3H43

N-terminal domain of the proteasome-activating nucleotidase of Methanocaldococcus jannaschii

Summary for 3H43

• Entry DOI: 10.2210/pdb3h43/pdb
• Related: 3H4M 3H4P
• Descriptor: Proteasome-activating nucleotidase (2 entities in total)
• Functional Keywords: proteasome, regulatory particle, nucleosidase, atp-binding, cytoplasm, nucleotide-binding, hydrolase
• Biological source: Methanocaldococcus jannaschii (Methanococcus jannaschii)
• Cellular location: Cytoplasm: Q58576
• Total number of polymer chains: 12
• Total formula weight: 117083.57

Authors

Jeffrey, P.D.,Zhang, F.,Hu, M.,Tian, G.,Zhang, P.,Finley, D.,Shi, Y. (deposition date: 2009-04-17, release date: 2009-06-09, Last modification date: 2024-10-30)

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 (2.1 Å)