Journal
JOURNAL OF CELL BIOLOGY
Volume 150, Issue 3, Pages 447-459Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.150.3.447
Keywords
ribosomes; protein synthesis; tRNA-binding sites; cryoelectron microscopy; elongation cycle
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Funding
- NIGMS NIH HHS [1RO1 GM 55440, 1R37 GM 29169] Funding Source: Medline
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Three-dimensional cryomaps have been reconstructed for tRNA-ribosome complexes in pre- and posttranslocational states at 17-Angstrom resolution. The positions of tRNAs in the A and P sites in the pretranslocational complexes and in the P and E sites in the posttranslocational complexes have been determined. Of these, the P-site tRNA position is the same as seen earlier in the initiation-like fMet-tRNA(f)(Met)-ribosome complex, where it was visualized with high accuracy. Now, the positions of the A- and E-site tRNAs are determined with similar accuracy. The positions of the CCA end of the tRNAs at the A site are different before and after peptide bond formation. The relative positions of anticodons of P- and E-site tRNAs in the posttranslocational state are such that a codon-anticodon interaction at the E site appears feasible.
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