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2nlw

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==Overview==
==Overview==
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Mammalian eIF3 is a 700 kDa multiprotein complex essential for initiation, of protein synthesis in eukaryotic cells. It consists of 13 subunits, (eIF3a-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 non-canonical RRM with a negatively charged surface in the, beta-sheet area contradictory with potential RNA binding activity., Instead, eIF3j, which is required for stable 40S 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 40S 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 40S ribosome.
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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==
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==Reference==
==Reference==
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Structure of eIF3b-RRM and its interaction with eIF3j: Structural insights into the recruitment of eIF3b to the 40S ribosomal subunit., Elantak L, Tzakos AG, Locker N, Lukavsky PJ, J Biol Chem. 2006 Dec 26;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17190833 17190833]
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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.]]
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[[Category: Lukavsky, P.J.]]
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[[Category: Lukavsky, P J.]]
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[[Category: Tzakos, A.G.]]
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[[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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:39:00 2008''
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''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


2nlw

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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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