4my5

Publication Abstract from PubMed

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 A 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.

Crystal structure of the aromatic-amino-acid aminotransferase from Streptococcus mutans.,Cong X, Li X, Li S Acta Crystallogr F Struct Biol Commun. 2019 Feb 1;75(Pt 2):141-146. doi:, 10.1107/S2053230X18018472. Epub 2019 Jan 24. PMID:30713166^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.