3H4P

Proteasome 20S core particle from Methanocaldococcus jannaschii

Summary for 3H4P

• Entry DOI: 10.2210/pdb3h4p/pdb
• Related: 3H43 3H4M
• Descriptor: Proteasome subunit alpha, Proteasome subunit beta (2 entities in total)
• Functional Keywords: 20s, proteasome, core particle, hydrolase, protease, threonine protease
• Biological source: Methanocaldococcus jannaschii (Methanococcus jannaschii); More
• Cellular location: Cytoplasm : Q60177 Q58634
• Total number of polymer chains: 28
• Total formula weight: 748086.99

Authors

Jeffrey, P.D.,Zhang, F.,Hu, M.,Tian, G.,Zhang, P.,Finley, D.,Shi, Y. (deposition date: 2009-04-20, release date: 2009-06-09, Last modification date: 2024-02-21)

Primary citation

Zhang, F.,Hu, M.,Tian, G.,Zhang, P.,Finley, D.,Jeffrey, P.D.,Shi, Y.
Structural Insights into the Regulatory Particle of the Proteasome from Methanocaldococcus jannaschii.
Mol.Cell, 34:473-484, 2009

PubMed Abstract: Eukaryotic proteasome consists of a core particle (CP), which degrades unfolded protein, and a regulatory particle (RP), which is responsible for recognition, ATP-dependent unfolding, and translocation of polyubiquitinated substrate protein. In the archaea Methanocaldococcus jannaschii, the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). Here, we report the crystal structures of essential elements of the archaeal proteasome: the CP, the ATPase domain of PAN, and a distal subcomplex that is likely the first to encounter substrate. The distal subcomplex contains a coiled-coil segment and an OB-fold domain, both of which appear to be conserved in the eukaryotic proteasome. The OB domains of PAN form a hexameric ring with a 13 A pore, which likely constitutes the outermost constriction of the substrate translocation channel. These studies reveal structural codes and architecture of the complete proteasome, identify potential substrate-binding sites, and uncover unexpected asymmetry in the RP of archaea and eukaryotes.

PubMed: 19481527
DOI: 10.1016/j.molcel.2009.04.021

Experimental method

X-RAY DIFFRACTION (4.1 Å)