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Signal transduction
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PDB id
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1cey
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Contents |
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* Residue conservation analysis
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PDB id:
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Signal transduction
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Title:
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Assignments, secondary structure, global fold, and dynamics of chemotaxis y protein using three-and four-dimensional heteronuclear (13c,15n) nmr spectroscopy
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Structure:
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Chey. Chain: a. Engineered: yes
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Source:
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Escherichia coli. Organism_taxid: 562.
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NMR struc:
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46 models
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Authors:
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F.J.Moy,D.F.Lowry,P.Matsumura,F.W.Dahlquist,J.E.Krywko, P.J.Domaille
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Key ref:
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F.J.Moy
et al.
(1994).
Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy.
Biochemistry,
33,
10731-10742.
PubMed id:
DOI:
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Date:
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23-Nov-94
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Release date:
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07-Feb-95
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PROCHECK
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Headers
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References
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P0AE67
(CHEY_ECOLI) -
Chemotaxis protein CheY
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Seq:
Struc:
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129 a.a.
128 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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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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Biochemistry
33:10731-10742
(1994)
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PubMed id:
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Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy.
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F.J.Moy,
D.F.Lowry,
P.Matsumura,
F.W.Dahlquist,
J.E.Krywko,
P.J.Domaille.
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ABSTRACT
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NMR spectroscopy has been used to study recombinant Escherichia coli CheY, a
128-residue protein involved in regulating bacterial chemotaxis. Heteronuclear
three- and four-dimensional (3D and 4D) experiments have provided
sequence-specific resonance assignments and quantitation of short-, medium-, and
long-range distance restraints from nuclear Overhauser enhancement (NOE)
intensities. These distance restraints were further supplemented with
measurements of three-bond scalar coupling constants to define the local
dihedral angles, and with the identification of amide protons undergoing slow
solvent exchange from which hydrogen-bonding patterns were identified. The
current model structure shows the same global fold of CheY as existing X-ray
structures (Volz & Matsumura, 1991; Stock et al. 1993) with a (beta/alpha)5
motif of five parallel beta-strands at the central core surrounded by three
alpha-helices on one face and with two on the opposite side. Heteronuclear
15N-1H relaxation experiments are interpreted to show portions of the protein
structure in the Mg2+ binding loop are ill-defined because of slow motion
(chemical exchange) on the NMR time scale. Moreover, the presence of Mg2+
disrupts the salt bridge between the highly conserved Lys-109 and Asp-57, the
site of phosphorylation.
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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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|
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K.Itoh,
and
M.Sasai
(2011).
Statistical mechanics of protein allostery: roles of backbone and side-chain structural fluctuations.
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J Chem Phys, 134,
125102.
|
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|
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K.Itoh,
and
M.Sasai
(2010).
Entropic mechanism of large fluctuation in allosteric transition.
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Proc Natl Acad Sci U S A, 107,
7775-7780.
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M.H.Knaggs,
F.R.Salsbury,
M.H.Edgell,
and
J.S.Fetrow
(2007).
Insights into correlated motions and long-range interactions in CheY derived from molecular dynamics simulations.
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Biophys J, 92,
2062-2079.
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C.M.Dyer,
and
F.W.Dahlquist
(2006).
Switched or not?: the structure of unphosphorylated CheY bound to the N terminus of FliM.
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J Bacteriol, 188,
7354-7363.
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PDB code:
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M.A.Seeliger,
M.Spichty,
S.E.Kelly,
M.Bycroft,
S.M.Freund,
M.Karplus,
and
L.S.Itzhaki
(2005).
Role of conformational heterogeneity in domain swapping and adapter function of the Cks proteins.
|
| |
J Biol Chem, 280,
30448-30459.
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T.J.Lowery,
M.Doucleff,
E.J.Ruiz,
S.M.Rubin,
A.Pines,
and
D.E.Wemmer
(2005).
Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR.
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Protein Sci, 14,
848-855.
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PDB code:
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J.G.Smith,
J.A.Latiolais,
G.P.Guanga,
J.D.Pennington,
R.E.Silversmith,
and
R.B.Bourret
(2004).
A search for amino acid substitutions that universally activate response regulators.
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Mol Microbiol, 51,
887-901.
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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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R.E.Silversmith,
G.P.Guanga,
L.Betts,
C.Chu,
R.Zhao,
and
R.B.Bourret
(2003).
CheZ-mediated dephosphorylation of the Escherichia coli chemotaxis response regulator CheY: role for CheY glutamate 89.
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J Bacteriol, 185,
1495-1502.
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PDB code:
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B.Ma,
M.Shatsky,
H.J.Wolfson,
and
R.Nussinov
(2002).
Multiple diverse ligands binding at a single protein site: a matter of pre-existing populations.
