1MJ1 | pdb_00001mj1

FITTING THE TERNARY COMPLEX OF EF-Tu/tRNA/GTP AND RIBOSOMAL PROTEINS INTO A 13 A CRYO-EM MAP OF THE COLI 70S RIBOSOME

Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 13.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Starting Models: experimental
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This is version 1.4 of the entry. See complete history. 


Literature

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) Nat Struct Biol 9: 849-854

  • DOI: https://doi.org/10.1038/nsb859
  • Primary Citation of Related Structures:  
    1MJ1

  • 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.

    • Organizational Affiliation: 

    Max-Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany. holger.stark@mpibpc.mpg.de


Macromolecules

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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Elongation Factor TuE [auth A]405Escherichia coliMutation(s): 0 
UniProt
Find proteins for Q01698 (Thermus aquaticus)
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Go to UniProtKB:  Q01698
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UniProt GroupQ01698
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
S12 ribosomal proteinF [auth O]135Escherichia coliMutation(s): 0 
UniProt
Find proteins for Q5SHN3 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
S13 ribosomal proteinG [auth P]126Escherichia coliMutation(s): 0 
UniProt
Find proteins for P80377 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
L11 ribosomal proteinH [auth L]141Escherichia coliMutation(s): 0 
UniProt
Find proteins for P29395 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
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Go to UniProtKB:  P29395
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UniProt GroupP29395
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 13.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONIMAGIC

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-11-01
    Type: Initial release
  • Version 1.1: 2008-04-28
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Non-polymer description, Version format compliance
  • Version 1.3: 2018-07-18
    Changes: Data collection
  • Version 1.4: 2024-02-14
    Changes: Data collection, Database references, Derived calculations, Refinement description