View source for 6ra9


==Novel structural features and post-translational modifications in eukaryotic elongation factor 1A2 from Oryctolagus cuniculus==
<StructureSection load='6ra9' size='340' side='right'caption='[[6ra9]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ra9]] 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=6RA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RA9 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]] 2.7&#8491;</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GPE:L-ALPHA-GLYCEROPHOSPHORYLETHANOLAMINE'>GPE</scene>, <scene name='pdbligand=POK:2-[[~{N}-[(4~{S})-4-azanyl-5-oxidanylidene-pentyl]carbamimidoyl]amino]ethanoic+acid'>POK</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6ra9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ra9 OCA], [https://pdbe.org/6ra9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ra9 RCSB], [https://www.ebi.ac.uk/pdbsum/6ra9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ra9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EF1A2_RABIT EF1A2_RABIT] 
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== Publication Abstract from PubMed ==
Spontaneous mutations in the EEF1A2 gene cause epilepsy and severe neurological disabilities in children. The crystal structure of eEF1A2 protein purified from rabbit skeletal muscle reveals a post-translationally modified dimer that provides information about the sites of interaction with numerous binding partners, including itself, and maps these mutations onto the dimer and tetramer interfaces. The spatial locations of the side chain carboxylates of Glu301 and Glu374, to which phosphatidylethanolamine is uniquely attached via an amide bond, define the anchoring points of eEF1A2 to cellular membranes and interorganellar membrane contact sites. Additional bioinformatic and molecular modeling results provide novel structural insight into the demonstrated binding of eEF1A2 to SH3 domains, the common MAPK docking groove, filamentous actin, and phosphatidylinositol-4 kinase IIIbeta. In this new light, the role of eEF1A2 as an ancient, multifaceted, and articulated G protein at the crossroads of autophagy, oncogenesis and viral replication appears very distant from the "canonical" one of delivering aminoacyl-tRNAs to the ribosome that has dominated the scene and much of the thinking for many decades.

Structural Cues for Understanding eEF1A2 Moonlighting.,Carriles AA, Mills A, Munoz-Alonso MJ, Gutierrez D, Dominguez JM, Hermoso JA, Gago F Chembiochem. 2021 Jan 15;22(2):374-391. doi: 10.1002/cbic.202000516. Epub 2020, Oct 20. PMID:32875694<ref>PMID:32875694</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6ra9" style="background-color:#fffaf0;"></div>

==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Carriles AA]]
[[Category: Gago F]]
[[Category: Hermoso J]]