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Signal transduction
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PDB id
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1cye
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Contents |
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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cytoplasm
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1 term
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Biological process
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intracellular signal transduction
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7 terms
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Biochemical function
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two-component response regulator activity
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3 terms
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DOI no:
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J Mol Biol
247:717-725
(1995)
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PubMed id:
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Three-dimensional structure of chemotactic Che Y protein in aqueous solution by nuclear magnetic resonance methods.
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J.Santoro,
M.Bruix,
J.Pascual,
E.López,
L.Serrano,
M.Rico.
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ABSTRACT
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The three-dimensional structure of chemotactic Che Y protein from Escherichia
coli in aqueous solution has been determined by nuclear magnetic resonance (NMR)
spectroscopy combined with restrained molecular dynamics calculations. A total
of 20 converged structures were computed from 1545 conformationally relevant
distance restraints derived from 1858 unambiguously assigned NOE
cross-correlations. The resulting average pairwise root-mean-square deviation is
1.03 A for the backbone atoms and 1.69 A for all heavy atoms. If residues in the
regions structurally least defined (1 to 5, 47 to 50, 76 to 79, 88 to 91 and 124
to 129) are excluded from the analysis, the root-mean-square deviations are
reduced to 0.53 A and 1.23 A, respectively. The solution structure is closely
similar to the refined X-ray crystal structure, except in the regions found to
be less defined by NMR spectroscopy. The root-mean-square deviation between the
average solution structure and the X-ray crystal structure is 0.92 A for the
backbone residues (2 to 129). The highly refined solution structure determined
herewith provides an essential background to delineate functionally important
conformational changes brought about by different effectors.
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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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J.A.Hubbard,
L.K.MacLachlan,
G.W.King,
J.J.Jones,
and
A.P.Fosberry
(2003).
Nuclear magnetic resonance spectroscopy reveals the functional state of the signalling protein CheY in vivo in Escherichia coli.
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Mol Microbiol, 49,
1191-1200.
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P.Garcia,
L.Serrano,
M.Rico,
and
M.Bruix
(2002).
An NMR view of the folding process of a CheY mutant at the residue level.
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Structure, 10,
1173-1185.
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P.Garcia,
L.Serrano,
D.Durand,
M.Rico,
and
M.Bruix
(2001).
NMR and SAXS characterization of the denatured state of the chemotactic protein CheY: implications for protein folding initiation.
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Protein Sci, 10,
1100-1112.
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A.M.Stock,
V.L.Robinson,
and
P.N.Goudreau
(2000).
Two-component signal transduction.
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Annu Rev Biochem, 69,
183-215.
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D.Yan,
H.S.Cho,
C.A.Hastings,
M.M.Igo,
S.Y.Lee,
J.G.Pelton,
V.Stewart,
D.E.Wemmer,
and
S.Kustu
(1999).
Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators.
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Proc Natl Acad Sci U S A, 96,
14789-14794.
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J.L.Appleby,
and
R.B.Bourret
(1999).
Activation of CheY mutant D57N by phosphorylation at an alternative site, Ser-56.
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Mol Microbiol, 34,
915-925.
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D.Wilcock,
M.T.Pisabarro,
E.López-Hernandez,
L.Serrano,
and
M.Coll
(1998).
Structure analysis of two CheY mutants: importance of the hydrogen-bond contribution to protein stability.
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Acta Crystallogr D Biol Crystallogr, 54,
378-385.
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PDB codes:
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J.L.Appleby,
and
R.B.Bourret
(1998).
Proposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator active-site quintet.
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J Bacteriol, 180,
3563-3569.
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R.Ramakrishnan,
M.Schuster,
and
R.B.Bourret
(1998).
Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY.
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Proc Natl Acad Sci U S A, 95,
4918-4923.
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J.J.Falke,
R.B.Bass,
S.L.Butler,
S.A.Chervitz,
and
M.A.Danielson
(1997).
The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes.
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Annu Rev Cell Dev Biol, 13,
457-512.
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M.Bruix,
V.Muñoz,
R.Campos-Olivas,
J.R.Del Bosque,
L.Serrano,
and
M.Rico
(1997).
Characterisation of the isolated Che Y C-terminal fragment (79-129)--Exploring the structure/stability/folding relationship of the alpha/beta parallel protein Che Y.
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Eur J Biochem, 243,
384-392.
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M.Madhusudan,
J.Zapf,
J.A.Hoch,
J.M.Whiteley,
N.H.Xuong,
and
K.I.Varughese
(1997).
A response regulatory protein with the site of phosphorylation blocked by an arginine interaction: crystal structure of Spo0F from Bacillus subtilis.
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Biochemistry, 36,
12739-12745.
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PDB code:
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V.A.Feher,
J.W.Zapf,
J.A.Hoch,
J.M.Whiteley,
L.P.McIntosh,
M.Rance,
N.J.Skelton,
F.W.Dahlquist,
and
J.Cavanagh
(1997).
High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition.
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Biochemistry, 36,
10015-10025.
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PDB codes:
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V.Muñoz,
F.J.Blanco,
and
L.Serrano
(1995).
The distribution of alpha-helix propensity along the polypeptide chain is not conserved in proteins from the same family.
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Protein Sci, 4,
1577-1586.
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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
