2tpl

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[[Image:2tpl.gif|left|200px]]<br />
 
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<applet load="2tpl" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2tpl, resolution 2.5&Aring;" />
 
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'''TYROSINE PHENOL-LYASE FROM CITROBACTER INTERMEDIUS COMPLEX WITH 3-(4'-HYDROXYPHENYL)PROPIONIC ACID, PYRIDOXAL-5'-PHOSPHATE AND CS+ ION'''<br />
 
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==Overview==
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==TYROSINE PHENOL-LYASE FROM CITROBACTER INTERMEDIUS COMPLEX WITH 3-(4'-HYDROXYPHENYL)PROPIONIC ACID, PYRIDOXAL-5'-PHOSPHATE AND CS+ ION==
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The X-ray structure of tyrosine phenol-lyase (TPL) complexed with a, substrate analog, 3-(4'-hydroxyphenyl)propionic acid, shows that Arg 381, is located in the substrate binding site, with the side-chain NH1 4.1 A, from the 4'-OH of the analog. The structure has been deduced at 2.5 A, resolution using crystals that belong to the P2(1)2(1)2 space group with a, = 135.07 A, b = 143.91 A, and c = 59.80 A. To evaluate the role of Arg 381, in TPL catalysis, we prepared mutant proteins replacing arginine with, alanine (R381A), with isoleucine (R381I), and with valine (R381V). The, beta-elimination activity of R381A TPL has been reduced by 10(-4)-fold, compared to wild type, whereas R381I and R381V TPL exhibit no detectable, beta-elimination activity with L-tyrosine as substrate. However, R381A, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9174368 (full description)]]
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<StructureSection load='2tpl' size='340' side='right'caption='[[2tpl]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2tpl]] 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=2TPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TPL 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]] 2.5&#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=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=HPP:HYDROXYPHENYL+PROPIONIC+ACID'>HPP</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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=2tpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tpl OCA], [https://pdbe.org/2tpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2tpl RCSB], [https://www.ebi.ac.uk/pdbsum/2tpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2tpl 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/2tpl_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=2tpl ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2TPL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]] with CS and HPP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Sites: CS and PLP. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2TPL OCA]].
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*[[Tyrosinase 3D structures|Tyrosinase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity., Sundararaju B, Antson AA, Phillips RS, Demidkina TV, Barbolina MV, Gollnick P, Dodson GG, Wilson KS, Biochemistry. 1997 May 27;36(21):6502-10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9174368 9174368]
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[[Category: Citrobacter freundii]]
[[Category: Citrobacter freundii]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Tyrosine phenol-lyase]]
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[[Category: Antson AA]]
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[[Category: Antson, A.A.]]
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[[Category: Demidkina TV]]
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[[Category: Demidkina, T.V.]]
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[[Category: Wilson KS]]
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[[Category: Wilson, K.S.]]
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[[Category: CS]]
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[[Category: HPP]]
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[[Category: lyase]]
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[[Category: plp-dependent enzyme]]
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[[Category: pyridoxal phosphate]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:36:41 2007''
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Current revision

TYROSINE PHENOL-LYASE FROM CITROBACTER INTERMEDIUS COMPLEX WITH 3-(4'-HYDROXYPHENYL)PROPIONIC ACID, PYRIDOXAL-5'-PHOSPHATE AND CS+ ION

PDB ID 2tpl

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