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[[Image:3tat.jpg|left|200px]]


{{Structure
==TYROSINE AMINOTRANSFERASE FROM E. COLI==
|PDB= 3tat |SIZE=350|CAPTION= <scene name='initialview01'>3tat</scene>, resolution 3.5&Aring;
<StructureSection load='3tat' size='340' side='right'caption='[[3tat]], [[Resolution|resolution]] 3.50&Aring;' 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>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
<table><tr><td colspan='2'>[[3tat]] is a 6 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TAT FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tat OCA], [https://pdbe.org/3tat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tat RCSB], [https://www.ebi.ac.uk/pdbsum/3tat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tat ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tat OCA], [http://www.ebi.ac.uk/pdbsum/3tat PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3tat RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/TYRB_ECOLI TYRB_ECOLI]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ta/3tat_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3tat ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''TYROSINE AMINOTRANSFERASE FROM E. COLI'''
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<ref>PMID:10417420</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3tat" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==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:[http://www.ncbi.nlm.nih.gov/pubmed/10417420 10417420]
[[Category: Aromatic-amino-acid transaminase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ko, T P.]]
[[Category: Ko TP]]
[[Category: Tsai, H.]]
[[Category: Tsai H]]
[[Category: Wu, S P.]]
[[Category: Wu SP]]
[[Category: Yang, W Z.]]
[[Category: Yang WZ]]
[[Category: Yuan, H S.]]
[[Category: Yuan HS]]
[[Category: aminotransferase]]
[[Category: aromatic substrate]]
[[Category: plp enzyme]]
 
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Retrieved from "https://proteopedia.org/3tat"