PloS one, 2013-03, Vol.8 (3), p.e58829-e58829
2013
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Details
- Autor(en) / Beteiligte
- Titel
- Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex
- Ist Teil von
- PloS one, 2013-03, Vol.8 (3), p.e58829-e58829
- Ort / Verlag
- United States: Public Library of Science
- Erscheinungsjahr
- 2013
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- During the translation cycle, a cognate deacylated tRNA can only move together with the codon into the E site. We here present the first structure of a cognate tRNA bound to the ribosomal E site resulting from translocation by EF-G, in which an entire L1 stalk (L1 protein and L1 rRNA) interacts with E-site tRNA (E-tRNA), representing an authentic ribosome elongation complex. Our results revealed that the Watson-Crick base pairing is formed at the first and second codon-anticodon positions in the E site in the ribosome elongation complex, whereas the codon-anticodon interaction in the third position is indirect. Analysis of the observed conformations of mRNA and E-tRNA suggests that the ribosome intrinsically has the potential to form codon-anticodon interaction in the E site, independently of the mRNA configuration. We also present a detailed description of the biologically relevant position of the entire L1 stalk and its interacting cognate E-tRNA, which provides a better understanding of the structural basis for translation elongation. Furthermore, to gain insight into translocation, we report the positioning of protein L6 contacting EF-G, as well as the conformational change of the C-terminal tail of protein S13 in the decoding center.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1932-6203eISSN: 1932-6203DOI: 10.1371/journal.pone.0058829Titel-ID: cdi_plos_journals_1330889471
- Format
- –
- Schlagworte
- Antibiotics, Biology, Codon, Codons, Crystal structure, Decoding, Elongated structure, L1 protein, Models, Molecular, mRNA, Multiprotein Complexes - chemistry, Multiprotein Complexes - metabolism, Nucleic Acid Conformation, Peptide Chain Elongation, Translational - physiology, Peptide Elongation Factors - chemistry, Peptide Elongation Factors - metabolism, Protein Binding, Protein Conformation, Protein synthesis, Proteins, Ribosome Subunits - chemistry, Ribosome Subunits - metabolism, RNA, Messenger - chemistry, RNA, Messenger - metabolism, RNA, Transfer - chemistry, RNA, Transfer - metabolism, rRNA, Science, Transfer RNA, Translation, Translation elongation, Translocation, tRNA