Unknown

Dataset Information

0

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


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.

SUBMITTER: Cong X 

PROVIDER: S-EPMC6360443 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Cong Xuzhen X   Li Xiaolu X   Li Shentao S  

Acta crystallographica. Section F, Structural biology communications 20190124 Pt 2


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  ...[more]

Similar Datasets

| S-EPMC9290597 | biostudies-literature
| S-EPMC6279937 | biostudies-literature
| S-EPMC6626674 | biostudies-literature
| S-EPMC1152940 | biostudies-other
| S-EPMC7755246 | biostudies-literature
2020-06-09 | GSE152021 | GEO
| S-EPMC2897675 | biostudies-literature
| S-EPMC4822980 | biostudies-literature
| S-EPMC2446784 | biostudies-literature
| S-EPMC2685563 | biostudies-literature