Summary information and primary citation
- PDB-id
-
3jam;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- translation
- Method
- cryo-EM (3.46 Å)
- Summary
- Cryoem structure of 40s-eif1a-eif1 complex from
yeast
- Reference
-
Llacer JL, Hussain T, Marler L, Aitken CE, Thakur A,
Lorsch JR, Hinnebusch AG, Ramakrishnan V (2015):
"Conformational
Differences between Open and Closed States of the
Eukaryotic Translation Initiation Complex."
Mol.Cell, 59, 399-412. doi:
10.1016/j.molcel.2015.06.033.
- Abstract
- Translation initiation in eukaryotes begins with the
formation of a pre-initiation complex (PIC) containing the
40S ribosomal subunit, eIF1, eIF1A, eIF3, ternary complex
(eIF2-GTP-Met-tRNAi), and eIF5. The PIC, in an open
conformation, attaches to the 5' end of the mRNA and scans
to locate the start codon, whereupon it closes to arrest
scanning. We present single particle cryo-electron
microscopy (cryo-EM) reconstructions of 48S PICs from yeast
in these open and closed states, at 6.0 Å and 4.9 Å,
respectively. These reconstructions show eIF2β as well as a
configuration of eIF3 that appears to encircle the 40S,
occupying part of the subunit interface. Comparison of the
complexes reveals a large conformational change in the 40S
head from an open mRNA latch conformation to a closed one
that constricts the mRNA entry channel and narrows the P
site to enclose tRNAi, thus elucidating key events in start
codon recognition.