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| | <StructureSection load='5o8w' size='340' side='right'caption='[[5o8w]], [[Resolution|resolution]] 1.67Å' scene=''> | | <StructureSection load='5o8w' size='340' side='right'caption='[[5o8w]], [[Resolution|resolution]] 1.67Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5o8w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O8W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O8W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5o8w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O8W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O8W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.67Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>, <scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f60|1f60]]</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=5o8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o8w OCA], [https://pdbe.org/5o8w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o8w RCSB], [https://www.ebi.ac.uk/pdbsum/5o8w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o8w ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EFB1, TEF5, YAL003W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=5o8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o8w OCA], [http://pdbe.org/5o8w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o8w RCSB], [http://www.ebi.ac.uk/pdbsum/5o8w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o8w ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/EF1B_YEAST EF1B_YEAST]] Catalytic subunit of the guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) of the eukaryotic elongation factor 1 complex (eEF1). Stimulates the exchange of GDP for GTP on elongation factor 1A (eEF1A), probably by displacing GDP from the nucleotide binding pocket in eEF1A. The 30-fold higher concentration of GTP compared to GDP in cells favors the formation of eEF1A-GTP, which rapidly forms a ternary complex with aminoacyl-tRNA that in turn displaces eEF1B from the complex.<ref>PMID:10409717</ref> | + | [https://www.uniprot.org/uniprot/EF1A_YEAST EF1A_YEAST] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Elongation factor|Elongation factor]] | + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Andersen, G R]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Hunte, C]] | + | [[Category: Andersen GR]] |
| - | [[Category: Wirth, C]] | + | [[Category: Hunte C]] |
| - | [[Category: Covalent modification]] | + | [[Category: Wirth C]] |
| - | [[Category: Protein-protein complex]]
| + | |
| - | [[Category: Translation]]
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| Structural highlights
5o8w is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.67Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
EF1A_YEAST
Publication Abstract from PubMed
Ribosomal translation factors are fundamental for protein synthesis and highly conserved in all kingdoms of life. The essential eukaryotic elongation factor 1A (eEF1A), delivers aminoacyl tRNAs to the A-site of the translating 80S ribosome. Several studies have revealed that eEF1A is posttranslationally modified. Using MS analysis, site-directed mutagenesis, and X-ray structural data analysis of Saccharomyces cerevisiae eEF1A, we identified a posttranslational modification in which the alpha amino group of mono-L-glutamine is covalently linked to the side chain of glutamate 45 in eEF1A. The MS analysis suggested that all eEF1A molecules are modified by this glutaminylation and that this posttranslational modification occurs at all stages of yeast growth. The mutational studies revealed that this glutaminylation is not essential for the normal functions of eEF1A in S. cerevisiae However, eEF1A glutaminylation slightly reduced growth under antibiotic-induced translational stress conditions. Moreover, we identified the same posttranslational modification in eEF1A from Schizosaccharomyces pombe, but not in various other eukaryotic organisms tested despite strict conservation of the Glu-45 residue among these organisms. We therefore conclude that eEF1A glutaminylation is a yeast-specific posttranslational modification, which appears to influence protein translation.
Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A.,Jank T, Belyi Y, Wirth C, Rospert S, Hu Z, Dengjel J, Tzivelekidis T, Andersen GR, Hunte C, Schlosser A, Aktories K J Biol Chem. 2017 Aug 11. pii: jbc.M117.801035. doi: 10.1074/jbc.M117.801035. PMID:28801462[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jank T, Belyi Y, Wirth C, Rospert S, Hu Z, Dengjel J, Tzivelekidis T, Andersen GR, Hunte C, Schlosser A, Aktories K. Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A. J Biol Chem. 2017 Aug 11. pii: jbc.M117.801035. doi: 10.1074/jbc.M117.801035. PMID:28801462 doi:http://dx.doi.org/10.1074/jbc.M117.801035
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