Summary information and primary citation
- PDB-id
-
1zo1;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- translation-RNA
- Method
- cryo-EM (13.8 Å)
- Summary
- If2, if1, and trna fitted to cryo-EM data of e. coli
70s initiation complex
- Reference
-
Allen GS, Zavialov A, Gursky R, Ehrenberg M, Frank J
(2005): "The
Cryo-EM Structure of a Translation Initiation Complex
from Escherichia coli."
Cell(Cambridge,Mass.), 121,
703-712. doi: 10.1016/j.cell.2005.03.023.
- Abstract
- The 70S ribosome and its complement of factors required
for initiation of translation in E. coli were purified
separately and reassembled in vitro with GDPNP, producing a
stable initiation complex (IC) stalled after 70S assembly.
We have obtained a cryo-EM reconstruction of the IC showing
IF2*GDPNP at the intersubunit cleft of the 70S ribosome.
IF2*GDPNP contacts the 30S and 50S subunits as well as
fMet-tRNA(fMet). IF2 here adopts a conformation radically
different from that seen in the recent crystal structure of
IF2. The C-terminal domain of IF2 binds to the
single-stranded portion of fMet-tRNA(fMet), thereby forcing
the tRNA into a novel orientation at the P site. The GTP
binding domain of IF2 binds to the GTPase-associated center
of the 50S subunit in a manner similar to EF-G and EF-Tu.
Additionally, we present evidence for the localization of
IF1, IF3, one C-terminal domain of L7/L12, and the
N-terminal domain of IF2 in the initiation complex.