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  Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex.

Stark, H., Rodnina, M. V., Wieden, H. J., Zemlin, F., Wintermeyer, W., & van Heel, M. (2002). Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex. Nature Structural Biology, 9(11), 849-854. Retrieved from http://www.nature.com/nsmb/journal/v9/n11/pdf/nsb859.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-4541-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-4545-3
Genre: Journal Article

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 Creators:
Stark, H.1, Author              
Rodnina, M. V., Author
Wieden, H. J., Author
Zemlin, F., Author
Wintermeyer, W.2, Author              
van Heel, M., Author
Affiliations:
1Research Group of 3D Electron Cryo-Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578577              
2Research Group of Ribosome Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578599              

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 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 Angstrom 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.

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Language(s): eng - English
 Dates: 2002-11
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
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Title: Nature Structural Biology
Source Genre: Journal
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Pages: - Volume / Issue: 9 (11) Sequence Number: - Start / End Page: 849 - 854 Identifier: -