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* Residue conservation analysis
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Enzyme class:
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E.C.2.7.11.1
- Non-specific serine/threonine protein kinase.
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Reaction:
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ATP + a protein = ADP + a phosphoprotein
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ATP
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+
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protein
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=
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ADP
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+
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phosphoprotein
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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J Mol Biol
342:681-693
(2004)
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PubMed id:
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The solution structure of the S.cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50.
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J.J.Kwan,
N.Warner,
T.Pawson,
L.W.Donaldson.
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ABSTRACT
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Ste11 is a MAPKKK from Saccharomyces cerevisiae that helps mediate the response
to mating pheromone and the ability to thrive in high-salt environments. These
diverse functions are facilitated by a direct interaction between the SAM domain
of Ste11 with the SAM domain of its regulatory partner, Ste50. We have solved
the NMR structure of the Ste11 SAM domain (PDB 1OW5), which reveals a compact,
five alpha-helix bundle and a high degree of structural similarity to the
Polyhomeotic SAM domain. The combined study of Ste11 SAM rotational correlation
times and crosslinking to Ste50-SAM has suggested a mode through which Ste11-SAM
oligomerizes and selectively associates with Ste50-SAM. To probe homotypic and
heterotypic interations, Ste11-SAM variants each containing a substitution of a
surface-exposed hydrophobic residue were constructed. An I59R variant of
Ste11-SAM, disrupted binding to Ste50-SAM in vitro. Yeast expressing full-length
Ste11-I59R could neither respond to mating pheromone nor thrive in high salt
media-demonstrating that the interaction between Ste11 and Ste50 SAM domains is
a prerequisite for key signal transduction events.
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Selected figure(s)
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Figure 2.
Figure 2. The tertiary structure of the Ste11[15-92] SAM
domain was determined by NMR. A, Best fit backbone
superimposition of 25 Ste11-SAM structures with the a-helices
denoted H1-H5. B, Surface amino acid substitutions that disrupt
binding partially (yellow) or fully (red) to Ste50-SAM are
highlighted in space-filling representation, those with binding
properties that were comparable to wild-type Ste11-SAM are
denoted in stick respresentation.
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Figure 3.
Figure 3. Combined 1H and 15N chemical-shift differences
between concentrated (0.7 mM) and dilute (0.2 mM) Ste11-SAM. A,
Differences above an arbitrary 8 Hz cut-off are highlighted. B,
With the exception of F28 (yellow), the major perturbations
(red) occur at either the EH surface (blue monomer) or ML
surface (purple monomer). C, A model of dimeric Ste11-SAM based
on the crystal structure of Ph-SAM.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2004,
342,
681-693)
copyright 2004.
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Figures were
selected
by the author.
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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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A.Bhunia,
P.N.Domadia,
H.Mohanram,
and
S.Bhattacharjya
(2009).
NMR structural studies of the Ste11 SAM domain in the dodecyl phosphocholine micelle.
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Proteins, 74,
328-343.
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A.D.Meruelo,
and
J.U.Bowie
(2009).
Identifying polymer-forming SAM domains.
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Proteins, 74,
1-5.
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B.D.Slaughter,
J.M.Huff,
W.Wiegraebe,
J.W.Schwartz,
and
R.Li
(2008).
SAM domain-based protein oligomerization observed by live-cell fluorescence fluctuation spectroscopy.
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PLoS ONE, 3,
e1931.
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T.Rajakulendran,
M.Sahmi,
I.Kurinov,
M.Tyers,
M.Therrien,
and
F.Sicheri
(2008).
CNK and HYP form a discrete dimer by their SAM domains to mediate RAF kinase signaling.
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Proc Natl Acad Sci U S A, 105,
2836-2841.
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PDB codes:
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H.Li,
K.L.Fung,
D.Y.Jin,
S.S.Chung,
Y.P.Ching,
I.O.Ng,
K.H.Sze,
B.C.Ko,
and
H.Sun
(2007).
Solution structures, dynamics, and lipid-binding of the sterile alpha-motif domain of the deleted in liver cancer 2.
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Proteins, 67,
1154-1166.
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PDB code:
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J.J.Kwan,
and
L.W.Donaldson
(2007).
The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle.
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BMC Struct Biol, 7,
34.
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C.Wu,
G.Jansen,
J.Zhang,
D.Y.Thomas,
and
M.Whiteway
(2006).
Adaptor protein Ste50p links the Ste11p MEKK to the HOG pathway through plasma membrane association.
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Genes Dev, 20,
734-746.
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D.M.Truckses,
J.E.Bloomekatz,
and
J.Thorner
(2006).
The RA domain of Ste50 adaptor protein is required for delivery of Ste11 to the plasma membrane in the filamentous growth signaling pathway of the yeast Saccharomyces cerevisiae.
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Mol Cell Biol, 26,
912-928.
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D.Shao,
W.Zheng,
W.Qiu,
Q.Ouyang,
and
C.Tang
(2006).
Dynamic studies of scaffold-dependent mating pathway in yeast.
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Biophys J, 91,
3986-4001.
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R.L.Rich,
and
D.G.Myszka
(2005).
Survey of the year 2004 commercial optical biosensor literature.
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J Mol Recognit, 18,
431-478.
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S.Bhattacharjya,
P.Xu,
M.Chakrapani,
L.Johnston,
and
F.Ni
(2005).
Polymerization of the SAM domain of MAPKKK Ste11 from the budding yeast: implications for efficient signaling through the MAPK cascades.
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Protein Sci, 14,
828-835.
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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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Links
