Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase.
Open Access
- 1 June 1988
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 85 (12) , 4205-4208
- https://doi.org/10.1073/pnas.85.12.4205
Abstract
The three-dimensional strucutre of the ternary complex of carbamoyl phosphate, succinate, and aspartate carbamoyltransferase (EC 2.1.3.2) has been determined to 2.6-.ANG. 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 succinates 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.This publication has 18 references indexed in Scilit:
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