010746:Phosphonoacetic Acid