Summary information and primary citation
- PDB-id
- 1mj1; SNAP-derived features in text and JSON formats;
DNAproDB
- 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.
Cartoon-block schematics in six views