4my5

Crystal structure of the aromatic amino acid aminotransferase from Streptococcus mutantsCrystal structure of the aromatic amino acid aminotransferase from Streptococcus mutants

Structural highlights 4my5 is a 4 chain structure with sequence from Streptococcus mutans UA159. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8DWM1_STRMU 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 4my5, resolution 2.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image