Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase.
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.
Ko
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TP
Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan 11529, Taiwan.
Wu
S P
SP
Yang
W Z
WZ
Tsai
H
H
Yuan
H S
HS
D000818:Animals; D001665:Binding Sites; D002645:Chickens; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D004563:Electrochemistry; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D011487:Protein Conformation; D011732:Pyridoxal Phosphate / Q000737:chemistry; D013045:Species Specificity; D014444:Tyrosine Transaminase / Q000737:chemistry* / Q000302:isolation & purification*
D011732:Pyridoxal Phosphate; D014444:Tyrosine Transaminase