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3tat

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{{Seed}}
 
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[[Image:3tat.png|left|200px]]
 
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==TYROSINE AMINOTRANSFERASE FROM E. COLI==
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The line below this paragraph, containing "STRUCTURE_3tat", creates the "Structure Box" on the page.
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<StructureSection load='3tat' size='340' side='right'caption='[[3tat]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_3tat| PDB=3tat | SCENE= }}
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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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===TYROSINE AMINOTRANSFERASE FROM E. COLI===
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3tat" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10417420}}, adds the Publication Abstract to the page
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*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10417420 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10417420}}
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__TOC__
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</StructureSection>
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==About this Structure==
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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].
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==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://www.ncbi.nlm.nih.gov/pubmed/10417420 10417420]
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[[Category: Aromatic-amino-acid transaminase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ko, T P.]]
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[[Category: Ko TP]]
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[[Category: Tsai, H.]]
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[[Category: Tsai H]]
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[[Category: Wu, S P.]]
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[[Category: Wu SP]]
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[[Category: Yang, W Z.]]
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[[Category: Yang WZ]]
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[[Category: Yuan, H S.]]
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[[Category: Yuan HS]]
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[[Category: Aminotransferase]]
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[[Category: Aromatic substrate]]
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[[Category: Plp enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:08:15 2008''
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Current revision

TYROSINE AMINOTRANSFERASE FROM E. COLI

PDB ID 3tat

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