2nlw
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Mammalian eIF3 is a 700 kDa multiprotein complex essential for initiation | + | 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. |
==About this Structure== | ==About this Structure== | ||
| Line 10: | Line 10: | ||
==Reference== | ==Reference== | ||
| - | Structure of eIF3b | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17190833 17190833] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: ElAntak, L.]] | [[Category: ElAntak, L.]] | ||
[[Category: Locker, N.]] | [[Category: Locker, N.]] | ||
| - | [[Category: Lukavsky, P | + | [[Category: Lukavsky, P J.]] |
| - | [[Category: Tzakos, A | + | [[Category: Tzakos, A G.]] |
[[Category: eukaryotic initiation factor 3 complex]] | [[Category: eukaryotic initiation factor 3 complex]] | ||
[[Category: rna recognition motif]] | [[Category: rna recognition motif]] | ||
[[Category: translation initiation]] | [[Category: translation initiation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:08:27 2008'' |
Revision as of 16:08, 21 February 2008
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Solution structure of the RRM domain of human eukaryotic initiation factor 3b
Overview
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.
About this Structure
2NLW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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