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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1988 Jun;85(12):4205–4208. doi: 10.1073/pnas.85.12.4205

Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase.

J E Gouaux 1, W N Lipscomb 1
PMCID: PMC280395  PMID: 3380787

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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