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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

Summary for 1MJ1
Entry DOI10.2210/pdb1mj1/pdb
EMDB information1004
DescriptorPhe-tRNA, sarcin-ricin loop of 23SrRNA, helix 69 of 23S rRNA, ... (7 entities in total)
Functional Keywords70s ribosome, low resolution model ternary complex, ef-tu, ribosome
Biological sourceEscherichia coli
More
Total number of polymer chains8
Total formula weight162273.77
Authors
Stark, H.,Rodnina, M.V.,Wieden, H.-J.,Zemlin, F.,Wintermeyer, W.,Vanheel, M. (deposition date: 2002-08-26, release date: 2002-11-01, Last modification date: 2024-02-14)
Primary citationStark, H.,Rodnina, M.V.,Wieden, H.-J.,Zemlin, F.,Wintermeyer, W.,van Heel, M.
Ribosome Interactions of Aminoacyl-tRNA and Elongation Factor TU in the Codon Recognition Complex
Nat.Struct.Biol., 9:849-854, 2002
Cited by
PubMed 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.
PubMed: 12379845
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (13 Å)
Structure validation

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