 |
PDBsum entry 1vsy
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
243 a.a.
|
|
|
|
|
|
|
|
|
|
|
231 a.a.
|
|
|
|
|
|
|
|
|
|
|
232 a.a.
|
|
|
|
|
|
|
|
|
|
|
227 a.a.
|
|
|
|
|
|
|
|
|
|
|
250 a.a.
|
|
|
|
|
|
|
|
|
|
|
234 a.a.
|
|
|
|
|
|
|
|
|
|
|
244 a.a.
|
|
|
|
|
|
|
|
|
|
|
196 a.a.
|
|
|
|
|
|
|
|
|
|
|
222 a.a.
|
|
|
|
|
|
|
|
|
|
|
204 a.a.
|
|
|
|
|
|
|
|
|
|
|
198 a.a.
|
|
|
|
|
|
|
|
|
|
|
212 a.a.
|
|
|
|
|
|
|
|
|
|
|
222 a.a.
|
|
|
|
|
|
|
|
|
|
|
233 a.a.
|
|
|
|
|
|
|
|
|
|
|
76 a.a.
|
|
|
|
|
|
|
|
|
|
|
799 a.a.
|
|
|
|
|
|
|
|
|
|
|
997 a.a.
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structure of a blm10 complex reveals common mechanisms for proteasome binding and gate opening.
|
|
|
Authors
|
|
K.Sadre-Bazzaz,
F.G.Whitby,
H.Robinson,
T.Formosa,
C.P.Hill.
|
|
|
Ref.
|
|
Mol Cell, 2010,
37,
728-735.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The proteasome is an abundant protease that is critically important for numerous
cellular pathways. Proteasomes are activated in vitro by three known classes of
proteins/complexes, including Blm10/PA200. Here, we report a 3.4 A resolution
crystal structure of a proteasome-Blm10 complex, which reveals that Blm10
surrounds the proteasome entry pore in the 1.2 MDa complex to form a largely
closed dome that is expected to restrict access of potential substrates. This
architecture and the observation that Blm10 induces a disordered proteasome gate
structure challenge the assumption that Blm10 functions as an activator of
proteolysis in vivo. The Blm10 C terminus binds in the same manner as seen for
11S activators and inferred for 19S/PAN activators and indicates a unified model
for gate opening. We also demonstrate that Blm10 acts to maintain mitochondrial
function. Consistent with the structural data, the C-terminal residues of Blm10
are needed for this activity.
|
|
|
|
|
|
|
