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  • Title: Structural consequences of a one atom mutation on aspartate transcarbamylase from E. coli.
    Author: Cherfils J, Sweet RM, Middleton SA, Kantrowitz ER, Tauc P, Vachette P.
    Journal: FEBS Lett; 1989 Apr 24; 247(2):361-6. PubMed ID: 2653863.
    Abstract:
    Tyr-240 of the catalytic chain of aspartate transcarbamylase from E. coli has been substituted by Phe using site-directed mutagenesis. The regulatory mechanisms of the mutant enzyme have been shown to be slightly less effective than the wild-type enzyme. A study of the structural consequences of the mutation using solution X-ray scattering and computer simulations is reported here. No significant change from the wild-type enzyme is detectable in the quaternary structure. Simulations suggest that the only effect of the mutation is an increased mobility of the mutated side chain.
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