 |
PDBsum entry 2dzn
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Protein binding
|
PDB id
|
|
|
|
2dzn
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Structural basis for the recognition between the regulatory particles nas6 and rpt3 of the yeast 26s proteasome.
|
 |
|
Authors
|
 |
Y.Nakamura,
T.Umehara,
A.Tanaka,
M.Horikoshi,
B.Padmanabhan,
S.Yokoyama.
|
 |
|
Ref.
|
 |
Biochem Biophys Res Commun, 2007,
359,
503-509.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
The 26S proteasome-dependent protein degradation is an evolutionarily conserved
process. The mammalian oncoprotein gankyrin, which associates with S6 of the
proteasome, facilitates the degradation of pRb, and thus possibly acts as a
bridging factor between the proteasome and its substrates. However, the
mechanism of the proteasome-dependent protein degradation in yeast is poorly
understood. Here, we report the tertiary structure of the complex between Nas6
and a C-terminal domain of Rpt3, which are the yeast orthologues of gankyrin and
S6, respectively. The concave region of Nas6 bound to the alpha-helical domain
of Rpt3. The stable interaction between Nas6 and Rpt3 was mediated by
intermolecular interactions composed of complementary charged patches. The
recognition of Rpt3 by Nas6 in the crystal suggests that Nas6 is indeed a
subunit of the 26S proteasome. These results provide a structural basis for the
association between Nas6 and the heterohexameric ATPase ring of the proteasome
through Rpt3.
|
 |
|
|
|
|
 |