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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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Nmr structure of minor s5a (196-306):k48 linked diubiquitin species
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Structure:
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26s proteasome non-atpase regulatory subunit 4. Chain: a. Fragment: unp residues 196-306, s5a fragment. Synonym: 26s proteasome regulatory subunit s5a, rpn10, multiubiquitin chain-binding protein, antisecretory factor 1, asf, af. Engineered: yes. Ubiquitin. Chain: b, c. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: psmd4, mcb1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: rps27a, uba80, ubcep1, uba52, ubcep2, ubb, ubc.
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NMR struc:
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7 models
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Authors:
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N.Zhang,Q.Wang,A.Ehlinger,L.Randles,J.W.Lary,Y.Kang,A.Haririnia, J.L.Cole,D.Fushman,K.J.Walters
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Key ref:
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N.Zhang
et al.
(2009).
Structure of the s5a:k48-linked diubiquitin complex and its interactions with rpn13.
Mol Cell,
35,
280-290.
PubMed id:
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Date:
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06-Jan-09
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Release date:
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01-Sep-09
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PROCHECK
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Headers
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References
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Mol Cell
35:280-290
(2009)
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PubMed id:
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Structure of the s5a:k48-linked diubiquitin complex and its interactions with rpn13.
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N.Zhang,
Q.Wang,
A.Ehlinger,
L.Randles,
J.W.Lary,
Y.Kang,
A.Haririnia,
A.J.Storaska,
J.L.Cole,
D.Fushman,
K.J.Walters.
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ABSTRACT
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Degradation by the proteasome typically requires substrate ubiquitination. Two
ubiquitin receptors exist in the proteasome, S5a/Rpn10 and Rpn13. Whereas Rpn13
has only one ubiquitin-binding surface, S5a binds ubiquitin with two independent
ubiquitin-interacting motifs (UIMs). Here, we use nuclear magnetic resonance
(NMR) and analytical ultracentrifugation to define at atomic level resolution
how S5a binds K48-linked diubiquitin, in which K48 of one ubiquitin subunit (the
"proximal" one) is covalently bonded to G76 of the other (the
"distal" subunit). We demonstrate that S5a's UIMs bind the two
subunits simultaneously with a preference for UIM2 binding to the proximal
subunit while UIM1 binds to the distal one. In addition, NMR experiments reveal
that Rpn13 and S5a bind K48-linked diubiquitin simultaneously with subunit
specificity, and a model structure of S5a and Rpn13 bound to K48-linked
polyubiquitin is provided. Altogether, our data demonstrate that S5a is highly
adaptive and cooperative toward binding ubiquitin chains.
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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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M.Bieri,
A.H.Kwan,
M.Mobli,
G.F.King,
J.P.Mackay,
and
P.R.Gooley
(2011).
Macromolecular NMR spectroscopy for the non-spectroscopist: beyond macromolecular solution structure determination.
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FEBS J,
278,
704-715.
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A.Bremm,
S.M.Freund,
and
D.Komander
(2010).
Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne.
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Nat Struct Mol Biol,
17,
939-947.
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PDB code:
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A.Peth,
T.Uchiki,
and
A.L.Goldberg
(2010).
ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation.
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Mol Cell,
40,
671-681.
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A.X.Song,
C.J.Zhou,
Y.Peng,
X.C.Gao,
Z.R.Zhou,
Q.S.Fu,
J.Hong,
D.H.Lin,
and
H.Y.Hu
(2010).
Structural transformation of the tandem ubiquitin-interacting motifs in ataxin-3 and their cooperative interactions with ubiquitin chains.
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PLoS One,
5,
e13202.
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C.Riedinger,
J.Boehringer,
J.F.Trempe,
E.D.Lowe,
N.R.Brown,
K.Gehring,
M.E.Noble,
C.Gordon,
and
J.A.Endicott
(2010).
Structure of Rpn10 and its interactions with polyubiquitin chains and the proteasome subunit Rpn12.
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J Biol Chem,
285,
33992-34003.
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PDB code:
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F.Ikeda,
N.Crosetto,
and
I.Dikic
(2010).
What determines the specificity and outcomes of ubiquitin signaling?
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Cell,
143,
677-681.
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F.Liu,
and
K.J.Walters
(2010).
Multitasking with ubiquitin through multivalent interactions.
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Trends Biochem Sci,
35,
352-360.
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H.Wu,
Y.C.Lo,
and
S.C.Lin
(2010).
Recent advances in polyubiquitin chain recognition.
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F1000 Biol Rep,
2,
1-5.
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J.F.Trempe,
N.R.Brown,
M.E.Noble,
and
J.A.Endicott
(2010).
A new crystal form of Lys48-linked diubiquitin.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
66,
994-998.
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PDB code:
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J.M.Winget,
and
T.Mayor
(2010).
The diversity of ubiquitin recognition: hot spots and varied specificity.
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Mol Cell,
38,
627-635.
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X.Chen,
B.H.Lee,
D.Finley,
and
K.J.Walters
(2010).
Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2.
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Mol Cell,
38,
404-415.
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PDB codes:
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D.Zhang,
T.Chen,
I.Ziv,
R.Rosenzweig,
Y.Matiuhin,
V.Bronner,
M.H.Glickman,
and
D.Fushman
(2009).
Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.
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Mol Cell,
36,
1018-1033.
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I.Dikic,
S.Wakatsuki,
and
K.J.Walters
(2009).
Ubiquitin-binding domains - from structures to functions.
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Nat Rev Mol Cell Biol,
10,
659-671.
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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.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
