 |
PDBsum entry 3h4p
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
(+ 8 more)
232 a.a.
|
|
|
|
|
|
|
|
|
|
|
(+ 8 more)
202 a.a.
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural insights into the regulatory particle of the proteasome from methanocaldococcus jannaschii.
|
|
|
Authors
|
|
F.Zhang,
M.Hu,
G.Tian,
P.Zhang,
D.Finley,
P.D.Jeffrey,
Y.Shi.
|
|
|
Ref.
|
|
Mol Cell, 2009,
34,
473-484.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
