3tat

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[[Image:3tat.jpg|left|200px]]<br /><applet load="3tat" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:3tat.jpg|left|200px]]
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caption="3tat, resolution 3.5&Aring;" />
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'''TYROSINE AMINOTRANSFERASE FROM E. COLI'''<br />
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{{Structure
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|PDB= 3tat |SIZE=350|CAPTION= <scene name='initialview01'>3tat</scene>, resolution 3.5&Aring;
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|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>
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>
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|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]
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|GENE=
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}}
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'''TYROSINE AMINOTRANSFERASE FROM E. COLI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=PLP:'>PLP</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=3TAT OCA].
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3TAT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TAT OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10417420 10417420]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10417420 10417420]
[[Category: Aromatic-amino-acid transaminase]]
[[Category: Aromatic-amino-acid transaminase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: PLP]]
[[Category: PLP]]
[[Category: aminotransferase]]
[[Category: aminotransferase]]
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[[Category: aromatic substrates]]
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[[Category: aromatic substrate]]
[[Category: plp enzyme]]
[[Category: plp enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:11:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:07:19 2008''

Revision as of 17:07, 20 March 2008

Image:3tat.jpg


PDB ID 3tat

Drag the structure with the mouse to rotate
, 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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