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  • Title: Crystal structure of the aromatic-amino-acid aminotransferase from Streptococcus mutans.
    Author: Cong X, Li X, Li S.
    Journal: Acta Crystallogr F Struct Biol Commun; 2019 Feb 01; 75(Pt 2):141-146. PubMed ID: 30713166.
    Abstract:
    Streptococcus mutans, a facultatively aerobic and Gram-positive bacterium, is the primary causative agent of dental caries and contributes to the multispecies biofilm known as dental plaque. In this study, the aromatic-amino-acid aminotransferase from Streptococcus mutans (SmAroAT) was recombinantly expressed in Escherichia coli. An effective purification protocol was established. The recombinant protein was crystallized using the hanging-drop vapor-diffusion method with PEG 3350 as the primary precipitant. The crystal structure of SmAroAT was solved at 2.2 Å resolution by the molecular-replacement method. Structural analysis indicated that the proteins of the aromatic-amino-acid aminotransferase family have conserved structural elements that might play a role in substrate binding. These results may help in obtaining a better understanding of the catabolism and biosynthesis of aromatic amino acids.
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