| Literature DB >> 12379845 |
Holger Stark1, Marina V Rodnina, Hans-Joachim Wieden, Friedrich Zemlin, Wolfgang Wintermeyer, Marin van Heel.
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.Entities:
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Year: 2002 PMID： 12379845 DOI： 10.1038/nsb859
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368