3TAT

TYROSINE AMINOTRANSFERASE FROM E. COLI

Summary for 3TAT

• Entry DOI: 10.2210/pdb3tat/pdb
• Descriptor: TYROSINE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE (2 entities in total)
• Functional Keywords: aminotransferase, aromatic substrates, plp enzyme
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P04693
• Total number of polymer chains: 6
• Total formula weight: 262960.76

Authors

Ko, T.P.,Yang, W.Z.,Wu, S.P.,Tsai, H.,Yuan, H.S. (deposition date: 1998-08-12, release date: 1999-08-12, Last modification date: 2023-08-09)

Primary citation

Ko, T.P.,Wu, S.P.,Yang, W.Z.,Tsai, H.,Yuan, H.S.
Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase.
Acta Crystallogr.,Sect.D, 55:1474-1477, 1999

PubMed 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.

PubMed: 10417420
DOI: 10.1107/S0907444999006630

Experimental method

X-RAY DIFFRACTION (3.5 Å)