PMID:12379845: Difference between revisions
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| | !align=left |Citation | ||
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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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!align=left |Abstract | |||
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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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|{{ | !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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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
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==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
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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