1G0U

A GATED CHANNEL INTO THE PROTEASOME CORE PARTICLE

Summary for 1G0U

• Entry DOI: 10.2210/pdb1g0u/pdb
• Related: 1RYP
• Descriptor: PROTEASOME COMPONENT Y7, PROTEASOME COMPONENT C11, PROTEASOME COMPONENT PRE2, ... (16 entities in total)
• Functional Keywords: proteasome, ubiquitin, degradation, protease, ntn-hydrolase, hydrolase
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Cytoplasm: P23639 P22141 P30656 P23724 P30657 P38624 P23638 P40303 P32379 P40302 P21242 P21243 P25043 P25451
• Total number of polymer chains: 28
• Total formula weight: 718944.35

Authors

Groll, M.,Bajorek, M.,Kohler, A.,Moroder, L.,Rubin, D.M.,Huber, R.,Glickman, M.H.,Finley, D. (deposition date: 2000-10-09, release date: 2000-11-06, Last modification date: 2024-02-07)

Primary citation

Groll, M.,Bajorek, M.,Kohler, A.,Moroder, L.,Rubin, D.M.,Huber, R.,Glickman, M.H.,Finley, D.
A gated channel into the proteasome core particle.
Nat.Struct.Biol., 7:1062-1067, 2000

PubMed 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.

PubMed: 11062564
DOI: 10.1038/80992

Experimental method

X-RAY DIFFRACTION (2.4 Å)