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| | ==Crystal structure of the eIF3b-CTD/eIF3i/eIF3g-NTD translation initiation complex== | | ==Crystal structure of the eIF3b-CTD/eIF3i/eIF3g-NTD translation initiation complex== |
| - | <StructureSection load='4u1e' size='340' side='right' caption='[[4u1e]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4u1e' size='340' side='right'caption='[[4u1e]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4u1e]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U1E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U1E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4u1e]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_YJM789 Saccharomyces cerevisiae YJM789]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U1E FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u1f|4u1f]], [[4u1d|4u1d]], [[4u1c|4u1c]]</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]] 2Å</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=4u1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u1e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u1e RCSB], [http://www.ebi.ac.uk/pdbsum/4u1e PDBsum]</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=4u1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u1e OCA], [https://pdbe.org/4u1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u1e RCSB], [https://www.ebi.ac.uk/pdbsum/4u1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u1e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/EIF3I_YEAS7 EIF3I_YEAS7]] 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 (By similarity). [[http://www.uniprot.org/uniprot/EIF3G_YEAST EIF3G_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. TIF35 binds to mRNA and rRNA. Binds to the 18S rRNA but non-specifically.<ref>PMID:10085088</ref> [[http://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/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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4u1e" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Eukaryotic initiation factor 3D structures|Eukaryotic initiation factor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ban, N]] | + | [[Category: Large Structures]] |
| - | [[Category: Erzberger, J P]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Schaefer, T]] | + | [[Category: Saccharomyces cerevisiae YJM789]] |
| - | [[Category: Zhang, S]] | + | [[Category: Ban N]] |
| - | [[Category: Beta-propeller]] | + | [[Category: Erzberger JP]] |
| - | [[Category: Eif3 complex]] | + | [[Category: Schaefer T]] |
| - | [[Category: Translation]] | + | [[Category: Zhang S]] |
| - | [[Category: Translation initiation]]
| + | |
| Structural highlights
Function
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.[1]
Publication Abstract from PubMed
Eukaryotic translation initiation requires the recruitment of the large, multiprotein eIF3 complex to the 40S ribosomal subunit. We present X-ray structures of all major components of the minimal, six-subunit Saccharomyces cerevisiae eIF3 core. These structures, together with electron microscopy reconstructions, cross-linking coupled to mass spectrometry, and integrative structure modeling, allowed us to position and orient all eIF3 components on the 40SeIF1 complex, revealing an extended, modular arrangement of eIF3 subunits. Yeast eIF3 engages 40S in a clamp-like manner, fully encircling 40S to position key initiation factors on opposite ends of the mRNA channel, providing a platform for the recruitment, assembly, and regulation of the translation initiation machinery. The structures of eIF3 components reported here also have implications for understanding the architecture of the mammalian 43S preinitiation complex and the complex of eIF3, 40S, and the hepatitis C internal ribosomal entry site RNA.
Molecular Architecture of the 40SeIF1eIF3 Translation Initiation Complex.,Erzberger JP, Stengel F, Pellarin R, Zhang S, Schaefer T, Aylett CH, Cimermancic P, Boehringer D, Sali A, Aebersold R, Ban N Cell. 2014 Aug 28;158(5):1123-35. doi: 10.1016/j.cell.2014.07.044. PMID:25171412[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ Erzberger JP, Stengel F, Pellarin R, Zhang S, Schaefer T, Aylett CH, Cimermancic P, Boehringer D, Sali A, Aebersold R, Ban N. Molecular Architecture of the 40SeIF1eIF3 Translation Initiation Complex. Cell. 2014 Aug 28;158(5):1123-35. doi: 10.1016/j.cell.2014.07.044. PMID:25171412 doi:http://dx.doi.org/10.1016/j.cell.2014.07.044
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