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Science 4 November 2005:
Vol. 310. no. 5749, pp. 827 - 834
DOI: 10.1126/science.1117230
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Research Articles

Structures of the Bacterial Ribosome at 3.5 Å Resolution

Barbara S. Schuwirth,1,4* Maria A. Borovinskaya,3* Cathy W. Hau,2 Wen Zhang,1 Antón Vila-Sanjurjo,3 James M. Holton,3 Jamie H. Doudna Cate1,2,3{dagger}

We describe two structures of the intact bacterial 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.

1 Department of Chemistry, University of California, Berkeley, CA 94720, USA.
2 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
3 Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
4 Institute of Chemistry-Crystallography, Free University of Berlin, 14195 Berlin, Germany.

* These authors contributed equally to this work.

{dagger} To whom correspondence should be addressed. E-mail: jcate{at}lbl.gov

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