3tat
From Proteopedia
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|PDB= 3tat |SIZE=350|CAPTION= <scene name='initialview01'>3tat</scene>, resolution 3.5Å | |PDB= 3tat |SIZE=350|CAPTION= <scene name='initialview01'>3tat</scene>, resolution 3.5Å | ||
|SITE= <scene name='pdbsite=PBA:Covalently+Linked+w.+Plp+500.+Site+Site_identifier+Pbb+S+...'>PBA</scene>, <scene name='pdbsite=PBB:Covalently+Linked+w.+Plp+500.+Site+Site_identifier+Pbc+S+...'>PBB</scene>, <scene name='pdbsite=PBC:Covalently+Linked+w.+Plp+500.+Site+Site_identifier+Pbd+S+...'>PBC</scene>, <scene name='pdbsite=PBD:Covalently+Linked+w.+Plp+500.+Site+Site_identifier+Pbe+S+...'>PBD</scene>, <scene name='pdbsite=PBE:Covalently+Linked+w.+Plp+500.+Site+Site_identifier+Pbf+S+...'>PBE</scene> and <scene name='pdbsite=PBF:Covalently+Linked+w.+Plp+500'>PBF</scene> | |SITE= <scene name='pdbsite=PBA:Covalently+Linked+w.+Plp+500.+Site+Site_identifier+Pbb+S+...'>PBA</scene>, <scene name='pdbsite=PBB:Covalently+Linked+w.+Plp+500.+Site+Site_identifier+Pbc+S+...'>PBB</scene>, <scene name='pdbsite=PBC:Covalently+Linked+w.+Plp+500.+Site+Site_identifier+Pbd+S+...'>PBC</scene>, <scene name='pdbsite=PBD:Covalently+Linked+w.+Plp+500.+Site+Site_identifier+Pbe+S+...'>PBD</scene>, <scene name='pdbsite=PBE:Covalently+Linked+w.+Plp+500.+Site+Site_identifier+Pbf+S+...'>PBE</scene> and <scene name='pdbsite=PBF:Covalently+Linked+w.+Plp+500'>PBF</scene> | ||
| - | |LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5 | + | |LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> |
|ACTIVITY= [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] | |ACTIVITY= [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] | ||
|GENE= | |GENE= | ||
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[[Category: plp enzyme]] | [[Category: plp enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 16:03:28 2008'' |
Revision as of 14:03, 23 March 2008
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| , resolution 3.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , and | ||||||
| Ligands: | |||||||
| Activity: | Aromatic-amino-acid transaminase, with EC number 2.6.1.57 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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