PMID:10417420

Citation	Ko, TP, Wu, SP, Yang, WZ, Tsai, H and Yuan, HS (1999) Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase. Acta Crystallogr. D Biol. Crystallogr. 55:1474-7
Abstract	Tyrosine aminotransferase catalyzes transamination for both dicarboxylic and aromatic amino-acid substrates. The substrate-free Escherichia coli tyrosine aminotransferase (eTAT) bound with the cofactor pyridoxal 5'-phosphate (PLP) was crystallized in the trigonal space group P3(2). A low-resolution crystal structure of eTAT was determined by molecular-replacement methods. The overall folding of eTAT resembles that of the aspartate aminotransferases, with the two identical subunits forming a dimer in which each monomer binds a PLP molecule via a covalent bond linked to the epsilon-NH(2) group of Lys258. Comparison of the structure of eTAT with those of the open, half-open or closed form of chicken or E. coli aspartate aminotransferases shows the eTAT structure to be in the open conformation.
Links	PubMed
Keywords	Animals; Binding Sites; Chickens; Crystallization; Crystallography, X-Ray; Dimerization; Electrochemistry; Escherichia coli/enzymology; Models, Molecular; Protein Conformation; Pyridoxal Phosphate/chemistry; Species Specificity; Tyrosine Transaminase/chemistry; Tyrosine Transaminase/isolation & purification
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