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1qru

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GLUTAMINYL-TRNA SYNTHETASE MUTANT I129T COMPLEXED WITH GLUTAMINE TRANSFER RNA

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

Categories: Escherichia coli | Large Structures | Arnez JG | Steitz TA

@@ Line 1: / Line 1: @@
-[[Image:1qru.jpg|left|200px]]<br /><applet load="1qru" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1qru, resolution 3.000&Aring;" />
-'''GLUTAMINYL-TRNA SYNTHETASE MUTANT I129T COMPLEXED WITH GLUTAMINE TRANSFER RNA'''<br />
-==Overview==
+==GLUTAMINYL-TRNA SYNTHETASE MUTANT I129T COMPLEXED WITH GLUTAMINE TRANSFER RNA==
-Three previously described mutant Escherichia coli glutaminyl-tRNA, synthetase (GlnRS) proteins that incorrectly aminoacylate the amber, suppressor derived from tRNATyr (supF) with glutamine were cocrystallized, with wild-type tRNAGln and their structures determined. In two of the, mutant enzymes studied, Asp235, which contacts base pair G3-C70 in the, acceptor stem, has been changed to asparagine in GlnRS7 and to glycine in, GlnRS10. These mutations result in changed interactions between Asn235 of, GlnRS7 and G3-C70 of the tRNA and an altered water structure between, Gly235 of GlnRS10 and base pair G3-C70. These structures suggest how the, mutant enzymes can show only small changes in their ability to, aminoacylate wild-type cognate tRNA on the one hand and yet show a lack of, discrimination against a noncognate U3-A70 base pair on the other. In, contrast, the change of Ile129 to Thr in GlnRS15 causes virtually no, change in the structure of the complex, and the explanation for its, ability to misacylate supF is unclear.
+<StructureSection load='1qru' size='340' side='right'caption='[[1qru]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1qru]] 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=1QRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QRU 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]] 3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=1qru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qru OCA], [https://pdbe.org/1qru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qru RCSB], [https://www.ebi.ac.uk/pdbsum/1qru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qru 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/qr/1qru_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=1qru ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-QRU 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 ATP 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=1QRU OCA].
+*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
+*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
-==Reference==
+__TOC__
-Crystal structures of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP., Arnez JG, Steitz TA, Biochemistry. 1996 Nov 26;35(47):14725-33. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8942633 8942633]
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Glutamine--tRNA ligase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Arnez JG]]
-[[Category: Arnez, J.G.]]
+[[Category: Steitz TA]]
-[[Category: Steitz, T.A.]]
-[[Category: ATP]]
-[[Category: aminoacyl-trna synthase]]
-[[Category: atp-b]]
-[[Category: complex (aminoacyl-trna synthase/trna)]]
-[[Category: ligase]]
-[[Category: protein biosynthesis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:55:47 2007''

1qru

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GLUTAMINYL-TRNA SYNTHETASE MUTANT I129T COMPLEXED WITH GLUTAMINE TRANSFER RNA

Structural highlights

Function

Evolutionary Conservation

See Also

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