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PDBsum entry 1b9m
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Transcription
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PDB id
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1b9m
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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 high-Resolution crystal structure of the molybdate-Dependent transcriptional regulator (mode) from escherichia coli: a novel combination of domain folds.
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Authors
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D.R.Hall,
D.G.Gourley,
G.A.Leonard,
E.M.Duke,
L.A.Anderson,
D.H.Boxer,
W.N.Hunter.
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Ref.
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EMBO J, 1999,
18,
1435-1446.
[DOI no: ]
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PubMed id
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Abstract
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The molybdate-dependent transcriptional regulator (ModE) from Escherichia coli
functions as a sensor of molybdate concentration and a regulator for
transcription of operons involved in the uptake and utilization of the essential
element, molybdenum. We have determined the structure of ModE using
multi-wavelength anomalous dispersion. Selenomethionyl and native ModE models
are refined to 1. 75 and 2.1 A, respectively and describe the architecture and
structural detail of a complete transcriptional regulator. ModE is a homodimer
and each subunit comprises N- and C-terminal domains. The N-terminal domain
carries a winged helix-turn-helix motif for binding to DNA and is primarily
responsible for ModE dimerization. The C-terminal domain contains the
molybdate-binding site and residues implicated in binding the oxyanion are
identified. This domain is divided into sub-domains a and b which have similar
folds, although the organization of secondary structure elements varies. The
sub-domain fold is related to the oligomer binding-fold and similar to that of
the subunits of several toxins which are involved in extensive protein-protein
interactions. This suggests a role for the C-terminal domain in the formation of
the ModE-protein-DNA complexes necessary to regulate transcription. Modelling of
ModE interacting with DNA suggests that a large distortion of DNA is not
necessary for complex formation.
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Figure 2.
Figure 2 Ribbon diagrams to depict the architecture of ModE. (A)
Domains I and II. The helices of the HTH motif of domain I are
coloured green. Sub-domains a and b of domain II are coloured
blue and yellow. Residues Arg128, Lys183 and Trp186 are shown as
sticks. (B) A ModE monomer. (C) The dimer with elements of
secondary structure at the C-terminal domain assigned to aid
orientation of this domain with respect to (A). Figures 2, 3, 4,
5 and 6 were generated with MOLSCRIPT (Kraulis, 1991) and
RASTER3D (Merritt and Murphy, 1994). (D) The amino acid sequence
with elements of secondary structure that have been assigned.
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Figure 6.
Figure 6 A model of ModE interacting with double helix DNA. The
DNA strands are purple and cyan, the palindromic DNA recognition
site is black.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(1999,
18,
1435-1446)
copyright 1999.
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Secondary reference #1
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Title
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Two crystal forms of mode, The molybdate-Dependent transcriptional regulator from escherichia coli.
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Authors
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D.R.Hall,
D.G.Gourley,
E.M.Duke,
G.A.Leonard,
L.A.Anderson,
R.N.Pau,
D.H.Boxer,
W.N.Hunter.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1999,
55,
542-543.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1 Crystals of ModE, form II.
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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Secondary reference #2
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Title
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Characterisation of the molybdenum-Responsive mode regulatory protein and its binding to the promoter region of the modabcd (molybdenum transport) operon of escherichia coli.
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Authors
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L.A.Anderson,
T.Palmer,
N.C.Price,
S.Bornemann,
D.H.Boxer,
R.N.Pau.
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Ref.
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Eur J Biochem, 1997,
246,
119-126.
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PubMed id
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