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[[Image:1tpl.gif|left|200px]]


{{Structure
==THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE==
|PDB= 1tpl |SIZE=350|CAPTION= <scene name='initialview01'>1tpl</scene>, resolution 2.3&Aring;
<StructureSection load='1tpl' size='340' side='right'caption='[[1tpl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
<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>
|ACTIVITY= [http://en.wikipedia.org/wiki/Tyrosine_phenol-lyase Tyrosine phenol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.2 4.1.99.2]  
</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>
|GENE=  
<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>
}}
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPL_CITFR TPL_CITFR]
== 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/tp/1tpl_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=1tpl ConSurf].
<div style="clear:both"></div>


'''THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE'''
==See Also==
 
*[[Tyrosinase 3D structures|Tyrosinase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Citrobacter intermedius]]
 
[[Category: Large Structures]]
==About this Structure==
[[Category: Antson A]]
1TPL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TPL OCA].
[[Category: Dauter Z]]
 
[[Category: Demidkina T]]
==Reference==
[[Category: Harutyunyan E]]
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]
[[Category: Wilson K]]
[[Category: Single protein]]
[[Category: Tyrosine phenol-lyase]]
[[Category: Antson, A.]]
[[Category: Dauter, Z.]]
[[Category: Demidkina, T.]]
[[Category: Harutyunyan, E.]]
[[Category: Wilson, K.]]
[[Category: SO4]]
[[Category: lyase(carbon-carbon)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:21:27 2008''

Latest revision as of 08:41, 14 February 2024

THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE

1tpl, resolution 2.30Å

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