| Literature DB >> 11099376 |
M S VanLoock1, R K Agrawal, I S Gabashvili, L Qi, J Frank, S C Harvey.
Abstract
The ribosome undergoes pronounced periodic conformational changes during protein synthesis. Of particular importance are those occurring around the decoding site, the region of the 16 S rRNA interacting with the mRNA-(tRNA)(2) complex. We have incorporated structural information from X-ray crystallography and nuclear magnetic resonance into cryo-electron microscopic maps of ribosomal complexes designed to capture structural changes at the translocation step of the polypeptide elongation cycle. The A-site region of the decoding site actively participates in the translocation of the tRNA from the A to the P-site upon GTP hydrolysis by elongation factor G, shifting approximately 8 A toward the P-site. This implies that elongation factor G actively pushes both the decoding site and the mRNA/tRNA complex during translocation. Copyright 2000 Academic Press.Entities:
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Year: 2000 PMID: 11099376 DOI: 10.1006/jmbi.2000.4213
Source DB: PubMed Journal: J Mol Biol ISSN: 0022-2836 Impact factor: 5.469