2NLW
Solution structure of the RRM domain of human eukaryotic initiation factor 3b
Summary for 2NLW
| Entry DOI | 10.2210/pdb2nlw/pdb |
| Descriptor | Eukaryotic translation initiation factor 3 subunit 9 (1 entity in total) |
| Functional Keywords | translation initiation, eukaryotic initiation factor 3 complex, rna recognition motif, translation |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm (Probable): P55884 |
| Total number of polymer chains | 1 |
| Total formula weight | 11955.44 |
| Authors | ElAntak, L.,Tzakos, A.G.,Locker, N.,Lukavsky, P.J. (deposition date: 2006-10-20, release date: 2007-02-06, Last modification date: 2023-12-27) |
| Primary citation | ElAntak, L.,Tzakos, A.G.,Locker, N.,Lukavsky, P.J. 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., 282:8165-8174, 2007 Cited by PubMed Abstract: 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. PubMed: 17190833DOI: 10.1074/jbc.M610860200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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