4my5

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4my5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4my5 OCA], [https://pdbe.org/4my5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4my5 RCSB], [https://www.ebi.ac.uk/pdbsum/4my5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4my5 ProSAT]</span></td></tr>

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== 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<ref>PMID:30713166</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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