2NLW

Solution structure of the RRM domain of human eukaryotic initiation factor 3b

2NLW の概要

• エントリーDOI: 10.2210/pdb2nlw/pdb
• 分子名称: Eukaryotic translation initiation factor 3 subunit 9 (1 entity in total)
• 機能のキーワード: translation initiation, eukaryotic initiation factor 3 complex, rna recognition motif, translation
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (Probable): P55884
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11955.44

構造登録者

ElAntak, L.,Tzakos, A.G.,Locker, N.,Lukavsky, P.J. (登録日: 2006-10-20, 公開日: 2007-02-06, 最終更新日: 2023-12-27)

主引用文献

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

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: 17190833
DOI: 10.1074/jbc.M610860200

実験手法

SOLUTION NMR