2hra

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(New page: 200px<br /><applet load="2hra" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hra, resolution 1.90&Aring;" /> '''Crystal structures o...)
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[[Image:2hra.jpg|left|200px]]<br /><applet load="2hra" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2hra, resolution 1.90&Aring;" />
 
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'''Crystal structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA aminoacylation and nuclear export cofactor Arc1p reveal a novel function for an old fold'''<br />
 
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==Overview==
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==Crystal structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA aminoacylation and nuclear export cofactor Arc1p reveal a novel function for an old fold==
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Eukaryotic aminoacyl-tRNA synthetases (aaRS) frequently contain additional, appended domains that are absent from their prokaryotic counterparts which, mediate complex formation between eukaryotic aaRS and cofactors of, aminoacylation and translation. However, the structural basis of such, interactions has remained elusive. The heteromerization domain of yeast, glutamyl-tRNA synthetase (GluRS) has been cloned, expressed, purified and, crystallized in space group C222(1), with unit-cell parameters a = 52, b =, 107, c = 168 A. Phase information was obtained from multiple-wavelength, anomalous dispersion with selenomethionine to 2.5 A resolution and the, structure, comprising two monomers per asymmetric unit, was determined and, refined to 1.9 A resolution. The structure of the interacting domain of, its accessory protein Arc1p was determined and refined to 1.9 A resolution, in a crystal form containing 20 monomers organized in five tetramers per, asymmetric unit (space group C2, unit-cell parameters a = 222, b = 89, c =, 127 A, beta = 99.4 degrees ). Both domains adopt a GST-like fold, demonstrating a novel role for this fold as a protein-protein interaction, module.
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<StructureSection load='2hra' size='340' side='right'caption='[[2hra]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2hra]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HRA 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]] 1.9&#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=IOD:IODIDE+ION'>IOD</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=2hra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hra OCA], [https://pdbe.org/2hra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hra RCSB], [https://www.ebi.ac.uk/pdbsum/2hra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hra ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYEC_YEAST SYEC_YEAST] Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (By similarity).
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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/hr/2hra_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=2hra 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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2HRA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with IOD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutamate--tRNA_ligase Glutamate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.17 6.1.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HRA OCA].
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA-aminoacylation and nuclear-export cofactor Arc1p reveal a novel function for an old fold., Simader H, Hothorn M, Suck D, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1510-9. Epub 2006, Nov 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17139087 17139087]
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[[Category: Large Structures]]
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[[Category: Glutamate--tRNA ligase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Hothorn M]]
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[[Category: Hothorn, M.]]
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[[Category: Simader H]]
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[[Category: Simader, H.]]
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[[Category: Suck D]]
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[[Category: Suck, D.]]
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[[Category: IOD]]
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[[Category: gst-fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:55:38 2007''
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Current revision

Crystal structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA aminoacylation and nuclear export cofactor Arc1p reveal a novel function for an old fold

PDB ID 2hra

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