Molecular Machinery
← GroEL–GroES

Evidence and sources

Each number on the GroEL–GroES 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

EstimateSakikawa 1999, opens the source in a new tab
MeasuredKerner 2005, opens the source in a new tabBNID 110575, opens the source in a new tabBNID 110576, opens the source in a new tabBNID 110579, opens the source in a new tab
MeasuredKerner 2005, opens the source in a new tabBNID 110575, opens the source in a new tabBNID 110576, opens the source in a new tabBNID 110579, opens the source in a new tab
MeasuredEwalt 1997, opens the source in a new tab
MeasuredFayet 1989, opens the source in a new tab
MeasuredCheng 1989, opens the source in a new tabHansen 2002, opens the source in a new tab

Structures

  • 1XCK
    Apo GroEL tetradecamer
    Wild-type apo GroEL at 2.92 A. It is the start state for every cage-opening morph. X-ray diffraction, 2.92 Å.
  • 1OEL
    Apo GroEL heptamer, T state
    The apo heptamer used as fit reference for the cryo-EM ATP states, so numbering matches them. X-ray diffraction, 2.8 Å.
  • 4AAQ
    GroEL-ATP7, Rs1 state
    First step after ATP binding. It starts the morph series to the GroES-bound cage. Electron microscopy, 8 Å.
  • 4AAR
    GroEL-ATP7, Rs2 state
    Second step of apical-domain motion, same chain numbering as the other ATP states. Electron microscopy, 8 Å.
  • 4AAS
    GroEL-ATP7, Rs-open state
    The open state that can hold substrate and still dock GroES. Electron microscopy, 8.5 Å.
  • 1AON
    GroEL-GroES-(ADP)7 bullet
    The folding chamber itself. It is the end state of the cage-opening morph. X-ray diffraction, 3 Å.
  • 1SVT
    GroEL-GroES-(ADP-AlFx)7
    Traps the hydrolysis step inside the capped cis ring. X-ray diffraction, 2.808 Å.
  • 1KP8
    GroEL with ATP analogue in all 14 subunits
    High-resolution view of the nucleotide pocket with K+ and Mg2+ in place. X-ray diffraction, 2 Å.
  • 4PKO
    GroEL-GroES2 football
    Shows that both rings can carry GroES at the same time. X-ray diffraction, 3.84 Å.
  • 2CGT
    GroEL with phage co-chaperonin gp31
    A natural cage-size variant: gp31 builds a larger chamber than GroES. Electron microscopy, 8.2 Å.
  • 1G31
    Phage T4 gp31 heptamer
    The lid part on its own, for comparing GroES and gp31 geometry. X-ray diffraction, 2.3 Å.
  • 4PJ1
    Human mitochondrial HSP60-HSP10 football
    The human group I chaperonin, for a species comparison with GroEL. X-ray diffraction, 3.15 Å.
  • 1A6D
    Archaeal thermosome, group II chaperonin
    A group II chaperonin that closes with its own apical lid and needs no GroES. X-ray diffraction, 2.6 Å.

References

  1. 1Braig et al., Nature 1994
  2. 2Xu et al., Nature 1997
  3. 3Rye et al., Nature 1997
  4. 4Rye et al., Cell 1999
  5. 5Burston et al., Journal of Molecular Biology 1995
  6. 6Todd et al., Science 1994
  7. 7Weissman et al., Cell 1995
  8. 8Weissman et al., Cell 1996
  9. 9Clare et al., Cell 2012
  10. 10Clare et al., Journal of Molecular Biology 2006
  11. 11Tang et al., Cell 2006
  12. 12Sakikawa et al., Journal of Biological Chemistry 1999
  13. 13Kerner et al., Cell 2005
  14. 14Hunt et al., Cell 1997
  15. 15Ditzel et al., Cell 1998
  16. 16Nisemblat et al., PNAS 2015
  17. 17Yang et al., PNAS 2013
  18. 18Wang et al., Cell 2002
  19. 19Hayer-Hartl et al., Trends in Biochemical Sciences 2016
  20. 20Horwich et al., Quarterly Reviews of Biophysics 2009
  21. 21Bartolucci et al., Journal of Molecular Biology 2005
  22. 22King et al., Nature 2014
  23. 23Bale et al., Science 2016
  24. 24Hsia et al., Nature 2016