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


{{Structure
==D-Tyr tRNATyr deacylase from Escherichia coli==
|PDB= 1jke |SIZE=350|CAPTION= <scene name='initialview01'>1jke</scene>, resolution 1.55&Aring;
<StructureSection load='1jke' size='340' side='right'caption='[[1jke]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
<table><tr><td colspan='2'>[[1jke]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JKE FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
|GENE= YIHZ or B3887 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1jke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jke OCA], [https://pdbe.org/1jke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jke RCSB], [https://www.ebi.ac.uk/pdbsum/1jke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jke ProSAT]</span></td></tr>
 
</table>
'''D-Tyr tRNATyr deacylase from Escherichia coli'''
== Function ==
 
[https://www.uniprot.org/uniprot/DTD_ECOLI DTD_ECOLI] Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr). Could be a defense mechanism against a harmful effect of D-tyrosine. Can also cleave D-aspartyl-tRNA(Asp) and D-tryptophanyl-tRNA(Trp).
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
Cell growth inhibition by several d-amino acids can be explained by an in vivo production of d-aminoacyl-tRNA molecules. Escherichia coli and yeast cells express an enzyme, d-Tyr-tRNA(Tyr) deacylase, capable of recycling such d-aminoacyl-tRNA molecules into free tRNA and d-amino acid. Accordingly, upon inactivation of the genes of the above deacylases, the toxicity of d-amino acids increases. Orthologs of the deacylase are found in many cells. In this study, the crystallographic structure of dimeric E. coli d-Tyr-tRNA(Tyr) deacylase at 1.55 A resolution is reported. The structure corresponds to a beta-barrel closed on one side by a beta-sheet lid. This barrel results from the assembly of the two subunits. Analysis of the structure in relation with sequence homologies in the orthologous family suggests the location of the active sites at the carboxy end of the beta-strands. The solved structure markedly differs from those of all other documented tRNA-dependent hydrolases.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jk/1jke_consurf.spt"</scriptWhenChecked>
1JKE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JKE OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolases., Ferri-Fioni ML, Schmitt E, Soutourina J, Plateau P, Mechulam Y, Blanquet S, J Biol Chem. 2001 Dec 14;276(50):47285-90. Epub 2001 Sep 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11568181 11568181]
</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=1jke ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Blanquet, S.]]
[[Category: Blanquet S]]
[[Category: Ferri-Fioni, M L.]]
[[Category: Ferri-Fioni ML]]
[[Category: Mechulam, Y.]]
[[Category: Mechulam Y]]
[[Category: Plateau, P.]]
[[Category: Plateau P]]
[[Category: Schmitt, E.]]
[[Category: Schmitt E]]
[[Category: Soutourina, J.]]
[[Category: Soutourina J]]
[[Category: ZN]]
[[Category: beta-alpha-barrel]]
 
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