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PDBsum entry 1nm7
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Protein transport
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PDB id
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1nm7
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Contents |
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* Residue conservation analysis
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DOI no:
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J Mol Biol
326:1427-1435
(2003)
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PubMed id:
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The ScPex13p SH3 domain exposes two distinct binding sites for Pex5p and Pex14p.
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J.R.Pires,
X.Hong,
C.Brockmann,
R.Volkmer-Engert,
J.Schneider-Mergener,
H.Oschkinat,
R.Erdmann.
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ABSTRACT
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Pex13p is an essential component of the peroxisomal protein import machinery and
interacts via its C-terminal SH3 domain with the type II SH3-ligand Pex14p and
the non-PXXP protein Pex5p. We report the solution structure of the SH3 domain
of Pex13p from Saccharomyces cerevisiae and the identification of a
novel-binding pocket, which binds a non-PXXP-peptide representing the binding
site of Pex5p. Chemical shift assays revealed the binding sites for Pex5p and
Pex14p ligand peptides to be distinct and spatially separated. Competition
assays demonstrated that the two ligand peptides can bind simultaneously to the
SH3 domain.
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Selected figure(s)
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Figure 2.
Figure 2. Identification of the SH3-binding fragments of
Pex5p and Pex14p. (A) Two hybrid interactions of
Pex13p[aa285-386] and various fragments of ScPex5p. Interactions
were analyzed by the b-galactosidase filter assay. (B) Cellulose
membranes decorated with 26-mer peptides covering amino acid
residues 181-312 of ScPex5p with one-amino acid shifts between
neighboring peptides and (C) 12-mer peptides covering the entire
protein sequence of ScPex14p with three-amino acid shifts
between neighboring peptides were incubated with the recombinant
GST-tagged SH3 domain of ScPex13p. Peptide-SH3complexes were
identified by the peptide spot overlay assay using antibodies
against GST.
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Figure 6.
Figure 6. ScPex13p SH3 domain-binding sites for Pex5p and
Pex14p. Domain surface and ribbon representation. Only residues
showing strong chemical shift changes upon addition of Pex14p
(red) and Pex5p (blue) are colored.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2003,
326,
1427-1435)
copyright 2003.
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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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S.Dutta,
and
K.Rittinger
(2010).
Regulation of NOXO1 activity through reversible interactions with p22 and NOXA1.
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PLoS One,
5,
e10478.
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T.Lanyon-Hogg,
S.L.Warriner,
and
A.Baker
(2010).
Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes.
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Biol Cell,
102,
245-263.
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J.Vyas,
R.J.Nowling,
M.W.Maciejewski,
S.Rajasekaran,
M.R.Gryk,
and
M.R.Schiller
(2009).
A proposed syntax for Minimotif Semantics, version 1.
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BMC Genomics,
10,
360.
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R.Tonikian,
X.Xin,
C.P.Toret,
D.Gfeller,
C.Landgraf,
S.Panni,
S.Paoluzi,
L.Castagnoli,
B.Currell,
S.Seshagiri,
H.Yu,
B.Winsor,
M.Vidal,
M.B.Gerstein,
G.D.Bader,
R.Volkmer,
G.Cesareni,
D.G.Drubin,
P.M.Kim,
S.S.Sidhu,
and
C.Boone
(2009).
Bayesian modeling of the yeast SH3 domain interactome predicts spatiotemporal dynamics of endocytosis proteins.
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PLoS Biol,
7,
e1000218.
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R.Volkmer
(2009).
Synthesis and application of peptide arrays: quo vadis SPOT technology.
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Chembiochem,
10,
1431-1442.
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K.Ma,
J.G.Forbes,
G.Gutierrez-Cruz,
and
K.Wang
(2006).
Titin as a giant scaffold for integrating stress and Src homology domain 3-mediated signaling pathways: the clustering of novel overlap ligand motifs in the elastic PEVK segment.
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J Biol Chem,
281,
27539-27556.
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M.R.Schiller,
K.Chakrabarti,
G.F.King,
N.I.Schiller,
B.A.Eipper,
and
M.W.Maciejewski
(2006).
Regulation of RhoGEF activity by intramolecular and intermolecular SH3 domain interactions.
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J Biol Chem,
281,
18774-18786.
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PDB code:
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A.Schell-Steven,
K.Stein,
M.Amoros,
C.Landgraf,
R.Volkmer-Engert,
H.Rottensteiner,
and
R.Erdmann
(2005).
Identification of a novel, intraperoxisomal pex14-binding site in pex13: association of pex13 with the docking complex is essential for peroxisomal matrix protein import.
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Mol Cell Biol,
25,
3007-3018.
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A.le Maire,
T.Weber,
S.Saunier,
I.Broutin,
C.Antignac,
A.Ducruix,
and
F.Dardel
(2005).
Solution NMR structure of the SH3 domain of human nephrocystin and analysis of a mutation-causing juvenile nephronophthisis.
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Proteins,
59,
347-355.
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PDB code:
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C.Reichman,
K.Singh,
Y.Liu,
S.Singh,
H.Li,
J.E.Fajardo,
A.Fiser,
and
R.B.Birge
(2005).
Transactivation of Abl by the Crk II adapter protein requires a PNAY sequence in the Crk C-terminal SH3 domain.
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Oncogene,
24,
8187-8199.
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I.Heiland,
and
R.Erdmann
(2005).
Biogenesis of peroxisomes. Topogenesis of the peroxisomal membrane and matrix proteins.
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FEBS J,
272,
2362-2372.
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R.J.Wanders,
and
H.R.Waterham
(2005).
Peroxisomal disorders I: biochemistry and genetics of peroxisome biogenesis disorders.
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Clin Genet,
67,
107-133.
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J.Moyersoen,
J.Choe,
E.Fan,
W.G.Hol,
and
P.A.Michels
(2004).
Biogenesis of peroxisomes and glycosomes: trypanosomatid glycosome assembly is a promising new drug target.
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FEMS Microbiol Rev,
28,
603-643.
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N.Shimozawa,
T.Tsukamoto,
T.Nagase,
Y.Takemoto,
N.Koyama,
Y.Suzuki,
M.Komori,
T.Osumi,
G.Jeannette,
R.J.Wanders,
and
N.Kondo
(2004).
Identification of a new complementation group of the peroxisome biogenesis disorders and PEX14 as the mutated gene.
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Hum Mutat,
23,
552-558.
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L.A.Brown,
and
A.Baker
(2003).
Peroxisome biogenesis and the role of protein import.
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J Cell Mol Med,
7,
388-400.
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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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}
}
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