Journal
SCIENCE
Volume 310, Issue 5749, Pages 827-834Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1117230
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- NCI NIH HHS [CA92584] Funding Source: Medline
- NIGMS NIH HHS [GM65050] Funding Source: Medline
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We describe two structures of the intact bacteria[ ribosome from Escherichia coli determined to a resolution of 3.5 angstroms by x-ray crystallography. These structures provide a detailed view of the interface between the small and large ribosomal subunits and the conformation of the peptidyl transferase center in the context of the intact ribosome. Differences between the two ribosomes reveal a high degree of flexibility between the head and the rest of the small subunit. Swiveling of the head of the small subunit observed in the present structures, coupled to-the ratchet-like motion of the two subunits observed previously, suggests a mechanism for the final movements of messenger RNA (mRNA) and transfer RNAs (tRNAs) during translocation.
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