+Search query
-Structure paper
Title | Interaction of the G' domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM. |
---|---|
Journal, issue, pages | Mol Cell, Vol. 20, Issue 5, Page 723-731, Year 2005 |
Publish date | Dec 9, 2005 |
Authors | Partha P Datta / Manjuli R Sharma / Li Qi / Joachim Frank / Rajendra K Agrawal / |
PubMed Abstract | During tRNA translocation on the ribosome, an arc-like connection (ALC) is formed between the G' domain of elongation factor G (EF-G) and the L7/L12-stalk base of the large ribosomal subunit in the ...During tRNA translocation on the ribosome, an arc-like connection (ALC) is formed between the G' domain of elongation factor G (EF-G) and the L7/L12-stalk base of the large ribosomal subunit in the GDP state. To delineate the boundary of EF-G within the ALC, we tagged an amino acid residue near the tip of the G' domain of EF-G with undecagold, which was then visualized with three-dimensional cryo-electron microscopy (cryo-EM). Two distinct positions for the undecagold, observed in the GTP-state and GDP-state cryo-EM maps of the ribosome bound EF-G, allowed us to determine the movement of the labeled amino acid. Molecular analyses of the cryo-EM maps show: (1) that three structural components, the N-terminal domain of ribosomal protein L11, the C-terminal domain of ribosomal protein L7/L12, and the G' domain of EF-G, participate in formation of the ALC; and (2) that both EF-G and the ribosomal protein L7/L12 undergo large conformational changes to form the ALC. |
External links | Mol Cell / PubMed:16337596 |
Methods | EM (single particle) |
Resolution | 11.2 Å |
Structure data | PDB-2bcw: |
Source |
|
Keywords | RIBOSOME / Components involved in interaction between EF-G AND L7/L12 stalk base of the ribosome |