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Protein Sci, 11,
184-197.
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S.Kumar,
and
R.Nussinov
(2002).
Relationship between ion pair geometries and electrostatic strengths in proteins.
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Biophys J, 83,
1595-1612.
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V.Guillet,
N.Ohta,
S.Cabantous,
A.Newton,
and
J.P.Samama
(2002).
Crystallographic and biochemical studies of DivK reveal novel features of an essential response regulator in Caulobacter crescentus.
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J Biol Chem, 277,
42003-42010.
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PDB codes:
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B.F.Volkman,
D.Lipson,
D.E.Wemmer,
and
D.Kern
(2001).
Two-state allosteric behavior in a single-domain signaling protein.
|
| |
Science, 291,
2429-2433.
|
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M.Buck,
and
M.K.Rosen
(2001).
Structural biology. Flipping a switch.
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| |
Science, 291,
2329-2330.
|
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M.P.Allen,
K.B.Zumbrennen,
and
W.R.McCleary
(2001).
Genetic evidence that the alpha5 helix of the receiver domain of PhoB is involved in interdomain interactions.
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| |
J Bacteriol, 183,
2204-2211.
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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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P.Gouet,
B.Fabry,
V.Guillet,
C.Birck,
L.Mourey,
D.Kahn,
and
J.P.Samama
(1999).
Structural transitions in the FixJ receiver domain.
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| |
Structure, 7,
1517-1526.
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PDB codes:
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T.L.Mayover,
C.J.Halkides,
and
R.C.Stewart
(1999).
Kinetic characterization of CheY phosphorylation reactions: comparison of P-CheA and small-molecule phosphodonors.
|
| |
Biochemistry, 38,
2259-2271.
|
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C.J.Halkides,
X.Zhu,
D.P.Phillion,
P.Matsumura,
and
F.W.Dahlquist
(1998).
Synthesis and biochemical characterization of an analogue of CheY-phosphate, a signal transduction protein in bacterial chemotaxis.
|
| |
Biochemistry, 37,
13674-13680.
|
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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.
|
| |
J Bacteriol, 180,
3563-3569.
|
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K.C.Usher,
A.F.de la Cruz,
F.W.Dahlquist,
R.V.Swanson,
M.I.Simon,
and
S.J.Remington
(1998).
Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability.
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| |
Protein Sci, 7,
403-412.
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PDB codes:
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M.M.McEvoy,
A.C.Hausrath,
G.B.Randolph,
S.J.Remington,
and
F.W.Dahlquist
(1998).
Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway.
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| |
Proc Natl Acad Sci U S A, 95,
7333-7338.
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PDB code:
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M.Welch,
N.Chinardet,
L.Mourey,
C.Birck,
and
J.P.Samama
(1998).
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY.
|
| |
Nat Struct Biol, 5,
25-29.
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PDB code:
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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.
|
| |
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.
|
| |
Annu Rev Cell Dev Biol, 13,
457-512.
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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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I.Baikalov,
I.Schröder,
M.Kaczor-Grzeskowiak,
K.Grzeskowiak,
R.P.Gunsalus,
and
R.E.Dickerson
(1996).
Structure of the Escherichia coli response regulator NarL.
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Biochemistry, 35,
11053-11061.
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PDB code:
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M.A.Danielson,
and
J.J.Falke
(1996).
Use of 19F NMR to probe protein structure and conformational changes.
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Annu Rev Biophys Biomol Struct, 25,
163-195.
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Madhusudan,
J.Zapf,
J.M.Whiteley,
J.A.Hoch,
N.H.Xuong,
and
K.I.Varughese
(1996).
Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis.
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Structure, 4,
679-690.
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PDB code:
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R.V.Swanson,
M.G.Sanna,
and
M.I.Simon
(1996).
Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima.
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J Bacteriol, 178,
484-489.
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A.M.Stock,
and
S.L.Mowbray
(1995).
Bacterial chemotaxis: a field in motion.
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Curr Opin Struct Biol, 5,
744-751.
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R.V.Swanson,
D.F.Lowry,
P.Matsumura,
M.M.McEvoy,
M.I.Simon,
and
F.W.Dahlquist
(1995).
Localized perturbations in CheY structure monitored by NMR identify a CheA binding interface.
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Nat Struct Biol, 2,
906-910.
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V.A.Feher,
J.W.Zapf,
J.A.Hoch,
F.W.Dahlquist,
J.M.Whiteley,
and
J.Cavanagh
(1995).
1H, 15N, and 13C backbone chemical shift assignments, secondary structure, and magnesium-binding characteristics of the Bacillus subtilis response regulator, Spo0F, determined by heteronuclear high-resolution NMR.
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Protein Sci, 4,
1801-1814.
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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
