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1euy

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GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH A TRNA MUTANT AND AN ACTIVE SITE INHIBITOR

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Retrieved from "http://52.214.119.220/wiki/index.php/1euy"

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-[[Image:1euy.gif|left|200px]]<br /><applet load="1euy" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1euy, resolution 2.6&Aring;" />
-'''GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH A TRNA MUTANT AND AN ACTIVE SITE INHIBITOR'''<br />
-==Overview==
+==GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH A TRNA MUTANT AND AN ACTIVE SITE INHIBITOR==
-The position of the tertiary Levitt pair between nucleotides 15 and 48 in, the transfer RNA core region suggests a key role in stabilizing the, joining of the two helical domains, and in maintaining the relative, orientations of the D and variable loops. E. coli tRNA(Gln) possesses the, canonical Pu15-Py48 trans pairing at this position (G15-C48), while the, tRNA(Cys) species from this organism instead features an unusual G15-G48, pair. To explore the structural context dependence of a G15-G48 Levitt, pair, a number of tRNA(Gln) species containing G15-G48 were constructed, and evaluated as substrates for glutaminyl and cysteinyl-tRNA synthetases., The glutaminylation efficiencies of these mutant tRNAs are reduced by two, to tenfold compared with native tRNA(Gln), consistent with previous, findings that the tertiary core of this tRNA plays a role in GlnRS, recognition. Introduction of tRNA(Cys) identity nucleotides at the, acceptor and anticodon ends of tRNA(Gln) produced a tRNA substrate which, was efficiently aminoacylated by CysRS, even though the tertiary core, region of this species contains the tRNA(Gln) G15-C48 pair. Surprisingly, introduction of G15-G48 into the non-cognate tRNA(Gln) tertiary core then, significantly impairs CysRS recognition. By contrast, previous work has, shown that CysRS aminoacylates tRNA(Cys) core regions containing G15-G48, with much better efficiency than those with G15-C48. Therefore, tertiary, nucleotides surrounding the Levitt pair must significantly modulate the, efficiency of aminoacylation by CysRS. To explore the detailed nature of, the structural interdependence, crystal structures of two tRNA(Gln), mutants containing G15-G48 were determined bound to GlnRS. These, structures show that the larger purine ring of G48 is accommodated by, rotation into the syn position, with the N7 nitrogen serving as hydrogen, bond acceptor from several groups of G15. The G15-G48 conformations differ, significantly compared to that observed in the native tRNA(Cys) structure, bound to EF-Tu, further implicating an important role for surrounding, nucleotides in maintaining the integrity of the tertiary core and its, consequent ability to present crucial recognition determinants to, aminoacyl-tRNA synthetases.
+<StructureSection load='1euy' size='340' side='right'caption='[[1euy]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1euy]] is a 2 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=1EUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EUY FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=QSI:5-O-[N-(L-GLUTAMINYL)-SULFAMOYL]ADENOSINE'>QSI</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=1euy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1euy OCA], [https://pdbe.org/1euy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1euy RCSB], [https://www.ebi.ac.uk/pdbsum/1euy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1euy ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SYQ_ECOLI SYQ_ECOLI]
+== 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/eu/1euy_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=1euy ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-EUY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with QSI as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutamine--tRNA_ligase Glutamine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.18 6.1.1.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EUY OCA].
+*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
+*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
-==Reference==
+__TOC__
-Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases., Sherlin LD, Bullock TL, Newberry KJ, Lipman RS, Hou YM, Beijer B, Sproat BS, Perona JJ, J Mol Biol. 2000 Jun 2;299(2):431-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10860750 10860750]
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Glutamine--tRNA ligase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Beijer B]]
-[[Category: Beijer, B.]]
+[[Category: Bullock TL]]
-[[Category: Bullock, T.L.]]
+[[Category: Hou Y-M]]
-[[Category: Hou, Y.M.]]
+[[Category: Lipman RSA]]
-[[Category: Lipman, R.S.A.]]
+[[Category: Newberry KJ]]
-[[Category: Newberry, K.J.]]
+[[Category: Perona JJ]]
-[[Category: Perona, J.J.]]
+[[Category: Sherlin LD]]
-[[Category: Sherlin, L.D.]]
+[[Category: Sproat BS]]
-[[Category: Sproat, B.S.]]
-[[Category: QSI]]
-[[Category: complex]]
-[[Category: e. coli]]
-[[Category: glutamine]]
-[[Category: trna synthetase]]
-[[Category: trnagln]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:20:14 2007''

1euy

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GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH A TRNA MUTANT AND AN ACTIVE SITE INHIBITOR

Structural highlights

Function

Evolutionary Conservation

See Also

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