1tpl

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[[Image:1tpl.gif|left|200px]]
 
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==THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE==
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The line below this paragraph, containing "STRUCTURE_1tpl", creates the "Structure Box" on the page.
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<StructureSection load='1tpl' size='340' side='right'caption='[[1tpl]], [[Resolution|resolution]] 2.30&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'>[[1tpl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_intermedius Citrobacter intermedius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TPL 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]] 2.3&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1tpl| PDB=1tpl | 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=1tpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tpl OCA], [https://pdbe.org/1tpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tpl RCSB], [https://www.ebi.ac.uk/pdbsum/1tpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tpl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TPL_CITFR TPL_CITFR]
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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/tp/1tpl_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=1tpl ConSurf].
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<div style="clear:both"></div>
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'''THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE'''
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==See Also==
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*[[Tyrosinase 3D structures|Tyrosinase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Tyrosine phenol-lyase (EC 4.1.99.2) from Citrobacter freundii has been cloned and the primary sequence deduced from the DNA sequence. From the BrCN digest of the NaBH4-reduced holoenzyme, five peptides were purified and sequenced. The amino acid sequences of the peptides agreed with the corresponding parts of the tyrosine phenol-lyase sequence obtained from the gene structure. K257 is the pyridoxal 5'-phosphate binding residue. Assisted by the sequence data, the crystal structure of apotyrosine phenol-lyase, a pyridoxal 5'-phosphate-dependent enzyme, has been refined to an R-factor of 16.2% at 2.3-A resolution using synchrotron radiation diffraction data. The tetrameric molecule has 222 symmetry, with one of the axes coincident with the crystallographic 2-fold symmetry axis of the crystal which belongs to the space group P2(1)2(1)2 with a = 76.0 A, b = 138.3 A, and c = 93.5 A. Each subunit comprises 14 alpha-helices and 16 beta-strands, which fold into a small and a large domain. The coenzyme-binding lysine residue is located at the interface between the large and small domains of one subunit and the large domain of a crystallographically related subunit. The fold of the large, pyridoxal 5'-phosphate binding domain and the location of the active site are similar to that found in aminotransferases. Most of the residues which participate in binding of pyridoxal 5'-phosphate in aminotransferases are conserved in the structure of tyrosine phenol-lyase. Two dimers of tyrosine phenol-lyase, each of which has a domain architecture similar to that found in aspartate aminotransferases, are bound together through a hydrophobic cluster in the center of the molecule and intertwined N-terminal arms.
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[[Category: Citrobacter intermedius]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Antson A]]
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1TPL is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TPL OCA].
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[[Category: Dauter Z]]
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[[Category: Demidkina T]]
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==Reference==
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[[Category: Harutyunyan E]]
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Three-dimensional structure of tyrosine phenol-lyase., Antson AA, Demidkina TV, Gollnick P, Dauter Z, von Tersch RL, Long J, Berezhnoy SN, Phillips RS, Harutyunyan EH, Wilson KS, Biochemistry. 1993 Apr 27;32(16):4195-206. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7916622 7916622]
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[[Category: Wilson K]]
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[[Category: Single protein]]
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[[Category: Tyrosine phenol-lyase]]
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[[Category: Antson, A.]]
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[[Category: Dauter, Z.]]
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[[Category: Demidkina, T.]]
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[[Category: Harutyunyan, E.]]
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[[Category: Wilson, K.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:13:33 2008''
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Current revision

THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE

PDB ID 1tpl

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