5OA3

Human 40S-eIF2D-re-initiation complex

Summary for 5OA3

• Entry DOI: 10.2210/pdb5oa3/pdb
• EMDB information: 3770
• Descriptor: Eukaryotic translation initiation factor 2D, 40S ribosomal protein S5, 40S ribosomal protein S6, ... (39 entities in total)
• Functional Keywords: translation re-initiation complex, small ribosomal subunit, rna binding protein, eukaryotic translation initiation factor, translation
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 38
• Total formula weight: 1389584.97

Authors

Weisser, M.,Schaefer, T.,Leibundgut, M.,Boehringer, D.,Aylett, C.H.S.,Ban, N. (deposition date: 2017-06-20, release date: 2017-08-09, Last modification date: 2024-05-15)

Primary citation

Weisser, M.,Schafer, T.,Leibundgut, M.,Bohringer, D.,Aylett, C.H.S.,Ban, N.
Structural and Functional Insights into Human Re-initiation Complexes.
Mol. Cell, 67:447-456.e7, 2017

PubMed Abstract: After having translated short upstream open reading frames, ribosomes can re-initiate translation on the same mRNA. This process, referred to as re-initiation, controls the translation of a large fraction of mammalian cellular mRNAs, many of which are important in cancer. Key ribosomal binding proteins involved in re-initiation are the eukaryotic translation initiation factor 2D (eIF2D) or the homologous complex of MCT-1/DENR. We determined the structures of these factors bound to the human 40S ribosomal subunit in complex with initiator tRNA positioned on an mRNA start codon in the P-site using a combination of cryoelectron microscopy and X-ray crystallography. The structures, supported by biochemical experiments, reveal how eIF2D emulates the function of several canonical translation initiation factors by using three independent, flexibly connected RNA binding domains to simultaneously monitor codon-anticodon interactions in the ribosomal P-site and position the initiator tRNA.

PubMed: 28732596
DOI: 10.1016/j.molcel.2017.06.032

Experimental method

ELECTRON MICROSCOPY (4.2 Å)