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| | <StructureSection load='3zwl' size='340' side='right'caption='[[3zwl]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='3zwl' size='340' side='right'caption='[[3zwl]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zwl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZWL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zwl]] 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=3ZWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZWL FirstGlance]. <br> |
| - | </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=3zwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zwl OCA], [https://pdbe.org/3zwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zwl RCSB], [https://www.ebi.ac.uk/pdbsum/3zwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zwl ProSAT]</span></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]] 2.2Å</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=3zwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zwl OCA], [https://pdbe.org/3zwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zwl RCSB], [https://www.ebi.ac.uk/pdbsum/3zwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zwl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/EIF3I_YEAST EIF3I_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. [[https://www.uniprot.org/uniprot/EIF3B_YEAST EIF3B_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:11387228</ref>
| + | [https://www.uniprot.org/uniprot/EIF3I_YEAST EIF3I_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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Daujotyte, D]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Lukavsky, P J]] | + | [[Category: Daujotyte D]] |
| - | [[Category: Translation]] | + | [[Category: Lukavsky PJ]] |
| Structural highlights
Function
EIF3I_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.
Publication Abstract from PubMed
Translation initiation factor eIF3 acts as the key orchestrator of the canonical initiation pathway in eukaryotes, yet its structure is greatly unexplored. We report the 2.2 A resolution crystal structure of the complex between the yeast seven-bladed beta-propeller eIF3i/TIF34 and a C-terminal alpha-helix of eIF3b/PRT1, which reveals universally conserved interactions. Mutating these interactions displays severe growth defects and eliminates association of eIF3i/TIF34 and strikingly also eIF3g/TIF35 with eIF3 and 40S subunits in vivo. Unexpectedly, 40S-association of the remaining eIF3 subcomplex and eIF5 is likewise destabilized resulting in formation of aberrant pre-initiation complexes (PICs) containing eIF2 and eIF1, which critically compromises scanning arrest on mRNA at its AUG start codon suggesting that the contacts between mRNA and ribosomal decoding site are impaired. Remarkably, overexpression of eIF3g/TIF35 suppresses the leaky scanning and growth defects most probably by preventing these aberrant PICs to form. Leaky scanning is also partially suppressed by eIF1, one of the key regulators of AUG recognition, and its mutant sui1(G107R) but the mechanism differs. We conclude that the C-terminus of eIF3b/PRT1 orchestrates co-operative recruitment of eIF3i/TIF34 and eIF3g/TIF35 to the 40S subunit for a stable and proper assembly of 48S pre-initiation complexes necessary for stringent AUG recognition on mRNAs.
Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly.,Herrmannova A, Daujotyte D, Yang JC, Cuchalova L, Gorrec F, Wagner S, Danyi I, Lukavsky PJ, Shivaya Valasek L Nucleic Acids Res. 2011 Nov 15. PMID:22090426[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Herrmannova A, Daujotyte D, Yang JC, Cuchalova L, Gorrec F, Wagner S, Danyi I, Lukavsky PJ, Shivaya Valasek L. Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly. Nucleic Acids Res. 2011 Nov 15. PMID:22090426 doi:10.1093/nar/gkr765
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