@article{144911,
  keywords = {Models, Molecular, Protein Conformation, Nucleic Acid Conformation, Magnesium, Crystallography, X-Ray, Bacterial Proteins, Crystallization, RNA, Bacterial, RNA, Messenger, Protein Biosynthesis, Ribosomes, RNA, Transfer, Ribosomal Proteins, Codon, Thermus thermophilus, Anticodon, Peptidyl Transferases, RNA, Transfer, Met, RNA, Transfer, Phe},
  author = {Maria Selmer and Christine Dunham and Frank Murphy and Albert Weixlbaumer and Sabine Petry and Ann Kelley and John Weir and Ramakrishnan},
  title = {Structure of the 70S ribosome complexed with mRNA and tRNA},
  abstract = {<p>The crystal structure of the bacterial 70S ribosome refined to 2.8 angstrom resolution reveals atomic details of its interactions with messenger RNA (mRNA) and transfer RNA (tRNA). A metal ion stabilizes a kink in the mRNA that demarcates the boundary between A and P sites, which is potentially important to prevent slippage of mRNA. Metal ions also stabilize the intersubunit interface. The interactions of E-site tRNA with the 50S subunit have both similarities and differences compared to those in the archaeal ribosome. The structure also rationalizes much biochemical and genetic data on translation.</p>
},
  year = {2006},
  journal = {Science},
  volume = {313},
  pages = {1935-42},
  month = {09/2006},
  issn = {1095-9203},
  doi = {10.1126/science.1131127},
  language = {eng},
}