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5A5T

Structure of mammalian eIF3 in the context of the 43S preinitiation complex

Summary for 5A5T
Entry DOI10.2210/pdb5a5t/pdb
Related5A5U
EMDB information3056
DescriptorEUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT A, EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C, EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT E, ... (8 entities in total)
Functional Keywordshydrolase, eif3, eukaryotic initiation factor 3, preinitiation complex, pci/mpn core, eif3g/i/b, eif3d
Biological sourceORYCTOLAGUS CUNICULUS (RABBIT)
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Total number of polymer chains8
Total formula weight527397.15
Authors
des-Georges, A.,Dhote, V.,Kuhn, L.,Hellen, C.U.T.,Pestova, T.V.,Frank, J.,Hashem, Y. (deposition date: 2015-06-21, release date: 2015-09-09, Last modification date: 2024-05-08)
Primary citationDes-Georges, A.,Dhote, V.,Kuhn, L.,Hellen, C.U.T.,Pestova, T.V.,Frank, J.,Hashem, Y.
Structure of Mammalian Eif3 in the Context of the 43S Preinitiation Complex.
Nature, 525:491-, 2015
Cited by
PubMed Abstract: During eukaryotic translation initiation, 43S complexes, comprising a 40S ribosomal subunit, initiator transfer RNA and initiation factors (eIF) 2, 3, 1 and 1A, attach to the 5'-terminal region of messenger RNA and scan along it to the initiation codon. Scanning on structured mRNAs also requires the DExH-box protein DHX29. Mammalian eIF3 contains 13 subunits and participates in nearly all steps of translation initiation. Eight subunits having PCI (proteasome, COP9 signalosome, eIF3) or MPN (Mpr1, Pad1, amino-terminal) domains constitute the structural core of eIF3, to which five peripheral subunits are flexibly linked. Here we present a cryo-electron microscopy structure of eIF3 in the context of the DHX29-bound 43S complex, showing the PCI/MPN core at ∼6 Å resolution. It reveals the organization of the individual subunits and their interactions with components of the 43S complex. We were able to build near-complete polyalanine-level models of the eIF3 PCI/MPN core and of two peripheral subunits. The implications for understanding mRNA ribosomal attachment and scanning are discussed.
PubMed: 26344199
DOI: 10.1038/NATURE14891
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (6 Å)
Structure validation

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