@article{144906,
  keywords = {Models, Molecular, Crystallography, X-Ray, Protein Structure, Tertiary, Molecular Sequence Data, RNA, Bacterial, Binding Sites, Ligands, Amino Acid Sequence, Ribosomes, Ribosomal Proteins, Thermus thermophilus},
  author = {Albert Weixlbaumer and Sabine Petry and Christine Dunham and Maria Selmer and Ann Kelley and Ramakrishnan},
  title = {Crystal structure of the ribosome recycling factor bound to the ribosome},
  abstract = {<p>In bacteria, disassembly of the ribosome at the end of translation is facilitated by an essential protein factor termed ribosome recycling factor (RRF), which works in concert with elongation factor G. Here we describe the crystal structure of the Thermus thermophilus RRF bound to a 70S ribosomal complex containing a stop codon in the A site, a transfer RNA anticodon stem-loop in the P site and tRNA(fMet) in the E site. The work demonstrates that structures of translation factors bound to 70S ribosomes can be determined at reasonably high resolution. Contrary to earlier reports, we did not observe any RRF-induced changes in bridges connecting the two subunits. This suggests that such changes are not a direct requirement for or consequence of RRF binding but possibly arise from the subsequent stabilization of a hybrid state of the ribosome.</p>
},
  year = {2007},
  journal = {Nat Struct Mol Biol},
  volume = {14},
  pages = {733-7},
  month = {08/2007},
  issn = {1545-9993},
  doi = {10.1038/nsmb1282},
  language = {eng},
}