4MY5

Crystal structure of the aromatic amino acid aminotransferase from Streptococcus mutants

Summary for 4MY5

• Entry DOI: 10.2210/pdb4my5/pdb
• Descriptor: Putative amino acid aminotransferase (2 entities in total)
• Functional Keywords: smaroat, type 1 plp-dependent aminotransferases, amino acid metabolism, oral infectious diseases, transferase
• Biological source: Streptococcus mutans
• Total number of polymer chains: 4
• Total formula weight: 174648.55

Authors

Cong, X.,Li, X.,Ge, J.,Feng, Y.,Feng, X.,Li, S. (deposition date: 2013-09-27, release date: 2014-10-01, Last modification date: 2024-03-20)

Primary citation

Cong, X.,Li, X.,Li, S.
Crystal structure of the aromatic-amino-acid aminotransferase from Streptococcus mutans.
Acta Crystallogr.,Sect.F, 75:141-146, 2019

PubMed 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.

PubMed: 30713166
DOI: 10.1107/S2053230X18018472

Experimental method

X-RAY DIFFRACTION (2.194 Å)