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Original Article |
Correspondence to: Joachim Frank, HHMI, Wadsworth Center, Empire State Plaza, PO Box 509, Albany, NY 12201-0509. Tel:518 474-7002 Fax:518 486-2191 E-mail:joachim{at}wadsworth.org.
Three-dimensional cryomaps have been reconstructed for tRNAribosome complexes in pre- and posttranslocational states at 17-Å 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-tRNAfMet-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 codonanticodon interaction at the E site appears feasible.
Key Words: ribosomes, protein synthesis, tRNA-binding sites, cryoelectron microscopy, elongation cycle
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