The ribosome undergoes pronounced periodic conformational changes during pr
otein synthesis. Of particular importance are those occurring around the de
coding site, the region of the 16 S rRNA interacting with the mRNA-(tRNA)(2
) complex. We have incorporated structural information from X-ray crystallo
graphy and nuclear magnetic resonance into cryo-electron microscopic maps o
f ribosomal complexes designed to capture structural changes at the translo
cation step of the polypeptide elongation cycle. The A-site region of the d
ecoding site actively participates in the translocation of the tRNA from th
e A to the P-site upon GTP hydrolysis by elongation factor G, shifting appr
oximately 8 Angstrom toward the P-site. This implies that elongation factor
G actively pushes both the decoding site and the mRNA/tRNA complex during
translocation. (C) 2000 Academic Press.