 |
PDBsum entry 4esb
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Transcription
|
PDB id
|
|
|
|
4esb
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
|
Plos One
7:e48015
(2012)
|
|
PubMed id:
|
|
|
|
|
| |
|
Crystal structures of two transcriptional regulators from Bacillus cereus define the conserved structural features of a PadR subfamily.
|
|
G.Fibriansah,
..T.Kovács,
T.J.Pool,
M.Boonstra,
O.P.Kuipers,
A.M.Thunnissen.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
PadR-like transcriptional regulators form a structurally-related family of
proteins that control the expression of genes associated with detoxification,
virulence and multi-drug resistance in bacteria. Only a few members of this
family have been studied by genetic, biochemical and biophysical methods, and
their structure/function relationships are still largely undefined. Here, we
report the crystal structures of two PadR-like proteins from Bacillus cereus,
which we named bcPadR1 and bcPadR2 (products of gene loci BC4206 and BCE3449 in
strains ATCC 14579 and ATCC 10987, respectively). BC4206, together with its
neighboring gene BC4207, was previously shown to become significantly
upregulated in presence of the bacteriocin AS-48. DNA mobility shift assays
reveal that bcPadR1 binds to a 250 bp intergenic region containing the putative
BC4206-BC4207 promoter sequence, while in-situ expression of bcPadR1 decreases
bacteriocin tolerance, together suggesting a role for bcPadR1 as repressor of
BC4206-BC4207 transcription. The function of bcPadR2 (48% identical in sequence
to bcPadR1) is unknown, but the location of its gene just upstream from genes
encoding a putative antibiotic ABC efflux pump, suggests a role in regulating
antibiotic resistance. The bcPadR proteins are structurally similar to LmrR, a
PadR-like transcription regulator in Lactococcus lactis that controls expression
of a multidrug ABC transporter via a mechanism of multidrug binding and
induction. Together these proteins define a subfamily of conserved, relatively
small PadR proteins characterized by a single C-terminal helix for dimerization.
Unlike LmrR, bcPadR1 and bcPadR2 lack a central pore for ligand binding, making
it unclear whether the transcriptional regulatory roles of bcPadR1 and bcPadR2
involve direct ligand recognition and induction.
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
');
}
}
 |