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| | ==Solution structure of the RRM domain of human eukaryotic initiation factor 3b== | | ==Solution structure of the RRM domain of human eukaryotic initiation factor 3b== |
| - | <StructureSection load='2nlw' size='340' side='right'caption='[[2nlw]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''> | + | <StructureSection load='2nlw' size='340' side='right'caption='[[2nlw]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2nlw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NLW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2nlw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NLW FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EIF3S9 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2nlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nlw OCA], [https://pdbe.org/2nlw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nlw RCSB], [https://www.ebi.ac.uk/pdbsum/2nlw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nlw 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=2nlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nlw OCA], [https://pdbe.org/2nlw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nlw RCSB], [https://www.ebi.ac.uk/pdbsum/2nlw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nlw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/EIF3B_HUMAN EIF3B_HUMAN]] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.<ref>PMID:9388245</ref>
| + | [https://www.uniprot.org/uniprot/EIF3B_HUMAN EIF3B_HUMAN] Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.<ref>PMID:9388245</ref> |
| | == 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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: ElAntak, L]] | + | [[Category: ElAntak L]] |
| - | [[Category: Locker, N]] | + | [[Category: Locker N]] |
| - | [[Category: Lukavsky, P J]] | + | [[Category: Lukavsky PJ]] |
| - | [[Category: Tzakos, A G]] | + | [[Category: Tzakos AG]] |
| - | [[Category: Eukaryotic initiation factor 3 complex]]
| + | |
| - | [[Category: Rna recognition motif]]
| + | |
| - | [[Category: Translation]]
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| - | [[Category: Translation initiation]]
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| Structural highlights
Function
EIF3B_HUMAN Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.[1]
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
Mammalian eIF3 is a 700-kDa multiprotein complex essential for initiation of protein synthesis in eukaryotic cells. It consists of 13 subunits (eIF3a to -m), among which eIF3b serves as a major scaffolding protein. Here we report the solution structure of the N-terminal RNA recognition motif of human eIF3b (eIF3b-RRM) determined by NMR spectroscopy. The structure reveals a noncanonical RRM with a negatively charged surface in the beta-sheet area contradictory with potential RNA binding activity. Instead, eIF3j, which is required for stable 40 S ribosome binding of the eIF3 complex, specifically binds to the rear alpha-helices of the eIF3b-RRM, opposite to its beta-sheet surface. Moreover, we identify that an N-terminal 69-amino acid peptide of eIF3j is sufficient for binding to eIF3b-RRM and that this interaction is essential for eIF3b-RRM recruitment to the 40 S ribosomal subunit. Our results provide the first structure of an important subdomain of a core eIF3 subunit and detailed insights into protein-protein interactions between two eIF3 subunits required for stable eIF3 recruitment to the 40 S subunit.
Structure of eIF3b RNA recognition motif and its interaction with eIF3j: structural insights into the recruitment of eIF3b to the 40 S ribosomal subunit.,ElAntak L, Tzakos AG, Locker N, Lukavsky PJ J Biol Chem. 2007 Mar 16;282(11):8165-74. Epub 2006 Dec 26. PMID:17190833[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chaudhuri J, Chakrabarti A, Maitra U. Biochemical characterization of mammalian translation initiation factor 3 (eIF3). Molecular cloning reveals that p110 subunit is the mammalian homologue of Saccharomyces cerevisiae protein Prt1. J Biol Chem. 1997 Dec 5;272(49):30975-83. PMID:9388245
- ↑ ElAntak L, Tzakos AG, Locker N, Lukavsky PJ. Structure of eIF3b RNA recognition motif and its interaction with eIF3j: structural insights into the recruitment of eIF3b to the 40 S ribosomal subunit. J Biol Chem. 2007 Mar 16;282(11):8165-74. Epub 2006 Dec 26. PMID:17190833 doi:10.1074/jbc.M610860200
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