Molecular Machinery
← Ribosome

Evidence and sources

Each number on the Ribosome page goes back to an experiment or a calculation. Each card shows the result, how it was measured, and where it was published.

Measurements

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Big picture numbers

CalculatedCell Biology by the Numbers, opens the source in a new tabUniProt Q8WZ42, opens the source in a new tab
CalculatedCell Biology by the Numbers, opens the source in a new tabUniProt Q8WZ42, opens the source in a new tab
MeasuredBNID 107552, opens the source in a new tabBNID 107347, opens the source in a new tab
MeasuredPrinciotta 2003, opens the source in a new tabBNID 113783, opens the source in a new tab
EstimateMilo 2013, opens the source in a new tab
EstimateNorton 1981, opens the source in a new tabSchutz 2011, opens the source in a new tab

Structures

  • 8CVL
    70S ribosome with mRNA and A-, P- and E-site tRNAs
    One entry with all three tRNA sites filled, an mRNA and a nascent chain. It is the anchor for the elongation animation. X-ray diffraction, 2.3 Å.
  • 7K00
    E. coli 70S ribosome at 2 A
    The highest-resolution bacterial ribosome. It shows ions, polyamines and water around the RNA. The primary citation DOI could not be checked with Crossref in this session, so the DOI field is left empty. Electron microscopy, 1.98 Å.
  • 7N1P
    E. coli 70S, PRE-C
    Frame PRE-C of one translocation series. All six entries share chain names, so the ratchet and tRNA movement can morph. Electron microscopy, 2.33 Å.
  • 7N2U
    E. coli 70S, PRE-H1
    Frame PRE-H1 of one translocation series. All six entries share chain names, so the ratchet and tRNA movement can morph. Electron microscopy, 2.53 Å.
  • 7N30
    E. coli 70S, PRE-H2*
    Frame PRE-H2* of one translocation series. All six entries share chain names, so the ratchet and tRNA movement can morph. Electron microscopy, 2.66 Å.
  • 7N2V
    E. coli 70S, INT1
    Frame INT1 of one translocation series. All six entries share chain names, so the ratchet and tRNA movement can morph. Electron microscopy, 2.54 Å.
  • 7N2C
    E. coli 70S, INT2
    Frame INT2 of one translocation series. All six entries share chain names, so the ratchet and tRNA movement can morph. Electron microscopy, 2.72 Å.
  • 7N31
    E. coli 70S, POST
    Frame POST of one translocation series. All six entries share chain names, so the ratchet and tRNA movement can morph. Electron microscopy, 2.69 Å.
  • 4V5L
    70S with EF-Tu and aminoacyl-tRNA
    Shows how EF-Tu holds the incoming tRNA while the small subunit checks the codon pair. X-ray diffraction, 3.1 Å.
  • 6ND5
    70S with chloramphenicol
    Shows where chloramphenicol sits next to the catalytic centre, at 2.6 A. X-ray diffraction, 2.6 Å.
  • 6ND6
    70S with erythromycin
    The macrolide site in the exit tunnel, in the same crystal form as the chloramphenicol entry. X-ray diffraction, 2.85 Å.
  • 4V9A
    70S with tetracycline
    Places tetracycline on the small subunit, where it blocks tRNA binding in the A site. X-ray diffraction, 3.2999 Å.
  • 1FJG
    30S subunit with streptomycin, spectinomycin and paromomycin
    One entry with three aminoglycoside and aminocyclitol sites, for the drug layer of the small subunit. X-ray diffraction, 3 Å.
  • 6QZP
    Human 80S ribosome
    The human ribosome, with four rRNA chains and about 80 proteins. It shows what the drug-free eukaryotic machine looks like. Electron microscopy, 2.9 Å.
  • 4V88
    Yeast 80S ribosome
    The first complete eukaryotic ribosome at atomic resolution, and the reference for eukaryote-specific extensions. X-ray diffraction, 3 Å.
  • 3J9M
    Human mitochondrial ribosome
    A ribosome that lost 5S rRNA and gained many proteins. It shows how far the machine can drift inside one cell. Electron microscopy, 3.5 Å.
  • 1FFK
    Archaeal large subunit, 50S
    The structure that showed the catalytic centre is built from RNA alone, with no protein side chain nearby. X-ray diffraction, 2.4 Å.

References

  1. 1Ban et al., Science 2000
  2. 2Nissen et al., Science 2000
  3. 3Selmer et al., Science 2006
  4. 4Rheinberger, Sternbach and Nierhaus, PNAS 1981
  5. 5Moazed and Noller, Nature 1989
  6. 6Frank and Agrawal, Nature 2000
  7. 7Rundlet et al., Nature 2021
  8. 8Voorhees et al., Science 2010
  9. 9Carter et al., Nature 2000
  10. 10Young and Bremer, Biochemical Journal 1976
  11. 11Kramer and Farabaugh, RNA 2007
  12. 12Voss et al., Journal of Molecular Biology 2006
  13. 13Svetlov et al., RNA 2019
  14. 14Jenner et al., PNAS 2013
  15. 15Natchiar et al., Nature 2017
  16. 16Ben-Shem et al., Science 2011
  17. 17Amunts et al., Science 2015
  18. 18Syroegin et al., Nature Chemistry 2023
  19. 19Watson et al., eLife 2020
  20. 20Rackham and Chin, Nature Chemical Biology 2005
  21. 21Orelle et al., Nature 2015
  22. 22Neumann et al., Nature 2010
  23. 23Wang et al., Science 2001