3TAT

TYROSINE AMINOTRANSFERASE FROM E. COLI

3TAT の概要

• エントリーDOI: 10.2210/pdb3tat/pdb
• 分子名称: TYROSINE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE (2 entities in total)
• 機能のキーワード: aminotransferase, aromatic substrates, plp enzyme
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P04693
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 262960.76

構造登録者

Ko, T.P.,Yang, W.Z.,Wu, S.P.,Tsai, H.,Yuan, H.S. (登録日: 1998-08-12, 公開日: 1999-08-12, 最終更新日: 2023-08-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.5 Å)