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| | <StructureSection load='2vso' size='340' side='right'caption='[[2vso]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='2vso' size='340' side='right'caption='[[2vso]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vso]] is a 4 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=2VSO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VSO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vso]] is a 4 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=2VSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VSO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</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]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fuu|1fuu]], [[1qde|1qde]], [[1fuk|1fuk]], [[1qva|1qva]], [[1rf8|1rf8]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene></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=2vso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vso OCA], [http://pdbe.org/2vso PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vso RCSB], [http://www.ebi.ac.uk/pdbsum/2vso PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vso ProSAT]</span></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=2vso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vso OCA], [https://pdbe.org/2vso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vso RCSB], [https://www.ebi.ac.uk/pdbsum/2vso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vso ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/IF4A_YEAST IF4A_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: Altmann, M]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Baumann, U]] | + | [[Category: Altmann M]] |
| - | [[Category: Bieniossek, C]] | + | [[Category: Baumann U]] |
| - | [[Category: Bumann, M]] | + | [[Category: Bieniossek C]] |
| - | [[Category: Oberholzer, A E]] | + | [[Category: Bumann M]] |
| - | [[Category: Schutz, P]] | + | [[Category: Oberholzer AE]] |
| - | [[Category: Trachsel, H]] | + | [[Category: Schutz P]] |
| - | [[Category: Acetylation]]
| + | [[Category: Trachsel H]] |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Helicase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hydrolase-translation complex]]
| + | |
| - | [[Category: Hydrolase/translation]]
| + | |
| - | [[Category: Initiation factor]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Protein biosynthesis]]
| + | |
| - | [[Category: Rna-binding]]
| + | |
| - | [[Category: Translation initiation]]
| + | |
| - | [[Category: Translation regulation]]
| + | |
| Structural highlights
Function
IF4A_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
Translation initiation factors eIF4A and eIF4G form, together with the cap-binding factor eIF4E, the eIF4F complex, which is crucial for recruiting the small ribosomal subunit to the mRNA 5' end and for subsequent scanning and searching for the start codon. eIF4A is an ATP-dependent RNA helicase whose activity is stimulated by binding to eIF4G. We report here the structure of the complex formed by yeast eIF4G's middle domain and full-length eIF4A at 2.6-A resolution. eIF4A shows an extended conformation where eIF4G holds its crucial DEAD-box sequence motifs in a productive conformation, thus explaining the stimulation of eIF4A's activity. A hitherto undescribed interaction involves the amino acid Trp-579 of eIF4G. Mutation to alanine results in decreased binding to eIF4A and a temperature-sensitive phenotype of yeast cells that carry a Trp579Ala mutation as its sole source for eIF4G. Conformational changes between eIF4A's closed and open state provide a model for its RNA-helicase activity.
Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions.,Schutz P, Bumann M, Oberholzer AE, Bieniossek C, Trachsel H, Altmann M, Baumann U Proc Natl Acad Sci U S A. 2008 Jul 15;105(28):9564-9. Epub 2008 Jul 7. PMID:18606994[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schutz P, Bumann M, Oberholzer AE, Bieniossek C, Trachsel H, Altmann M, Baumann U. Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase controlled by protein-protein interactions. Proc Natl Acad Sci U S A. 2008 Jul 15;105(28):9564-9. Epub 2008 Jul 7. PMID:18606994
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