Structure of 20S proteasome from yeast at 2.4Å resolution

@article{Groll1997StructureO2,
  title={Structure of 20S proteasome from yeast at 2.4{\AA} resolution},
  author={Michael Groll and Lars Ditzel and Jan L{\"o}we and Daniela Stock and Matthias Bochtler and Hans D. Bartunik and Robert Huber},
  journal={Nature},
  year={1997},
  volume={386},
  pages={463-471}
}
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… Expand
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References

SHOWING 1-10 OF 52 REFERENCES
Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.
The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement andExpand
Autocatalytic processing of the 20S proteasome
TLDR
It is shown that propeptide processing in the proteasome from Thermoplasma acidophilum is indeed autocatalytic, but is probably intermolecular. Expand
Autocatalytic Subunit Processing Couples Active Site Formation in the 20S Proteasome to Completion of Assembly
TLDR
It is shown that the N-terminal propeptide is required for Doa3 incorporation into the proteasome and, remarkably, that the propeptides functions in trans, suggesting it serves a chaperone-like function in proteasomesome biogenesis. Expand
Structure and functions of the 20S and 26S proteasomes.
TLDR
Major advances have been achieved recently in knowledge about the molecular organization of the 20S and 19S particles, their subunits, the proteasome's role in MHC-class 1 antigen presentation, and regulators of its activities. Expand
PA28 activator protein forms regulatory caps on proteasome stacked rings.
The proteasome is a 700,000 dalton proteolytic complex found in eukaryotes and, in a simpler form, in archaebacteria. Its distinctive architecture consists of a stack of four rings, each containingExpand
Biogenesis, structure and function of the yeast 20S proteasome.
TLDR
Unexpectedly, the yeast Doa3 and Pre3 subunits are synthesized as precursors which are processed in a manner apparently identical to that of related mammalian proteasome subunits implicated in antigen presentation, suggesting that biogenesis of the proteasomes particle is highly conserved between yeast and mammals. Expand
Analysis of mammalian 20S proteasome biogenesis: the maturation of beta‐subunits is an ordered two‐step mechanism involving autocatalysis.
TLDR
A model for self‐activation of proteasomal beta‐subunits is proposed in which residue Thr1 serves as nucleophile and Lys33 as proton donor/acceptor and evidence that subunit processing of mammalian beta‐ subunits proceeds via a novel ordered two‐step mechanism involving autocatalysis is provided. Expand
MHC-linked LMP gene products specifically alter peptidase activities of the proteasome
TLDR
It is found that pro-teasomes of both types have endopeptidase activity against sub-strates bearing hydrophobic, basic or acidic residues immediately preceding the cleavage site (the PI position) and at sites following asparagine, glycine and proline residues. Expand
PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core.
The 20S proteasome of eukaryotes is an abundant multicatalytic/multifunctional proteinase complex composed of an array of nonidentical subunits which are encoded by alpha- or beta-type members of theExpand
Activation of the multicatalytic protease. The 11 S regulator and 20 S ATPase complexes contain distinct 30-kilodalton subunits.
TLDR
The multicatalytic protease associates with a 20 S ATPase complex in the presence of ATP to form the 26 S ubiquitin/ATP-dependent protease, a uniform 3-fold activation of peptide hydrolysis by MCP. Expand
...
1
2
3
4
5
...