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PDBsum entry 1k0s
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Signaling protein
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PDB id
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1k0s
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The solution structure and interactions of chew from thermotoga maritima.
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Authors
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I.J.Griswold,
H.Zhou,
M.Matison,
R.V.Swanson,
L.P.Mcintosh,
M.I.Simon,
F.W.Dahlquist.
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Ref.
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Nat Struct Biol, 2002,
9,
121-125.
[DOI no: ]
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PubMed id
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Abstract
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Using protein from the hyperthermophile Thermotoga maritima, we have determined
the solution structure of CheW, an essential component in the formation of the
bacterial chemotaxis signaling complex. The overall fold is similar to the
regulatory domain of the chemotaxis kinase CheA. In addition, interactions of
CheW with CheA were monitored by nuclear magnetic resonance (NMR) techniques.
The chemical shift perturbation data show the probable contacts that CheW makes
with CheA. In combination with previous genetic data, the structure also
suggests a possible binding site for the chemotaxis receptor. These results
provide a structural basis for a model in which CheW acts as a molecular bridge
between CheA and the cytoplasmic tails of the receptor.
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Figure 2.
Figure 2. Stereo view, topology diagram and superposition of
CheA and CheW. a, Stereo view showing the ensemble of
NMR-derived structures of CheW, with  -strands
in red and helices in blue. The 20 lowest energy structures
generated with CNS13 are superimposed to the mean. Disordered
regions of protein backbone were not used for the superposition.
b, Topology diagram of CheW showing the locations of secondary
structural elements within the primary sequence. -strands
are shown as red arrows; helices, as blue cylinders. c, Ribbon
diagram of CheW showing the superposition of the average
minimized NMR-derived structure of T. maritima CheW and CheA,
using homologous regions of secondary structure. The
superposition consists of CheW residues 10 -37, 51 -71, 79 -106,
124 -128 and 121 -141 from CheW (gold) and residues 538 -671
(543 -570, 581 -601, 610 -637, 652 -656 and 660 -670) from CheA
(blue). R.m.s. deviation of backbone atoms is 1.95 Å for
homologous regions. Residues corresponding to loops 1 and 2 and
the C-terminal helix of CheW are colored red. The stereo view
and ribbon diagrams were created with MOLMOL31, 32 and
RIBBONS33, respectively.
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Figure 4.
Figure 4. Ribbon diagrams and molecular surface representations
of CheW. a, Ribbon diagrams of the minimized average
structure of CheW. The two views are rotated 90° about the
x-axis. The order of the secondary structural elements is
indicated. Positions of absolutely conserved residues are shown
as balls; Gly 51, in red; and Arg 56, Gly 57, Gly 92 and Gly
124, in green. b, Chemical shift perturbations in CheW due to
binding of CheA^354 -671, mapped to a molecular surface
representation of CheW calculated from its minimized average
structure. Color ramp from white to red indicates 0 Hz to 150 Hz
change. Gray indicates no available data. c, Location of Tsr
repressor mutations (green) mapped onto the surface of CheW. d,
Combined map (a + b) of CheA interaction sites and repressor
mutations mapped to molecular surface of CheW. Overlap between
the two sites is shown in yellow. Surface representations were
created with GRASP34, after removal of the N-terminal nine amino
acids for clarity.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2002,
9,
121-125)
copyright 2002.
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