Structures of the Bacterial Ribosome at 3.5 Å Resolution

By B. Schuwirth, M. A. Borovinskaya, C. Hau, Wen Zhang, A. Vila-Sanjurjo, J. Holton, J. Cate. Science, 2005

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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.

Subfields: Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/00ba3b44dc92f049d8d1e761909793aa8f4edfa4

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Citations in the corpus

Studies on the role of helix 69 of 23S rRNA in the factor-dependent stages of translation initiation, elongation, and termination (2011, background): “A1493 and G1494 of 16S rRNA interact with the residues A1912 and A1913 from the loop region of helix 69 of 23S rRNA (Schuwirth et al. 2005; Jenner et al. 2010a).”
FR3D: finding local and composite recurrent structural motifs in RNA 3D structures (2007, background): “The database of atomic-resolution RNA 3D structures is growing rapidly [6,7,11,21] and now includes ribozymes [1,14,25], ribosomal subunits [3,16,44] and intact 70S ribosomes [42].”
rrnDB: documenting the number of rRNA and tRNA genes in bacteria and archaea (2008, background): “Crystal structures of this ribonucleoprotein complex reveal a catalytic center that consists primarily of ribosomal RNAs (rRNA) (1).”
GTP hydrolysis by IF2 guides progression of the ribosome into elongation (2009, background): “…domains, such as the 30S head and 50S L1 and L7/L12 stalk regions (Figure 1) (Carter et al., 2001; Allen et al., 2005; Myasnikov et al., 2005; Dallas and Noller, 2001; Pioletti et al., 2001; Schuwirth et al., 2005; Agrawal et al., 1999; Stark et al., 2000; Ogle et al., 2001; Harms et al., 2001).”
Initiation factor 2 stabilizes the ribosome in a semirotated conformation (2015, background): “The open conformation of the L1 stalk corresponds to the ribosome with a vacant 50S E site (2, 34).”