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<StructureSection load='1tpl' size='340' side='right'caption='[[1tpl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1tpl' size='340' side='right'caption='[[1tpl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1tpl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"citrobacter_intermedium"_werkman_and_gillen_1932 "citrobacter intermedium" werkman and gillen 1932]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TPL FirstGlance]. <br>
<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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</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>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tpl OCA], [http://pdbe.org/1tpl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tpl RCSB], [http://www.ebi.ac.uk/pdbsum/1tpl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tpl ProSAT]</span></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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPL_CITFR TPL_CITFR]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:7916622<ref>PMID:7916622</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1tpl" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Tyrosinase|Tyrosinase]]
*[[Tyrosinase 3D structures|Tyrosinase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Citrobacter intermedium werkman and gillen 1932]]
[[Category: Citrobacter intermedius]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Tyrosine phenol-lyase]]
[[Category: Antson A]]
[[Category: Antson, A]]
[[Category: Dauter Z]]
[[Category: Dauter, Z]]
[[Category: Demidkina T]]
[[Category: Demidkina, T]]
[[Category: Harutyunyan E]]
[[Category: Harutyunyan, E]]
[[Category: Wilson K]]
[[Category: Wilson, K]]
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