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[[Image:2ez2.gif|left|200px]]


{{Structure
==Apo tyrosine phenol-lyase from Citrobacter freundii at pH 8.0==
|PDB= 2ez2 |SIZE=350|CAPTION= <scene name='initialview01'>2ez2</scene>, resolution 1.850&Aring;
<StructureSection load='2ez2' size='340' side='right'caption='[[2ez2]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
<table><tr><td colspan='2'>[[2ez2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EZ2 FirstGlance]. <br>
|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
|GENE= TPL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=546 Citrobacter freundii])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ez2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ez2 OCA], [https://pdbe.org/2ez2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ez2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ez2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ez2 ProSAT]</span></td></tr>
|RELATEDENTRY=[[2ez1|2EZ1]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ez2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ez2 OCA], [http://www.ebi.ac.uk/pdbsum/2ez2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ez2 RCSB]</span>
== 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/ez/2ez2_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=2ez2 ConSurf].
<div style="clear:both"></div>


'''Apo tyrosine phenol-lyase from Citrobacter freundii at pH 8.0'''
==See Also==
 
*[[Tyrosinase 3D structures|Tyrosinase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Tyrosine phenol-lyase, a tetrameric pyridoxal 5'-phosphate dependent enzyme, catalyzes the reversible hydrolytic cleavage of L-tyrosine to phenol and ammonium pyruvate. Here we describe the crystal structure of the Citrobacter freundii holoenzyme at 1.9 A resolution. The structure reveals a network of protein interactions with the cofactor, pyridoxal 5'-phosphate, and details of coordination of the catalytically important K+ ion. We also present the structure of the apoenzyme at 1.85 A resolution. Both structures were determined using crystals grown at pH 8.0, which is close to the pH of the maximal enzymatic activity (8.2). Comparison of the apoenzyme structure with the one previously determined at pH 6.0 reveals significant differences. The data suggest that the decrease of the enzymatic activity at pH 6.0 may be caused by conformational changes in the active site residues Tyr71, Tyr291, and Arg381 and in the monovalent cation binding residue Glu69. Moreover, at pH 8.0 we observe two different active site conformations: open, which was characterized before, and closed, which is observed for the first time in beta-eliminating lyases. In the closed conformation a significant part of the small domain undergoes an extraordinary motion of up to 12 A toward the large domain, closing the active site cleft and bringing the catalytically important Arg381 and Phe448 into the active site. The closed conformation allows rationalization of the results of previous mutational studies and suggests that the observed active site closure is critical for the course of the enzymatic reaction and for the enzyme's specificity toward its physiological substrate. Finally, the closed conformation allows us to model keto(imino)quinonoid, the key transition intermediate.
 
==About this Structure==
2EZ2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EZ2 OCA].
 
==Reference==
Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions., Milic D, Matkovic-Calogovic D, Demidkina TV, Kulikova VV, Sinitzina NI, Antson AA, Biochemistry. 2006 Jun 20;45(24):7544-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16768450 16768450]
[[Category: Citrobacter freundii]]
[[Category: Citrobacter freundii]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Tyrosine phenol-lyase]]
[[Category: Antson AA]]
[[Category: Antson, A A.]]
[[Category: Demidkina TV]]
[[Category: Demidkina, T V.]]
[[Category: Matkovic-Calogovic D]]
[[Category: Matkovic-Calogovic, D.]]
[[Category: Milic D]]
[[Category: Milic, D.]]
[[Category: domain closure]]
[[Category: lyase]]
[[Category: plp-dependent enzyme]]
[[Category: pyridoxal-5'-phosphate]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:55:42 2008''

Latest revision as of 12:20, 14 February 2024

Apo tyrosine phenol-lyase from Citrobacter freundii at pH 8.0Apo tyrosine phenol-lyase from Citrobacter freundii at pH 8.0

Structural highlights

2ez2 is a 2 chain structure with sequence from Citrobacter freundii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TPL_CITFR

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2ez2, resolution 1.85Å

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OCA
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