Evidence and sources

Measurements

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Big picture numbers

Structures

• 1RYP
  Yeast 20S core particle

  The reference core particle. Two copies of each of the 14 subunits build the (alpha1-7 beta1-7)2 barrel. X-ray diffraction, 1.9 Å.
• 1G0U
  Yeast 20S, gated channel

  The gated-channel structure. No subunit mutation is recorded, so it shows the gate of the wild-type core. X-ray diffraction, 2.4 Å.
• 2F16
  Yeast 20S with bortezomib

  Shows which subunits the clinical drug blocks, and how a boronic acid binds the N-terminal threonine. X-ray diffraction, 2.8 Å.
• 5LE5
  Human 20S core particle

  The human core at 1.8 A, for a species comparison with yeast. X-ray diffraction, 1.8 Å.
• 5LF3
  Human 20S with bortezomib

  The drug bound to the human target. It anchors the subunit numbering used for human inhibitor design. X-ray diffraction, 2.1 Å.
• 1PMA
  Archaeal 20S proteasome

  The simplest core particle: two subunit types, 14 copies each. It shows the ancestral state of the barrel. X-ray diffraction, 3.4 Å.
• 6MSB
  Human 26S proteasome, state EA1

  One of seven states from a single substrate-engaged sample. State EA1 is a frame of the translocation cycle and shares chain names with the other six. Electron microscopy, 3 Å.
• 6MSD
  Human 26S proteasome, state EA2

  One of seven states from a single substrate-engaged sample. State EA2 is a frame of the translocation cycle and shares chain names with the other six. Electron microscopy, 3.2 Å.
• 6MSE
  Human 26S proteasome, state EB

  One of seven states from a single substrate-engaged sample. State EB is a frame of the translocation cycle and shares chain names with the other six. Electron microscopy, 3.3 Å.
• 6MSG
  Human 26S proteasome, state EC1

  One of seven states from a single substrate-engaged sample. State EC1 is a frame of the translocation cycle and shares chain names with the other six. Electron microscopy, 3.5 Å.
• 6MSH
  Human 26S proteasome, state EC2

  One of seven states from a single substrate-engaged sample. State EC2 is a frame of the translocation cycle and shares chain names with the other six. Electron microscopy, 3.6 Å.
• 6MSJ
  Human 26S proteasome, state ED1

  One of seven states from a single substrate-engaged sample. State ED1 is a frame of the translocation cycle and shares chain names with the other six. Electron microscopy, 3.3 Å.
• 6MSK
  Human 26S proteasome, state ED2

  One of seven states from a single substrate-engaged sample. State ED2 is a frame of the translocation cycle and shares chain names with the other six. Electron microscopy, 3.2 Å.
• 6EF3
  Yeast 26S proteasome with ubiquitinated substrate

  The yeast holoenzyme caught on a substrate, for a species comparison with the human states. Electron microscopy, 4.17 Å.

References

1. 1Groll et al., Nature 1997
2. 2Loewe et al., Science 1995
3. 3Seemueller et al., Science 1995
4. 4Groll et al., Nature Structural Biology 2000
5. 5Groll et al., Structure 2006
6. 6Schrader et al., Science 2016
7. 7Smith et al., Molecular Cell 2007
8. 8Rabl et al., Molecular Cell 2008
9. 9Lander et al., Nature 2012
10. 10Dong et al., Nature 2019
11. 11de la Pena et al., Science 2018
12. 12Bard et al., Annual Review of Biochemistry 2018
13. 13Bard et al., Cell 2019
14. 14Kisselev et al., Journal of Biological Chemistry 1999
15. 15Peth et al., Journal of Biological Chemistry 2013
16. 16Sakamoto et al., PNAS 2001
17. 17Winter et al., Science 2015
18. 18Zengerle et al., ACS Chemical Biology 2015
19. 19Gadd et al., Nature Chemical Biology 2017
20. 20Kroenke et al., Science 2014
21. 21Lu et al., Science 2014
22. 22Fischer et al., Nature 2014
23. 23Ito et al., Science 2010
24. 24Nabet et al., Nature Chemical Biology 2018
25. 25Nishimura et al., Nature Methods 2009
26. 26Arkinson et al., Nature Structural & Molecular Biology 2025