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- W2410022364 abstract "Mutation pAR5 replaces residues 145'-153' at the C terminus of the regulatory (r) chains of Escherichia coli ATCase by a new sequence of six residues. The mutated enzyme has been shown to lack substrate cooperativity and inhibition by CTP. Solution X-ray scattering curves demonstrate that, in the absence of ligands, its structure is intermediate between the T form and the R form. In the presence of N-phosphonacetyl-L-aspartate, the mutant is similar to the wild type. An examination of the crystal structure of unligated ATCase reveals that the mutated site is at an interface between r and catalytic (c) chains, which exists only in the T allosteric form. A computer simulation by energy minimization suggests that the pAR5 mutation destabilizes this interface and induces minor changes in the tertiary structure of r chains. The resulting lower stability of the T form explains the loss of substrate cooperativity. The lack of allosteric inhibition may be related to a new electrostatic interaction made in mutant r chains between the C-terminal carboxylate and a lysine residue of the allosteric domain." @default.
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- W2410022364 date "1987-09-01" @default.
- W2410022364 modified "2023-09-23" @default.
- W2410022364 title "The pAR5 mutation and the allosteric mechanism of Escherichia coli aspartate carbamoyltransferase." @default.
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- W2410022364 doi "https://doi.org/10.1002/j.1460-2075.1987.tb02581.x" @default.
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