5H7U

NMR structure of eIF3 36-163

Summary for 5H7U

• Entry DOI: 10.2210/pdb5h7u/pdb
• NMR Information: BMRB: 36034
• Descriptor: Eukaryotic translation initiation factor 3 subunit C (1 entity in total)
• Functional Keywords: translation, initiation factor, eukaryotic initiation factor
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Cellular location: Cytoplasm : P32497
• Total number of polymer chains: 1
• Total formula weight: 14598.32

Authors

Nagata, T.,Obayashi, E. (deposition date: 2016-11-21, release date: 2017-05-31, Last modification date: 2024-05-01)

Primary citation

Obayashi, E.,Luna, R.E.,Nagata, T.,Martin-Marcos, P.,Hiraishi, H.,Singh, C.R.,Erzberger, J.P.,Zhang, F.,Arthanari, H.,Morris, J.,Pellarin, R.,Moore, C.,Harmon, I.,Papadopoulos, E.,Yoshida, H.,Nasr, M.L.,Unzai, S.,Thompson, B.,Aube, E.,Hustak, S.,Stengel, F.,Dagraca, E.,Ananbandam, A.,Gao, P.,Urano, T.,Hinnebusch, A.G.,Wagner, G.,Asano, K.
Molecular Landscape of the Ribosome Pre-initiation Complex during mRNA Scanning: Structural Role for eIF3c and Its Control by eIF5.
Cell Rep, 18:2651-2663, 2017

PubMed Abstract: During eukaryotic translation initiation, eIF3 binds the solvent-accessible side of the 40S ribosome and recruits the gate-keeper protein eIF1 and eIF5 to the decoding center. This is largely mediated by the N-terminal domain (NTD) of eIF3c, which can be divided into three parts: 3c0, 3c1, and 3c2. The N-terminal part, 3c0, binds eIF5 strongly but only weakly to the ribosome-binding surface of eIF1, whereas 3c1 and 3c2 form a stoichiometric complex with eIF1. 3c1 contacts eIF1 through Arg-53 and Leu-96, while 3c2 faces 40S protein uS15/S13, to anchor eIF1 to the scanning pre-initiation complex (PIC). We propose that the 3c0:eIF1 interaction diminishes eIF1 binding to the 40S, whereas 3c0:eIF5 interaction stabilizes the scanning PIC by precluding this inhibitory interaction. Upon start codon recognition, interactions involving eIF5, and ultimately 3c0:eIF1 association, facilitate eIF1 release. Our results reveal intricate molecular interactions within the PIC, programmed for rapid scanning-arrest at the start codon.

PubMed: 28297669
DOI: 10.1016/j.celrep.2017.02.052

Experimental method

SOLUTION NMR