Useful Information
Human tyrosine aminotransferase
Click on the iSee icon to launch an enhanced annotation with interactive 3D representations and animated transitions. Please note that a web plugin (activeICM) is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available.
PDB Code 3DYD Target Class AA metabolic enzymes Target TAT Alias TAT Disease Area/Function Date Deposited Jul 27 2008 Authors
About this structure
Pyridoxal phosphate-dependent tyrosine aminotransferase, or tyrosine transaminase (TAT; EC: 2.6.1.5), a mitochondrial protein present in the liver, catalyzes the conversion of L-tyrosine into p-hydroxyphenylpyruvate. This reaction is required in tyrosine and phenylalanine metabolism. Mutations in the TAT gene cause tyrosinemia (type II, Richner-Hanhart syndrome), a rare disorder accompanied by major skin and corneal lesions and, in severe cases, mental and somatic retardation.Here, the crystal structure of human TAT (amino acids 41 – 444) is presented in complex with PLP at a resolution of 2.3 Å. The structure shows the putative physiological homodimer. As its bacterial and protist orthologs and the related aspartate aminotransferases, the enzyme consists of two lobes, the larger cofactor binding domain and the smaller substrate binding domain. The large domain, made up of the central part of the sequence, is an α/β/α sandwich with a mostly parallel, 7-stranded β-sheet in the order 1675432. The small domain, made up of the N- and C-terminal sequence, is a 3-stranded antiparallel β-sheet that rests on the large domain loops surrounding the cofactor binding site and that is covered by three α-helices on its outer face.
