1y2q

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Current revision (13:37, 13 March 2024) (edit) (undo)
 
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<StructureSection load='1y2q' size='340' side='right'caption='[[1y2q]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='1y2q' size='340' side='right'caption='[[1y2q]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1y2q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"pyrococcus_abyssi"_erauso_et_al._1993 "pyrococcus abyssi" erauso et al. 1993]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y2Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y2Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1y2q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y2Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y2Q FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1y2r|1y2r]]</div></td></tr>
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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]] 1.95&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">thrS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29292 "Pyrococcus abyssi" Erauso et al. 1993])</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=1y2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y2q OCA], [https://pdbe.org/1y2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y2q RCSB], [https://www.ebi.ac.uk/pdbsum/1y2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y2q ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1y2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y2q OCA], [http://pdbe.org/1y2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y2q RCSB], [http://www.ebi.ac.uk/pdbsum/1y2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y2q ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYT_PYRAB SYT_PYRAB]
== 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=1y2q 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=1y2q ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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We report the crystal structure of an archaea-specific editing domain of threonyl-tRNA synthetase that reveals a marked structural similarity to D-amino acid deacylases found in eubacteria and eukaryotes. The domain can bind D-amino acids despite a low sequence identity to other D-amino acid deacylases. These results together indicate the presence of these deacylases in all three kingdoms of life. This underlines an important role they may have played in enforcing homochirality during translation.
 
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A D-amino acid editing module coupled to the translational apparatus in archaea.,Dwivedi S, Kruparani SP, Sankaranarayanan R Nat Struct Mol Biol. 2005 Jun;12(6):556-7. Epub 2005 May 22. PMID:15908961<ref>PMID:15908961</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1y2q" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Pyrococcus abyssi erauso et al. 1993]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Threonine--tRNA ligase]]
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[[Category: Pyrococcus abyssi]]
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[[Category: Dwivedi, S]]
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[[Category: Dwivedi S]]
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[[Category: Kruparani, S P]]
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[[Category: Kruparani SP]]
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[[Category: Sankaranarayanan, R]]
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[[Category: Sankaranarayanan R]]
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[[Category: Beta-alpha-beta fold]]
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[[Category: Editing domain]]
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[[Category: Ligase]]
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[[Category: Trna-synthetase]]
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Current revision

Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi

PDB ID 1y2q

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