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PDBsum entry 2fbk
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Transcription
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PDB id
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2fbk
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Contents |
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* Residue conservation analysis
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DOI no:
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J Mol Biol
360:168-177
(2006)
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PubMed id:
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The crystal structure of the transcriptional regulator HucR from Deinococcus radiodurans reveals a repressor preconfigured for DNA binding.
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T.Bordelon,
S.P.Wilkinson,
A.Grove,
M.E.Newcomer.
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ABSTRACT
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We report here the 2.3 A resolution structure of the hypothetical uricase
regulator (HucR) from Deinococcus radiodurans R1. HucR, a member of the MarR
family of DNA-binding proteins, was previously shown to repress its own
expression as well as that of a uricase, a repression that is alleviated both in
vivo and in vitro upon binding uric acid, the substrate for uricase. As uric
acid is a potent scavenger of reactive oxygen species, and as D. radiodurans is
known for its remarkable resistance to DNA-damaging agents, these observations
indicate a novel oxidative stress response mechanism. The crystal structure of
HucR in the absence of ligand or DNA reveals a dimer in which the DNA
recognition helices are preconfigured for DNA binding. This configuration of
DNA-binding domains is achieved through an apparently stable dimer interface
that, in contrast to what is observed in other MarR homologs for which
structures have been determined, shows little conformational heterogeneity in
the absence of ligand. An additional amino-terminal segment, absent from other
MarR homologs, appears to brace the principal helix of the dimerization
interface. However, although HucR is preconfigured for DNA binding, the presence
of a stacked pair of symmetry-related histidine residues at a central pivot
point in the dimer interface suggests a mechanism for a conformational change to
attenuate DNA binding.
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Selected figure(s)
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Figure 2.
Figure 2. Superposition of HucR and OhrR structures. The
DNA-bound structure of OhrR (1Z9C) is in magenta and HucR is in
blue. The recognition helices are in lighter shades.
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Figure 5.
Figure 5. A region of the 2F[o]-F[c] electron density map.
The map is contoured at 1s. The region corresponds to the dimer
interface and the stacking of symmetry-related His51 residues is
apparent.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2006,
360,
168-177)
copyright 2006.
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Figures were
selected
by an automated process.
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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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I.C.Perera,
and
A.Grove
(2011).
MarR homologs with urate-binding signature.
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Protein Sci,
20,
621-629.
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A.Grove
(2010).
Urate-responsive MarR homologs from Burkholderia.
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Mol Biosyst,
6,
2133-2142.
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C.Andrésen,
S.Jalal,
D.Aili,
Y.Wang,
S.Islam,
A.Jarl,
B.Liedberg,
B.Wretlind,
L.G.Mårtensson,
and
M.Sunnerhagen
(2010).
Critical biophysical properties in the Pseudomonas aeruginosa efflux gene regulator MexR are targeted by mutations conferring multidrug resistance.
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Protein Sci,
19,
680-692.
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I.C.Perera,
and
A.Grove
(2010).
Molecular mechanisms of ligand-mediated attenuation of DNA binding by MarR family transcriptional regulators.
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J Mol Cell Biol,
2,
243-254.
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K.J.McLaughlin,
C.M.Strain-Damerell,
K.Xie,
D.Brekasis,
A.S.Soares,
M.S.Paget,
and
C.L.Kielkopf
(2010).
Structural basis for NADH/NAD+ redox sensing by a Rex family repressor.
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Mol Cell,
38,
563-575.
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PDB codes:
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S.Reverchon,
F.Van Gijsegem,
G.Effantin,
O.Zghidi-Abouzid,
and
W.Nasser
(2010).
Systematic targeted mutagenesis of the MarR/SlyA family members of Dickeya dadantii 3937 reveals a role for MfbR in the modulation of virulence gene expression in response to acidic pH.
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Mol Microbiol,
78,
1018-1037.
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C.E.Nichols,
S.Sainsbury,
J.Ren,
T.S.Walter,
A.Verma,
D.K.Stammers,
N.J.Saunders,
and
R.J.Owens
(2009).
The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
65,
204-209.
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PDB code:
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M.Kumaraswami,
J.T.Schuman,
S.M.Seo,
G.W.Kaatz,
and
R.G.Brennan
(2009).
Structural and biochemical characterization of MepR, a multidrug binding transcription regulator of the Staphylococcus aureus multidrug efflux pump MepA.
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Nucleic Acids Res,
37,
1211-1224.
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PDB code:
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T.Kumarevel,
T.Tanaka,
T.Umehara,
and
S.Yokoyama
(2009).
ST1710-DNA complex crystal structure reveals the DNA binding mechanism of the MarR family of regulators.
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Nucleic Acids Res,
37,
4723-4735.
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PDB codes:
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M.S.Wilke,
M.Heller,
A.L.Creagh,
C.A.Haynes,
L.P.McIntosh,
K.Poole,
and
N.C.Strynadka
(2008).
The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR.
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Proc Natl Acad Sci U S A,
105,
14832-14837.
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PDB code:
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K.J.Newberry,
M.Fuangthong,
W.Panmanee,
S.Mongkolsuk,
and
R.G.Brennan
(2007).
Structural mechanism of organic hydroperoxide induction of the transcription regulator OhrR.
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Mol Cell,
28,
652-664.
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PDB codes:
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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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