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TitleRibosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex.
Journal, issue, pagesNat Struct Biol, Vol. 9, Issue 11, Page 849-854, Year 2002
Publish dateNov 25, 2002
AuthorsHolger Stark / Marina V Rodnina / Hans-Joachim Wieden / Friedrich Zemlin / Wolfgang Wintermeyer / Marin van Heel /
PubMed AbstractThe 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 ...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.
External linksNat Struct Biol / PubMed:12379845
MethodsEM (single particle)
Resolution13.0 Å
Structure data

1004

1mj1

EMDB-1004: Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex.
PDB-1mj1: FITTING THE TERNARY COMPLEX OF EF-Tu/tRNA/GTP AND RIBOSOMAL PROTEINS INTO A 13 A CRYO-EM MAP OF THE COLI 70S RIBOSOME
Method: EM (single particle) / Resolution: 13.0 Å

Source
  • escherichia coli (E. coli)
KeywordsRIBOSOME / 70S RIBOSOME / LOW RESOLUTION MODEL TERNARY COMPLEX / EF-Tu

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