ArticleActa crystallographica. Section F, Structural biology communications2019
Crystal structure of the aromatic-amino-acid aminotransferase from Streptococcus mutans.
Article in Acta crystallographica. Section F, Structural biology communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- The Dynamic Change in Aromatic Compounds and Their Relationship withMetabolites · 2023Article
- Methylation-based epigenetic studies and gene integration analysis of preeclampsia.Annals of translational medicine · 2022Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
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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