3tat: Difference between revisions
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==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== | ||
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[[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'' | ||
