title: Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex.
abstract: The mRNA codon in the ribosomal A-site is recognized by aminoacyl-tRNA (aa-tRNA) in a ternary complex with elongation factor Tu (EF-Tu) and GTP. Here we report the 13 A resolution three-dimensional reconstruction determined by cryo-electron microscopy of the kirromycin-stalled codon-recognition complex. The structure of the ternary complex is distorted by binding of the tRNA anticodon arm in the decoding center. The aa-tRNA interacts with 16S rRNA, helix 69 of 23S rRNA and proteins S12 and L11, while the sarcin-ricin loop of 23S rRNA contacts domain 1 of EF-Tu near the nucleotide-binding pocket. These results provide a detailed snapshot view of an important functional state of the ribosome and suggest mechanisms of decoding and GTPase activation.
authors.affiliation: Max-Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany. holger.stark@mpibpc.mpg.de
authors.forename: Holger
authors.initials: H
authors.lastname: Stark
authors.forename: Marina V
authors.initials: MV
authors.lastname: Rodnina
authors.forename: Hans-Joachim
authors.initials: HJ
authors.lastname: Wieden
authors.forename: Friedrich
authors.initials: F
authors.lastname: Zemlin
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Wintermeyer
authors.forename: Marin
authors.initials: M
authors.lastname: van Heel
mesh_terms: D003062:Codon / Q000378:metabolism*; D004926:Escherichia coli; D046911:Macromolecular Substances; D009690:Nucleic Acid Conformation; D010444:Peptide Elongation Factor Tu / Q000378:metabolism*; D014176:Protein Biosynthesis / Q000502:physiology*; D017434:Protein Structure, Tertiary; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D003062:Codon; D046911:Macromolecular Substances; D012346:RNA, Transfer, Amino Acyl; D010444:Peptide Elongation Factor Tu