Crystal structure of the aromatic-amino-acid aminotransferase from Streptococcus mutans

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.

Source: Acta Crystallographica Section F - January 24, 2019 Category: Biochemistry Authors: Cong, X. Li, X. Li, S. Tags: Streptococcus mutans dental caries dental plaque infective endocarditis aromatic-amino-acid aminotransferase crystallization structure determination research communications Source Type: research