3tat
From Proteopedia
| Line 5: | Line 5: | ||
==Overview== | ==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 . | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 3TAT is a | + | 3TAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PLP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aromatic-amino-acid_transaminase Aromatic-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.57 2.6.1.57] Structure known Active Sites: PBA, PBB, PBC, PBD, PBE and PBF. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3TAT OCA]. |
==Reference== | ==Reference== | ||
| Line 25: | Line 25: | ||
[[Category: plp enzyme]] | [[Category: plp enzyme]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:24:29 2007'' |
Revision as of 12:19, 5 November 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 conformation.
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 Mon Nov 5 14:24:29 2007
