Structural Insights into the Regulatory Particle of the Proteasome from Methanocaldococcus jannaschii

Journal Article · Thu Jan 01 04:00:00 EST 2009 · Molecular Cell

DOI:https://doi.org/10.1016/j.molcel.2009.04.021· OSTI ID:980528

Zhang, F; Hu, M; Tian, G; Zhang, P; Finley, D; Jeffrey, P; Shi, Y

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.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 980528
• Report Number(s): BNL--93446-2010-JA
• Journal Information: Molecular Cell, Journal Name: Molecular Cell Journal Issue: 4 Vol. 34
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
ARCHITECTURE
ASYMMETRY
CRYSTAL STRUCTURE
ELEMENTS
NUCLEOTIDASES
PARTICLES
POTENTIALS
PYRIDYLAZONAPHTHOL
RINGS
SUBSTRATES
TRANSLOCATION
national synchrotron light source