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Structure of 20S proteasome from yeast at 2.4Å resolution

Author

Listed:
  • Michael Groll
  • Lars Ditzel
  • Jan Löwe

    (MRC Laboratory of Molecular Biology)

  • Daniela Stock

    (MRC Laboratory of Molecular Biology)

  • Matthias Bochtler
  • Hans D. Bartunik

    (Arbeitsgruppen für strukturelle Molekularbiologie der Max-Planck-Gesellschaft)

  • Robert Huber

    (Max-Planck-Institut für Biochemie)

Abstract

The crystal structure of the 20S proteasome from the yeast Saccharomyces cerevisiae shows that its 28 protein subunits are arranged as an (α1...α7, β1...β7)2 complex in four stacked rings and occupy unique locations. The interior of the particle, which harbours the active sites, is only accessible by some very narrow side entrances. The β-type subunits are synthesized as proproteins before being proteolytically processed for assembly into the particle. The proforms of three of the seven different β-type subunits, (β1/PRE3, β2/PUP1 and β5/PRE2, are cleaved between the threonine at position 1 and the last glycine of the pro-sequence, with release of the active-site residue Thr 1. These three β-type subunits have inhibitor-binding sites, indicating that PRE2 has a chymotrypsin-like and a trypsin-like activity and that PRE3 has peptidylglutamyl peptide hydrolytic specificity. Other β-type subunits are processed to an intermediate form, indicating that an additional nonspecific endopeptidase activity may exist which is important for peptide hydrolysis and for the generation of ligands for class I molecules of the major histocompatibility complex.

Suggested Citation

  • Michael Groll & Lars Ditzel & Jan Löwe & Daniela Stock & Matthias Bochtler & Hans D. Bartunik & Robert Huber, 1997. "Structure of 20S proteasome from yeast at 2.4Å resolution," Nature, Nature, vol. 386(6624), pages 463-471, April.
    • Handle: RePEc:nat:nature:v:386:y:1997:i:6624:d:10.1038_386463a0
    DOI: 10.1038/386463a0
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    Cited by:

    1. Jingyu Zhan & Allison Zeher & Rick Huang & Wai Kwan Tang & Lisa M. Jenkins & Di Xia, 2024. "Conformations of Bcs1L undergoing ATP hydrolysis suggest a concerted translocation mechanism for folded iron-sulfur protein substrate," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Indrajit Sahu & Sachitanand M. Mali & Prasad Sulkshane & Cong Xu & Andrey Rozenberg & Roni Morag & Manisha Priyadarsini Sahoo & Sumeet K. Singh & Zhanyu Ding & Yifan Wang & Sharleen Day & Yao Cong & O, 2021. "The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag," Nature Communications, Nature, vol. 12(1), pages 1-21, December.
    3. Nathan Jespersen & Kai Ehrenbolger & Rahel R. Winiger & Dennis Svedberg & Charles R. Vossbrinck & Jonas Barandun, 2022. "Structure of the reduced microsporidian proteasome bound by PI31-like peptides in dormant spores," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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