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| | <StructureSection load='1ije' size='340' side='right'caption='[[1ije]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='1ije' size='340' side='right'caption='[[1ije]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ije]] 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=1IJE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1IJE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ije]] 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=1IJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IJE FirstGlance]. <br> |
| - | </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></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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f60|1f60]], [[1g7c|1g7c]]</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></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TEF5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=1ije FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ije OCA], [https://pdbe.org/1ije PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ije RCSB], [https://www.ebi.ac.uk/pdbsum/1ije PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ije ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ije FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ije OCA], [http://pdbe.org/1ije PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ije RCSB], [http://www.ebi.ac.uk/pdbsum/1ije PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ije 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] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Andersen, G R]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Kinzy, T G]] | + | [[Category: Andersen GR]] |
| - | [[Category: Nyborg, J]] | + | [[Category: Kinzy TG]] |
| - | [[Category: Pedersen, L]] | + | [[Category: Nyborg J]] |
| - | [[Category: Valente, L]] | + | [[Category: Pedersen L]] |
| - | [[Category: Protein complex]]
| + | [[Category: Valente L]] |
| - | [[Category: Translation]]
| + | |
| Structural highlights
Function
EF1A_YEAST
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In the elongation cycle of protein biosynthesis, the nucleotide exchange factor eEF1Balpha catalyzes the exchange of GDP bound to the G-protein, eEF1A, for GTP. To obtain more information about the recently solved eEF1A-eEF1Balpha structure, we determined the structures of the eEF1A-eEF1Balpha-GDP-Mg2+, eEF1A-eEF1Balpha-GDP and eEF1A-eEF1Balpha-GDPNP complexes at 3.0, 2.4 and 2.05 A resolution, respectively. Minor changes, specifically around the nucleotide binding site, in eEF1A and eEF1Balpha are consistent with in vivo data. The base, sugar and alpha-phosphate bind as in other known nucleotide G-protein complexes, whereas the beta- and gamma-phosphates are disordered. A mutation of Lys 205 in eEF1Balpha that inserts into the Mg2+ binding site of eEF1A is lethal. This together with the structures emphasizes the essential role of Mg2+ in nucleotide exchange in the eEF1A-eEF1Balpha complex.
Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex.,Andersen GR, Valente L, Pedersen L, Kinzy TG, Nyborg J Nat Struct Biol. 2001 Jun;8(6):531-4. PMID:11373622[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Andersen GR, Valente L, Pedersen L, Kinzy TG, Nyborg J. Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex. Nat Struct Biol. 2001 Jun;8(6):531-4. PMID:11373622 doi:http://dx.doi.org/10.1038/88598
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