6YAM

Mammalian 48S late-stage translation initiation complex (LS48S+eIF3 IC) with beta-globin mRNA

This is a non-PDB format compatible entry.

Summary for 6YAM

• Entry DOI: 10.2210/pdb6yam/pdb
• Related: 6YAL 6YAN
• EMDB information: 10761 10763 10764
• Descriptor: initiator methionylated tRNA, ribosomal protein eS7, 40S ribosomal protein eS8, ... (53 entities in total)
• Functional Keywords: translation initiation, eukaryotic initiation factor 1, eukaryotic initiation factor 1a, eukaryotic initiation factor 3, late-stage initiation complex, rabbit, translation
• Biological source: Oryctolagus cuniculus (Rabbit); More
• Total number of polymer chains: 50
• Total formula weight: 1967717.01

Authors

Bochler, A.,Simonetti, A.,Guca, E.,Hashem, Y. (deposition date: 2020-03-12, release date: 2020-04-08, Last modification date: 2024-10-16)

Primary citation

Simonetti, A.,Guca, E.,Bochler, A.,Kuhn, L.,Hashem, Y.
Structural Insights into the Mammalian Late-Stage Initiation Complexes.
Cell Rep, 31:107497-107497, 2020

PubMed Abstract: In higher eukaryotes, the mRNA sequence in the direct vicinity of the start codon, called the Kozak sequence (CRCCaugG, where R is a purine), is known to influence the rate of the initiation process. However, the molecular basis underlying its role remains poorly understood. Here, we present the cryoelectron microscopy (cryo-EM) structures of mammalian late-stage 48S initiation complexes (LS48S ICs) in the presence of two different native mRNA sequences, β-globin and histone 4, at overall resolution of 3 and 3.5 Å, respectively. Our high-resolution structures unravel key interactions from the mRNA to eukaryotic initiation factors (eIFs): 1A, 2, 3, 18S rRNA, and several 40S ribosomal proteins. In addition, we are able to study the structural role of ABCE1 in the formation of native 48S ICs. Our results reveal a comprehensive map of ribosome/eIF-mRNA and ribosome/eIF-tRNA interactions and suggest the impact of mRNA sequence on the structure of the LS48S IC.

PubMed: 32268096
DOI: 10.1016/j.celrep.2020.03.061

Experimental method

ELECTRON MICROSCOPY (3.6 Å)