Database accession: MF7000314
Name: PadR-like transcriptional regulator (Listeria monocytogenes)
PDB ID: 7wjp
Experimental method: X-ray (2.25 Å)
Assembly: Homodimer
Source organism: Listeria monocytogenes
Primary publication of the structure:
Kim J, Park J, Choi Z, Hong M
Structure-based molecular characterization of the LltR transcription factor from Listeria monocytogenes.
(2022) Biochem. Biophys. Res. Commun. 600: 142-149
PMID: 35219103
Abstract:
Listeria monocytogenes is a psychrotrophic food-borne pathogenic bacterium that causes listeriosis. Due to its unusual adaptation, an ability to grow at extended temperatures ranging from 4 to 45 °C, L. monocytogenes is notoriously hard to control in food-manufacturing processes. In addition, the growing number of antibiotic-resistant L. monocytogenes strains have made listeriosis steadily refractory to clinical treatments and can lead to serious life-threatening diseases, such as sepsis and meningitis, in immunocompromised persons and neonates. Transcription factors that belong to the PadR family play a key role in bacterial survival against unfavorable environmental stresses. The LltR protein from L. monocytogenes was identified as a PadR-type transcription factor and was shown to be required for bacterial growth adaptation at low temperatures. Despite the functional significance of LltR in listeria survival and pathogenesis, our molecular understanding of the LltR-mediated transcriptional regulation is highly limited. Here, we report the crystal structure of LltR and reveal the operator DNA recognition mechanism used by LltR. LltR dimerizes into an isosceles triangle-like shape and requires a winged helix-turn-helix motif for dsDNA recognition. Indeed, LltR and putative operator dsDNA binding was observed and suggests a transcriptional repression of the llfR-lmo0600-lmo0601 operon by direct interaction between the LltR transcription factor and its promoter region. Structure-based comparative and mutational analyses showed that LltR interacts with dsDNA via a unique strategy that combines both LltR-specific and PadR family-common mechanisms.
Molecular function: not assigned
Biological process: not assigned
Cellular component: not assigned
Entry contents: 2 distinct polypeptide molecules
Chains: A, A-2
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: PadR family transcriptional regulator
Source organism: Listeria monocytogenes
Length: 110 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMEVNPQFKKGVLELCCLFLIQKKDCYGYELANQVSKYIEVAEGAIYPVLRRLVKEEYCSTYLVESNEGPSRKYYQLTVKGEIYLNELISEWNNFTDSVAKLLTEGEAVNE
UniProtKB AC: A0A1D2INR9 (positions: 5-105)
Coverage: 91%
Name: PadR family transcriptional regulator
Source organism: Listeria monocytogenes
Length: 110 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMEVNPQFKKGVLELCCLFLIQKKDCYGYELANQVSKYIEVAEGAIYPVLRRLVKEEYCSTYLVESNEGPSRKYYQLTVKGEIYLNELISEWNNFTDSVAKLLTEGEAVNE
UniProtKB AC: A0A1D2INR9 (positions: 5-105)
Coverage: 91%
Representative domain in related structures: Winged helix DNA-binding domain (PadR family) transcriptional regulator
Evidence level: Direct evidence
Evidence coverage: Only some parts of the structure participates in mutual synergistic folding.
Complex Evidence:
AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748).
Chain A:
N/A
Chain A-2:
N/A
Surface and contacts features:
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