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PDBsum entry 3e6d
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Transcription regulation
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PDB id
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3e6d
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Contents |
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* Residue conservation analysis
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Mol Microbiol
70:151-167
(2008)
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PubMed id:
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Molecular basis of halorespiration control by CprK, a CRP-FNR type transcriptional regulator.
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C.Levy,
K.Pike,
D.J.Heyes,
M.G.Joyce,
K.Gabor,
H.Smidt,
J.van der Oost,
D.Leys.
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ABSTRACT
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Certain bacteria are able to conserve energy via the reductive dehalogenation of
halo-organic compounds in a respiration-type metabolism. The transcriptional
regulator CprK from Desulfitobacterium spp. induces expression of
halorespiratory genes upon binding of o-chlorophenol ligands and is reversibly
inactivated by oxygen through disulphide bond formation. We report crystal
structures of D. hafniense CprK in the ligand-free (both oxidation states),
ligand-bound (reduced) and DNA-bound states, making it the first member of the
widespread CRP-FNR superfamily for which a complete structural description of
both redox-dependent and allosteric molecular rearrangements is available. In
conjunction with kinetic and thermodynamic ligand binding studies, we provide a
model for the allosteric mechanisms underpinning transcriptional control. Amino
acids that play a key role in this mechanism are not conserved in functionally
distinct CRP-FNR members. This suggests that, despite significant structural
homology, distinct allosteric mechanisms are used, enabling this protein family
to control a very wide range of processes.
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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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H.Antelmann,
and
J.D.Helmann
(2011).
Thiol-based redox switches and gene regulation.
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Antioxid Redox Signal,
14,
1049-1063.
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F.Maphosa,
W.M.de Vos,
and
H.Smidt
(2010).
Exploiting the ecogenomics toolbox for environmental diagnostics of organohalide-respiring bacteria.
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Trends Biotechnol,
28,
308-316.
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J.R.Haas
(2010).
The potential feasibility of chlorinic photosynthesis on exoplanets.
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Astrobiology,
10,
953-963.
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G.Giardina,
S.Rinaldo,
N.Castiglione,
M.Caruso,
and
F.Cutruzzolà
(2009).
A dramatic conformational rearrangement is necessary for the activation of DNR from Pseudomonas aeruginosa. Crystal structure of wild-type DNR.
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Proteins,
77,
174-180.
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PDB code:
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H.Sharma,
S.Yu,
J.Kong,
J.Wang,
and
T.A.Steitz
(2009).
Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding.
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Proc Natl Acad Sci U S A,
106,
16604-16609.
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PDB codes:
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M.John,
R.Rubick,
R.P.Schmitz,
J.Rakoczy,
T.Schubert,
and
G.Diekert
(2009).
Retentive memory of bacteria: Long-term regulation of dehalorespiration in Sulfurospirillum multivorans.
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J Bacteriol,
191,
1650-1655.
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N.Popovych,
S.R.Tzeng,
M.Tonelli,
R.H.Ebright,
and
C.G.Kalodimos
(2009).
Structural basis for cAMP-mediated allosteric control of the catabolite activator protein.
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Proc Natl Acad Sci U S A,
106,
6927-6932.
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PDB code:
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S.Mesa,
L.Reutimann,
H.M.Fischer,
and
H.Hennecke
(2009).
Posttranslational control of transcription factor FixK2, a key regulator for the Bradyrhizobium japonicum-soybean symbiosis.
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Proc Natl Acad Sci U S A,
106,
21860-21865.
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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
