Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex.
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.
Stark
Holger
H
Max-Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany. holger.stark@mpibpc.mpg.de
Rodnina
Marina V
MV
Wieden
Hans-Joachim
HJ
Zemlin
Friedrich
F
Wintermeyer
Wolfgang
W
van Heel
Marin
M
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
D003062:Codon; D046911:Macromolecular Substances; D012346:RNA, Transfer, Amino Acyl; D010444:Peptide Elongation Factor Tu