Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase.
The three-dimensional structure of the ternary complex of carbamoyl phosphate, succinate, and aspartate carbamoyltransferase (EC 2.1.3.2) has been determined to 2.6-A resolution. The binding of the phosphate of carbamoyl phosphate is similar to the binding of the phosphonate of N-(phosphonoacetyl)-L-aspartate (PALA); interacting with the carboxylates of succinate are some of the same residues that interact with the carboxylates of PALA. The amino group of carbamoyl phosphate donates hydrogen bonds to the main-chain carbonyls of residues Pro-266 and Leu-267 and the side-chain carbonyl of Gln-137. In comparing the structure of the active sites in the PALA-enzyme complex to the active sites in the carbamoyl phosphate-succinate-enzyme complex, we find that they are similar.
Gouaux
J E
JE
Gibbs Chemical Laboratory, Harvard University, Cambridge, MA 02138.
Lipscomb
W N
WN
D001221:Aspartate Carbamoyltransferase / Q000378:metabolism*; D001665:Binding Sites; D002219:Carbamates / Q000378:metabolism*; D002221:Carbamyl Phosphate / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D013386:Succinates / Q000378:metabolism*; D019802:Succinic Acid; D014961:X-Ray Diffraction
D002219:Carbamates; D013386:Succinates; D002221:Carbamyl Phosphate; D019802:Succinic Acid; D001221:Aspartate Carbamoyltransferase