A gated channel into the proteasome core particle - PubMed (original) (raw)
A gated channel into the proteasome core particle
M Groll et al. Nat Struct Biol. 2000 Nov.
Abstract
The core particle (CP) of the yeast proteasome is composed of four heptameric rings of subunits arranged in a hollow, barrel-like structure. We report that the CP is autoinhibited by the N-terminal tails of the outer (alpha) ring subunits. Crystallographic analysis showed that deletion of the tail of the alpha 3-subunit opens a channel into the proteolytically active interior chamber of the CP, thus derepressing peptide hydrolysis. In the latent state of the particle, the tails prevent substrate entry by imposing topological closure on the CP. Inhibition by the alpha-subunit tails is relieved upon binding of the regulatory particle to the CP to form the proteasome holoenzyme.
Comment in
- Opening doors into the proteasome.
Pickart CM, VanDemark AP. Pickart CM, et al. Nat Struct Biol. 2000 Nov;7(11):999-1001. doi: 10.1038/81018. Nat Struct Biol. 2000. PMID: 11062549 No abstract available. - The substrate translocation channel of the proteasome.
[No authors listed] [No authors listed] Biochimie. 2002 Apr;84(4):354. Biochimie. 2002. PMID: 12572557 No abstract available.
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