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| | ==Crystal Structure of the PCI domain of eIF3a== | | ==Crystal Structure of the PCI domain of eIF3a== |
| - | <StructureSection load='4k51' size='340' side='right' caption='[[4k51]], [[Resolution|resolution]] 2.65Å' scene=''> | + | <StructureSection load='4k51' size='340' side='right'caption='[[4k51]], [[Resolution|resolution]] 2.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4k51]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K51 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K51 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4k51]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K51 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPG1, TIF32, YBR079C, YBR0734 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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]] 2.65Å</td></tr> |
| - | <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=4k51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k51 OCA], [http://pdbe.org/4k51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k51 RCSB], [http://www.ebi.ac.uk/pdbsum/4k51 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k51 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=4k51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k51 OCA], [https://pdbe.org/4k51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k51 RCSB], [https://www.ebi.ac.uk/pdbsum/4k51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k51 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/EIF3A_YEAST EIF3A_YEAST]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome.<ref>PMID:9694884</ref> <ref>PMID:11387228</ref> <ref>PMID:12651896</ref> <ref>PMID:18765792</ref> | + | [https://www.uniprot.org/uniprot/EIF3A_YEAST EIF3A_YEAST] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome.<ref>PMID:9694884</ref> <ref>PMID:11387228</ref> <ref>PMID:12651896</ref> <ref>PMID:18765792</ref> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Transfer of genetic information from genes into proteins is mediated by messenger RNA (mRNA) that must be first recruited to ribosomal pre-initiation complexes (PICs) by a mechanism that is still poorly understood. Recent studies showed that besides eIF4F and poly(A)-binding protein, eIF3 also plays a critical role in this process, yet the molecular mechanism of its action is unknown. We showed previously that the PCI domain of the eIF3c/NIP1 subunit of yeast eIF3 is involved in RNA binding. To assess the role of the second PCI domain of eIF3 present in eIF3a/TIF32, we performed its mutational analysis and identified a 10-Ala-substitution (Box37) that severely reduces amounts of model mRNA in the 43-48S PICs in vivo as the major, if not the only, detectable defect. Crystal structure analysis of the a/TIF32-PCI domain at 2.65-A resolution showed that it is required for integrity of the eIF3 core and, similarly to the c/NIP1-PCI, is capable of RNA binding. The putative RNA-binding surface defined by positively charged areas contains two Box37 residues, R363 and K364. Their substitutions with alanines severely impair the mRNA recruitment step in vivo suggesting that a/TIF32-PCI represents one of the key domains ensuring stable and efficient mRNA delivery to the PICs.
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| - | Structural integrity of the PCI domain of eIF3a/TIF32 is required for mRNA recruitment to the 43S pre-initiation complexes.,Khoshnevis S, Gunisova S, Vlckova V, Kouba T, Neumann P, Beznoskova P, Ficner R, Valasek LS Nucleic Acids Res. 2014 Jan 13. PMID:24423867<ref>PMID:24423867</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4k51" style="background-color:#fffaf0;"></div>
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| | ==See Also== | | ==See Also== |
| - | *[[Eukaryotic initiation factor|Eukaryotic initiation factor]] | + | *[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: Ficner, R]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Khoshnevis, S]] | + | [[Category: Ficner R]] |
| - | [[Category: Neumann, P]] | + | [[Category: Khoshnevis S]] |
| - | [[Category: Biosynthetic protein]] | + | [[Category: Neumann P]] |
| - | [[Category: Eif3]]
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| - | [[Category: Pci domain]]
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| - | [[Category: Translation initiation]]
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| Structural highlights
Function
EIF3A_YEAST Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome.[1] [2] [3] [4]
See Also
References
- ↑ Valasek L, Trachsel H, Hasek J, Ruis H. Rpg1, the Saccharomyces cerevisiae homologue of the largest subunit of mammalian translation initiation factor 3, is required for translational activity. J Biol Chem. 1998 Aug 14;273(33):21253-60. PMID:9694884
- ↑ Phan L, Schoenfeld LW, Valasek L, Nielsen KH, Hinnebusch AG. A subcomplex of three eIF3 subunits binds eIF1 and eIF5 and stimulates ribosome binding of mRNA and tRNA(i)Met. EMBO J. 2001 Jun 1;20(11):2954-65. PMID:11387228 doi:http://dx.doi.org/10.1093/emboj/20.11.2954
- ↑ Valasek L, Mathew AA, Shin BS, Nielsen KH, Szamecz B, Hinnebusch AG. The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo. Genes Dev. 2003 Mar 15;17(6):786-99. PMID:12651896 doi:http://dx.doi.org/10.1101/gad.1065403
- ↑ Szamecz B, Rutkai E, Cuchalova L, Munzarova V, Herrmannova A, Nielsen KH, Burela L, Hinnebusch AG, Valasek L. eIF3a cooperates with sequences 5' of uORF1 to promote resumption of scanning by post-termination ribosomes for reinitiation on GCN4 mRNA. Genes Dev. 2008 Sep 1;22(17):2414-25. doi: 10.1101/gad.480508. PMID:18765792 doi:http://dx.doi.org/10.1101/gad.480508
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