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3wxm

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==Crystal structure of archaeal Pelota and GTP-bound EF1 alpha complex==
==Crystal structure of archaeal Pelota and GTP-bound EF1 alpha complex==
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<StructureSection load='3wxm' size='340' side='right' caption='[[3wxm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='3wxm' size='340' side='right'caption='[[3wxm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3wxm]] is a 8 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3agj 3agj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WXM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WXM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3wxm]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix_K1 Aeropyrum pernix K1]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3agj 3agj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WXM FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><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]] 2.3&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wxm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wxm RCSB], [http://www.ebi.ac.uk/pdbsum/3wxm PDBsum]</span></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=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<table>
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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=3wxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wxm OCA], [https://pdbe.org/3wxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wxm RCSB], [https://www.ebi.ac.uk/pdbsum/3wxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wxm ProSAT]</span></td></tr>
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<div style="background-color:#fffaf0;">
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</table>
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== Publication Abstract from PubMed ==
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== Function ==
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No-go decay and nonstop decay are mRNA surveillance pathways that detect translational stalling and degrade the underlying mRNA, allowing the correct translation of the genetic code. In eukaryotes, the protein complex of Pelota (yeast Dom34) and Hbs1 translational GTPase recognizes the stalled ribosome containing the defective mRNA. Recently, we found that archaeal Pelota (aPelota) associates with archaeal elongation factor 1alpha (aEF1alpha) to act in the mRNA surveillance pathway, which accounts for the lack of an Hbs1 ortholog in archaea. Here we present the complex structure of aPelota and GTP-bound aEF1alpha determined at 2.3-A resolution. The structure reveals how GTP-bound aEF1alpha recognizes aPelota and how aPelota in turn stabilizes the GTP form of aEF1alpha. Combined with the functional analysis in yeast, the present results provide structural insights into the molecular interaction between eukaryotic Pelota and Hbs1. Strikingly, the aPelota.aEF1alpha complex structurally resembles the tRNA.EF-Tu complex bound to the ribosome. Our findings suggest that the molecular mimicry of tRNA in the distorted "A/T state" conformation by Pelota enables the complex to efficiently detect and enter the empty A site of the stalled ribosome.
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[https://www.uniprot.org/uniprot/EF1A_AERPE EF1A_AERPE] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (By similarity).
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Structural basis for mRNA surveillance by archaeal Pelota and GTP-bound EF1alpha complex.,Kobayashi K, Kikuno I, Kuroha K, Saito K, Ito K, Ishitani R, Inada T, Nureki O Proc Natl Acad Sci U S A. 2010 Oct 12;107(41):17575-9. Epub 2010 Sep 27. PMID:20876129<ref>PMID:20876129</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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==See Also==
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</div>
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ishitani, R.]]
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[[Category: Aeropyrum pernix K1]]
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[[Category: Kobayashi, K.]]
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[[Category: Large Structures]]
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[[Category: Nureki, O.]]
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[[Category: Ishitani R]]
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[[Category: Mrna surveillance]]
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[[Category: Kobayashi K]]
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[[Category: Ribosome]]
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[[Category: Nureki O]]
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[[Category: Translation-hydrolase complex]]
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Current revision

Crystal structure of archaeal Pelota and GTP-bound EF1 alpha complex

PDB ID 3wxm

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