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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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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<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 ==
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 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 <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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==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://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:11:31 2008''
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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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