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.
Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan 11529, Taiwan.
T P
TP
Ko
S P
SP
Wu
W Z
WZ
Yang
H
H
Tsai
H S
HS
Yuan
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