3tat

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[[Image:3tat.jpg|left|200px]]<br /><applet load="3tat" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="3tat, resolution 3.5&Aring;" />
 
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'''TYROSINE AMINOTRANSFERASE FROM E. COLI'''<br />
 
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==Overview==
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==TYROSINE AMINOTRANSFERASE FROM E. COLI==
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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.
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<StructureSection load='3tat' size='340' side='right'caption='[[3tat]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TYRB_ECOLI TYRB_ECOLI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ta/3tat_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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:10417420<ref>PMID:10417420</ref>
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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 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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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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</div>
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[[Category: Aromatic-amino-acid transaminase]]
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<div class="pdbe-citations 3tat" style="background-color:#fffaf0;"></div>
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[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Ko, T.P.]]
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[[Category: Tsai, H.]]
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[[Category: Wu, S.P.]]
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[[Category: Yang, W.Z.]]
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[[Category: Yuan, H.S.]]
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[[Category: PLP]]
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[[Category: aminotransferase]]
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[[Category: aromatic substrates]]
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[[Category: plp enzyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 20:42:27 2007''
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==See Also==
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*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Ko TP]]
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[[Category: Tsai H]]
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[[Category: Wu SP]]
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[[Category: Yang WZ]]
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[[Category: Yuan HS]]

Current revision

TYROSINE AMINOTRANSFERASE FROM E. COLI

PDB ID 3tat

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