3tat

From Proteopedia

Revision as of 15:42, 30 October 2007

TYROSINE AMINOTRANSFERASE FROM E. COLI

Overview

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 ... [(full description)]

About this Structure

3TAT is a [Single protein] structure of sequence from [Escherichia coli] with PLP as [ligand]. Active as [Aromatic-amino-acid transaminase], with EC number [2.6.1.57]. Structure known Active Sites: PBA, PBB, PBC, PBD, PBE and PBF. Full crystallographic information is available from [OCA].

Reference

Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase., Ko TP, Wu SP, Yang WZ, Tsai H, Yuan HS, Acta Crystallogr D Biol Crystallogr. 1999 Aug;55(Pt 8):1474-7. PMID:10417420

Page seeded by OCA on Tue Oct 30 17:46:53 2007