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* Residue conservation analysis
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PDB id:
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Gene regulation/signaling protein
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Title:
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Crystal structure of the mouse rap80 uims in complex with lys63-linked di-ubiquitin
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Structure:
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Ubiquitin. Chain: a, d. Engineered: yes. Mutation: yes. Ubiquitin. Chain: b, e. Engineered: yes. Mutation: yes. Ubiquitin interaction motif-containing protein 1.
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Source:
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Mus musculus. Mouse. Organism_taxid: 10090. Gene: rps27a, uba80, ubcep1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: uimc1, rip110, rxrip110.
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Resolution:
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2.20Å
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R-factor:
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0.216
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R-free:
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0.268
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Authors:
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Y.Sato,A.Yoshikawa,H.Mimura,M.Yamashita,A.Yamagata,S.Fukai
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Key ref:
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Y.Sato
et al.
(2009).
Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by tandem UIMs of RAP80.
Embo J,
28,
2461-2468.
PubMed id:
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Date:
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21-Apr-09
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Release date:
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21-Jul-09
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PROCHECK
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Headers
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References
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P0CG50
(UBC_MOUSE) -
Polyubiquitin-C from Mus musculus
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Seq: Struc:
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734 a.a.
73 a.a.
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Embo J
28:2461-2468
(2009)
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PubMed id:
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Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by tandem UIMs of RAP80.
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Y.Sato,
A.Yoshikawa,
H.Mimura,
M.Yamashita,
A.Yamagata,
S.Fukai.
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ABSTRACT
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RAP80 has a key role in the recruitment of the Abraxas-BRCC36-BRCA1-BARD1
complex to DNA-damage foci for DNA repair through specific recognition of Lys
63-linked polyubiquitinated proteins by its tandem ubiquitin-interacting motifs
(UIMs). Here, we report the crystal structure of the RAP80 tandem UIMs
(RAP80-UIM1-UIM2) in complex with Lys 63-linked di-ubiquitin at 2.2 A
resolution. The two UIMs, UIM1 and UIM2, and the alpha-helical inter-UIM region
together form a continuous 60 A-long alpha-helix. UIM1 and UIM2 bind to the
proximal and distal ubiquitin moieties, respectively. Both UIM1 and UIM2 of
RAP80 recognize an Ile 44-centered hydrophobic patch on ubiquitin but neither
UIM interacts with the Lys 63-linked isopeptide bond. Our structure suggests
that the inter-UIM region forms a 12 A-long alpha-helix that ensures that the
UIMs are arranged to enable specific binding of Lys 63-linked di-ubiquitin. This
was confirmed by pull-down analyses using RAP80-UIM1-UIM2 mutants of various
length inter-UIM regions. Further, we show that the Epsin1 tandem UIM, which has
an inter-UIM region similar to that of RAP80-UIM1-UIM2, also selectively binds
Lys 63-linked di-ubiquitin.
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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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E.J.Davis,
C.Lachaud,
P.Appleton,
T.J.Macartney,
I.Näthke,
and
J.Rouse
(2012).
DVC1 (C1orf124) recruits the p97 protein segregase to sites of DNA damage.
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Nat Struct Mol Biol,
19,
1093-1100.
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R.Wiener,
X.Zhang,
T.Wang,
and
C.Wolberger
(2012).
The mechanism of OTUB1-mediated inhibition of ubiquitination.
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Nature,
483,
618-622.
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PDB codes:
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J.H.Hurley,
and
H.Stenmark
(2011).
Molecular mechanisms of ubiquitin-dependent membrane traffic.
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Annu Rev Biophys,
40,
119-142.
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S.Nakada
(2011).
Abnormalities in DNA double-strand break response beyond primary immunodeficiency.
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Int J Hematol,
93,
425-433.
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V.Bertelsen,
M.M.Sak,
K.Breen,
M.S.Rødland,
L.E.Johannessen,
L.M.Traub,
E.Stang,
and
I.H.Madshus
(2011).
A chimeric pre-ubiquitinated EGF receptor is constitutively endocytosed in a clathrin-dependent, but kinase-independent manner.
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Traffic,
12,
507-520.
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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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E.Lauwers,
Z.Erpapazoglou,
R.Haguenauer-Tsapis,
and
B.André
(2010).
The ubiquitin code of yeast permease trafficking.
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Trends Cell Biol,
20,
196-204.
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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.D.Ulrich,
and
H.Walden
(2010).
Ubiquitin signalling in DNA replication and repair.
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Nat Rev Mol Cell Biol,
11,
479-489.
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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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I.H.Ismail,
C.Andrin,
D.McDonald,
and
M.J.Hendzel
(2010).
BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair.
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J Cell Biol,
191,
45-60.
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J.B.Tang,
and
R.A.Greenberg
(2010).
Connecting the Dots: Interplay Between Ubiquitylation and SUMOylation at DNA Double Strand Breaks.
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Genes Cancer,
1,
787-796.
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M.Citarelli,
S.Teotia,
and
R.S.Lamb
(2010).
Evolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes.
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BMC Evol Biol,
10,
308.
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N.G.Sgourakis,
M.M.Patel,
A.E.Garcia,
G.I.Makhatadze,
and
S.A.McCallum
(2010).
Conformational dynamics and structural plasticity play critical roles in the ubiquitin recognition of a UIM domain.
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J Mol Biol,
396,
1128-1144.
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PDB code:
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S.G.Hymowitz,
and
I.E.Wertz
(2010).
A20: from ubiquitin editing to tumour suppression.
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Nat Rev Cancer,
10,
332-341.
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|
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E.Laplantine,
E.Fontan,
J.Chiaravalli,
T.Lopez,
G.Lakisic,
M.Véron,
F.Agou,
and
A.Israël
(2009).
NEMO specifically recognizes K63-linked poly-ubiquitin chains through a new bipartite ubiquitin-binding domain.
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EMBO J,
28,
2885-2895.
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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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K.J.Walters,
and
X.Chen
(2009).
Measuring ubiquitin chain linkage: Rap80 uses a molecular ruler mechanism for ubiquitin linkage specificity.
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EMBO J,
28,
2307-2308.
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L.M.Traub
(2009).
Tickets to ride: selecting cargo for clathrin-regulated internalization.
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Nat Rev Mol Cell Biol,
10,
583-596.
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T.E.Messick,
and
R.A.Greenberg
(2009).
The ubiquitin landscape at DNA double-strand breaks.
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J Cell Biol,
187,
319-326.
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Y.Sato,
A.Yoshikawa,
M.Yamashita,
A.Yamagata,
and
S.Fukai
(2009).
Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by NZF domains of TAB2 and TAB3.
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EMBO J,
28,
3903-3909.
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PDB codes:
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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
codes are
shown on the right.
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}
}
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