Summary information and primary citation
- PDB-id
-
1mj1;
SNAP-derived features in text and
JSON formats
- Class
- ribosome
- Method
- cryo-EM (13.0 Å)
- Summary
- Fitting the ternary complex of ef-tu-trna-gtp and
ribosomal proteins into a 13 a cryo-EM map of the coli 70s
ribosome
- Reference
-
Stark H, Rodnina MV, Wieden H-J, Zemlin F, Wintermeyer W,
van Heel M (2002): "Ribosome
Interactions of Aminoacyl-tRNA and Elongation Factor TU
in the Codon Recognition Complex."
Nat.Struct.Biol., 9, 849-854.
- Abstract
- The mRNA codon in the ribosomal A-site is recognized by
aminoacyl-tRNA (aa-tRNA) in a ternary complex with
elongation factor Tu (EF-Tu) and GTP. Here we report the 13
A resolution three-dimensional reconstruction determined by
cryo-electron microscopy of the kirromycin-stalled
codon-recognition complex. The structure of the ternary
complex is distorted by binding of the tRNA anticodon arm
in the decoding center. The aa-tRNA interacts with 16S
rRNA, helix 69 of 23S rRNA and proteins S12 and L11, while
the sarcin-ricin loop of 23S rRNA contacts domain 1 of
EF-Tu near the nucleotide-binding pocket. These results
provide a detailed snapshot view of an important functional
state of the ribosome and suggest mechanisms of decoding
and GTPase activation.
