4c0s

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<StructureSection load='4c0s' size='340' side='right'caption='[[4c0s]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='4c0s' size='340' side='right'caption='[[4c0s]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4c0s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C0S FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4c0s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C0S FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=4c0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0s OCA], [https://pdbe.org/4c0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c0s RCSB], [https://www.ebi.ac.uk/pdbsum/4c0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0s ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0s OCA], [http://pdbe.org/4c0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c0s RCSB], [http://www.ebi.ac.uk/pdbsum/4c0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0s ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/EF1A2_RABIT EF1A2_RABIT]]
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Eukaryotic elongation factor eEF1A transits between the GTP- and GDP-bound conformations during the ribosomal polypeptide chain elongation. eEF1A*GTP establishes a complex with the aminoacyl-tRNA in the A site of the 80S ribosome. Correct codon-anticodon recognition triggers GTP hydrolysis, with subsequent dissociation of eEF1A*GDP from the ribosome. The structures of both the 'GTP'- and 'GDP'-bound conformations of eEF1A are unknown. Thus, the eEF1A-related ribosomal mechanisms were anticipated only by analogy with the bacterial homolog EF-Tu. Here, we report the first crystal structure of the mammalian eEF1A2*GDP complex which indicates major differences in the organization of the nucleotide-binding domain and intramolecular movements of eEF1A compared to EF-Tu. Our results explain the nucleotide exchange mechanism in the mammalian eEF1A and suggest that the first step of eEF1A*GDP dissociation from the 80S ribosome is the rotation of the nucleotide-binding domain observed after GTP hydrolysis.
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Mammalian translation elongation factor eEF1A2: X-ray structure and new features of GDP/GTP exchange mechanism in higher eukaryotes.,Crepin T, Shalak VF, Yaremchuk AD, Vlasenko DO, McCarthy A, Negrutskii BS, Tukalo MA, El'skaya AV Nucleic Acids Res. 2014 Oct 17. pii: gku974. PMID:25326326<ref>PMID:25326326</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 4c0s" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Elongation factor|Elongation factor]]
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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>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Crepin, T]]
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[[Category: Crepin T]]
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[[Category: McCarthy, A A]]
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[[Category: El'skaya AV]]
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[[Category: Negrutskii, B S]]
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[[Category: McCarthy AA]]
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[[Category: Shalak, V F]]
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[[Category: Negrutskii BS]]
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[[Category: Tukalo, M A]]
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[[Category: Shalak VF]]
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[[Category: Vlasenko, D O]]
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[[Category: Tukalo MA]]
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[[Category: Yaremchuk, A D]]
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[[Category: Vlasenko DO]]
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[[Category: Skaya, A V.El]]
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[[Category: Yaremchuk AD]]
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[[Category: Translation]]
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Revision as of 17:19, 7 September 2022

Mammalian translation elongation factor eEF1A2

PDB ID 4c0s

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