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PDBsum entry 1fwp
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References listed in PDB file
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Key reference
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Title
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Structure and dynamics of a chey-Binding domain of the chemotaxis kinase chea determined by nuclear magnetic resonance spectroscopy.
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Authors
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M.M.Mcevoy,
D.R.Muhandiram,
L.E.Kay,
F.W.Dahlquist.
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Ref.
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Biochemistry, 1996,
35,
5633-5640.
[DOI no: ]
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PubMed id
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Abstract
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The Escherichia coli histidine autokinase CheA plays an important role in
coupling signals received from membrane-bound receptors to changes in the
swimming behavior of the cells in order to respond appropriately to
environmental signals. Here we describe the structure of the 14 kDa fragment of
the chemotaxis kinase CheA, residues 124--257, which binds to the downstream
targets of phosphorylation, the response regulators CheY and CheB. This protein
fragment contains the CheY-binding domain flanked on each side by regions that
correspond to domain linkers in the intact protein. The structure of the domain
was determined from 1429 restraints derived from heteronuclear multidimensional
NMR experiments. Hybrid distance geometry--dynamical simulated annealing methods
were used to calculate a family of structures that satisfy the experimental
distance restraints and torsion angle restraints. The root mean square deviation
of the 69 ordered residues in the domain is 0.52 A for the backbone heavy atoms
and 0.99 A for all heavy atoms. The residues that have been implicated as
important for CheY binding form a face consisting of several partially buried
hydrophobic residues, framed by charged residues. The dynamic properties of this
protein fragment were measured and analyzed using both isotropic and anisotropic
models of molecular motion. The linker regions are very flexible and disordered,
as evidenced by the very dynamics properties as compared to the CheY-binding
domain. The CheY-binding domain of CheA is structurally similar to the
histidine-containing phosphocarrier, HPr, which is a protein involved in the
phosphoenolpyruvate:sugar phosphotransferase (PTS) pathway. This structural
similarity suggests a possible evolutionary relationship of the PTS and
chemotaxis pathways.
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Secondary reference #1
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Title
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Nuclear magnetic resonance assignments and global fold of a chey-Binding domain in chea, The chemotaxis-Specific kinase of escherichia coli.
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Authors
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M.M.Mcevoy,
H.Zhou,
A.F.Roth,
D.F.Lowry,
T.B.Morrison,
L.E.Kay,
F.W.Dahlquist.
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Ref.
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Biochemistry, 1995,
34,
13871-13880.
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PubMed id
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