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PDBsum entry 1l2n
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Protein binding
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PDB id
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1l2n
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Contents |
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* Residue conservation analysis
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DOI no:
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Protein Sci
11:1482-1491
(2002)
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PubMed id:
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Solution structure of a yeast ubiquitin-like protein Smt3: the role of structurally less defined sequences in protein-protein recognitions.
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W.Sheng,
X.Liao.
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ABSTRACT
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Smt3 belongs to a growing family of ubiquitin-related proteins involved in
posttranslational protein modification. Independent studies demonstrate an
essential function of Smt3 in the regulation of nucleocytoplasmic transport, and
suggest a role in cell-cycle regulation. Here we report the high-resolution NMR
structure of yeast Smt3 in the complex free form. Our comparison of the Smt3 NMR
structure with the Smt3 crystal structure in complex with the C-Terminal Ulp1
protease domain revealed large structural differences in the binding surface,
which is also involved in the Smt3-Ubc-9 interaction detected by NMR. The
structural differences in the region indicate the important functions of
conserved residues in less structurally defined sequences.
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Selected figure(s)
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Figure 5.
Fig. 5. NMR structure of Smt3. (A) Stereo superposition of
20 selected conformers with the lowest target functions from the
final DYANA calculations. (B) A ribbon diagram showing the
NMR-derived tertiary structure used in this study. The average
structure was generated and analyzed by MolMol.
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Figure 7.
Fig. 7. A stereo diagram of the backbone C^  atom
coordinates of NMR solution structure of Smt3 (current
structure, red) overlaid with (A) that of SUMO-1 structure
(blue) obtained from heteronuclear NMR. (B) That of the X-ray
crystal structure of Smt3 (green) in complex with the C-Terminal
Ulp1 protease domain.
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The above figures are
reprinted
by permission from the Protein Society:
Protein Sci
(2002,
11,
1482-1491)
copyright 2002.
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Figures were
selected
by an automated process.
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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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Q.Shang,
C.Xu,
J.Zhang,
X.Zhang,
and
X.Tu
(2009).
Solution structure of SUMO from Trypanosoma brucei and its interaction with Ubc9.
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Proteins,
76,
266-269.
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PDB code:
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P.L.Andersen,
F.Xu,
and
W.Xiao
(2008).
Eukaryotic DNA damage tolerance and translesion synthesis through covalent modifications of PCNA.
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Cell Res,
18,
162-173.
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S.R.Hughes,
P.F.Dowd,
R.E.Hector,
T.Panavas,
D.E.Sterner,
N.Qureshi,
K.M.Bischoff,
S.S.Bang,
J.A.Mertens,
E.T.Johnson,
X.L.Li,
J.S.Jackson,
R.J.Caughey,
S.B.Riedmuller,
S.Bartolett,
S.Liu,
J.O.Rich,
P.J.Farrelly,
T.R.Butt,
J.Labaer,
and
M.A.Cotta
(2008).
Lycotoxin-1 insecticidal peptide optimized by amino acid scanning mutagenesis and expressed as a coproduct in an ethanologenic Saccharomyces cerevisiae strain.
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J Pept Sci,
14,
1039-1050.
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D.M.Duda,
R.C.van Waardenburg,
L.A.Borg,
S.McGarity,
A.Nourse,
M.B.Waddell,
M.A.Bjornsti,
and
B.A.Schulman
(2007).
Structure of a SUMO-binding-motif mimic bound to Smt3p-Ubc9p: conservation of a non-covalent ubiquitin-like protein-E2 complex as a platform for selective interactions within a SUMO pathway.
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J Mol Biol,
369,
619-630.
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PDB code:
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G.L.Moldovan,
B.Pfander,
and
S.Jentsch
(2007).
PCNA, the maestro of the replication fork.
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Cell,
129,
665-679.
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H.Ding,
Y.Yang,
J.Zhang,
J.Wu,
H.Liu,
and
Y.Shi
(2005).
Structural basis for SUMO-E2 interaction revealed by a complex model using docking approach in combination with NMR data.
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Proteins,
61,
1050-1058.
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PDB code:
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W.C.Huang,
T.P.Ko,
S.S.Li,
and
A.H.Wang
(2004).
Crystal structures of the human SUMO-2 protein at 1.6 A and 1.2 A resolution: implication on the functional differences of SUMO proteins.
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Eur J Biochem,
271,
4114-4122.
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PDB codes:
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J.S.Seeler,
and
A.Dejean
(2003).
Nuclear and unclear functions of SUMO.
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Nat Rev Mol Cell Biol,
4,
690-699.
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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
