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PDBsum entry 2dzn
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Protein binding
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PDB id
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2dzn
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Contents |
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* Residue conservation analysis
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PDB id:
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Protein binding
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Title:
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Crystal structure analysis of yeast nas6p complexed with the proteasome subunit, rpt3
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Structure:
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Probable 26s proteasome regulatory subunit p28. Chain: a, c, e. Synonym: nas6p, proteasome non-atpase subunit 6. Engineered: yes. 26s protease regulatory subunit 6b homolog. Chain: b, d, f. Fragment: c-terminal domain. Synonym: rpt3, protein ynt1, tat-binding homolog 2. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.20Å
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R-factor:
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0.197
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R-free:
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0.265
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Authors:
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S.Yokoyama,B.Padmanabhan,Riken Structural Genomics/proteomics Initiative (Rsgi)
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Key ref:
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Y.Nakamura
et al.
(2007).
Structural basis for the recognition between the regulatory particles Nas6 and Rpt3 of the yeast 26S proteasome.
Biochem Biophys Res Commun,
359,
503-509.
PubMed id:
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Date:
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29-Sep-06
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Release date:
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17-Jul-07
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PROCHECK
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Headers
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References
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P50086
(PSD10_YEAST) -
Probable 26S proteasome regulatory subunit p28 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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228 a.a.
226 a.a.
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Biochem Biophys Res Commun
359:503-509
(2007)
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PubMed id:
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Structural basis for the recognition between the regulatory particles Nas6 and Rpt3 of the yeast 26S proteasome.
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Y.Nakamura,
T.Umehara,
A.Tanaka,
M.Horikoshi,
B.Padmanabhan,
S.Yokoyama.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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N.Gallastegui,
and
M.Groll
(2010).
The 26S proteasome: assembly and function of a destructive machine.
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Trends Biochem Sci,
35,
634-642.
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D.Finley
(2009).
Recognition and processing of ubiquitin-protein conjugates by the proteasome.
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Annu Rev Biochem,
78,
477-513.
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F.Förster,
K.Lasker,
F.Beck,
S.Nickell,
A.Sali,
and
W.Baumeister
(2009).
An atomic model AAA-ATPase/20S core particle sub-complex of the 26S proteasome.
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Biochem Biophys Res Commun,
388,
228-233.
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J.Roelofs,
S.Park,
W.Haas,
G.Tian,
F.E.McAllister,
Y.Huo,
B.H.Lee,
F.Zhang,
Y.Shi,
S.P.Gygi,
and
D.Finley
(2009).
Chaperone-mediated pathway of proteasome regulatory particle assembly.
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Nature,
459,
861-865.
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K.Madura
(2009).
Cell biology: The proteasome assembly line.
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Nature,
459,
787-788.
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M.Funakoshi,
R.J.Tomko,
H.Kobayashi,
and
M.Hochstrasser
(2009).
Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base.
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Cell,
137,
887-899.
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S.Park,
J.Roelofs,
W.Kim,
J.Robert,
M.Schmidt,
S.P.Gygi,
and
D.Finley
(2009).
Hexameric assembly of the proteasomal ATPases is templated through their C termini.
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Nature,
459,
866-870.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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