PMID:12379845: Difference between revisions

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<span style = 'font-size: large'> '''Stark, H, Rodnina, MV, Wieden, HJ, Zemlin, F, Wintermeyer, W and van Heel, M'''  (2002) Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex.''Nat. Struct. Biol.'' '''9''':849-54</span>
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|{{TableHeadingColor}} |'''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.
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'''Stark, H, Rodnina, MV, Wieden, HJ, Zemlin, F, Wintermeyer, W and van Heel, M'''  (2002) Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex. ''Nat. Struct. Biol.'' '''9''':849-54
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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.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12379845 PubMed]
Online version:[http://dx.doi.org/10.1038/nsb859 10.1038/nsb859]
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|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12379845 PubMed]
!align=left  |Keywords
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Codon/metabolism; Escherichia coli; Macromolecular Substances; Nucleic Acid Conformation; Peptide Elongation Factor Tu/metabolism; Protein Biosynthesis/physiology; Protein Structure, Tertiary; RNA, Transfer, Amino Acyl/metabolism; Ribosomes/metabolism; Ribosomes/ultrastructure
 
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Latest revision as of 04:18, 15 September 2013

Citation

Stark, H, Rodnina, MV, Wieden, HJ, Zemlin, F, Wintermeyer, W and van Heel, M (2002) Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex. Nat. Struct. Biol. 9:849-54

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.

Links

PubMed Online version:10.1038/nsb859

Keywords

Codon/metabolism; Escherichia coli; Macromolecular Substances; Nucleic Acid Conformation; Peptide Elongation Factor Tu/metabolism; Protein Biosynthesis/physiology; Protein Structure, Tertiary; RNA, Transfer, Amino Acyl/metabolism; Ribosomes/metabolism; Ribosomes/ultrastructure

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