与天冬氨酸氨甲酰基转移酶结合的氨甲酰磷酸和琥珀酸的三维结构。
Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase.
作者信息
Gouaux J E, Lipscomb W N
机构信息
Gibbs Chemical Laboratory, Harvard University, Cambridge, MA 02138.
出版信息
Proc Natl Acad Sci U S A. 1988 Jun;85(12):4205-8. doi: 10.1073/pnas.85.12.4205.
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.
摘要
氨基甲酰磷酸、琥珀酸和天冬氨酸氨基甲酰转移酶（EC 2.1.3.2）三元复合物的三维结构已确定至2.6埃分辨率。氨基甲酰磷酸中磷酸基团的结合类似于N-（膦酰基乙酰基）-L-天冬氨酸（PALA）中膦酸酯的结合；与琥珀酸羧基相互作用的一些残基与PALA的羧基相互作用相同。氨基甲酰磷酸的氨基向残基Pro-266和Leu-267的主链羰基以及Gln-137的侧链羰基提供氢键。在比较PALA-酶复合物中活性位点的结构与氨基甲酰磷酸-琥珀酸-酶复合物中活性位点的结构时，我们发现它们相似。
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