3tat
From Proteopedia
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| - | [[Image:3tat. | + | [[Image:3tat.jpg|left|200px]]<br /><applet load="3tat" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="3tat" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="3tat, resolution 3.5Å" /> | caption="3tat, resolution 3.5Å" /> | ||
'''TYROSINE AMINOTRANSFERASE FROM E. COLI'''<br /> | '''TYROSINE AMINOTRANSFERASE FROM E. COLI'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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] | + | 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] Known structural/functional Sites: <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>. 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 Tue Dec 18 20:42:27 2007'' |
Revision as of 18:32, 18 December 2007
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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 Known structural/functional Sites: , , , , and . 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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