ArticleNucleic acids research2003
The structure of full-length LysR-type transcriptional regulators. Modeling of the full-length OxyR transcription factor dimer.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 66 citations in OpenAlex.
- Mutation ofAntibiotics (Basel, Switzerland) · 2025Article
- Two redox-responsive LysR-type transcription factors control the oxidative stress response of Agrobacterium tumefaciens.Nucleic acids research · 2025Article
- Fundamentals and Exceptions of the LysR-type Transcriptional Regulators.ACS synthetic biology · 2024Review
- Structural and functional insights into transcription activation of the essential LysR-type transcriptional regulators.Protein science : a publication of the Protein Society · 2024Article
- Divergent directed evolution of a TetR-type repressor towards aromatic molecules.Nucleic acids research · 2023Article
- SstF, a novel sulforaphane-sensing transcription factor of Xanthomonas campestris, is required for sulforaphane tolerance and virulence.Molecular plant pathology · 2023Article
- A LysR Transcriptional Regulator Manipulates Macrophage Autophagy Flux DuringFrontiers in cellular and infection microbiology · 2022Article
- How Bacterial Redox Sensors Transmit Redox Signals via Structural Changes.Antioxidants (Basel, Switzerland) · 2021Review
- A novel LysR-type regulator negatively affects biosynthesis of the immunosuppressant brasilicardin.Engineering in life sciences · 2021Article
- Design of a Transcriptional Biosensor for the Portable, On-Demand Detection of Cyanuric Acid.ACS synthetic biology · 2020Article
- Regulation of bistability in the std fimbrial operon of Salmonella enterica by DNA adenine methylation and transcription factors HdfR, StdE and StdF.Nucleic acids research · 2019Article
- A LysR-Type Transcriptional Regulator LcrX Is Involved in Virulence, Biofilm Formation, Swimming Motility, Siderophore Secretion, and Growth in Sugar Sources inFrontiers in plant science · 2019Article
- The Disruption of an OxyR-Like Protein Impairs Intracellular Magnetite Biomineralization inFrontiers in microbiology · 2017Article
- OxyR-dependent formation of DNA methylation patterns in OpvABOFF and OpvABON cell lineages of Salmonella enterica.Nucleic acids research · 2016Article
- Isolation and characterization of mutant Sinorhizobium meliloti NodD1 proteins with altered responses to luteolin.Journal of bacteriology · 2013Article
- ATP-dependent RecG helicase is required for the transcriptional regulator OxyR function in Pseudomonas species.The Journal of biological chemistry · 2012Article
- Characterization of OxyR as a negative transcriptional regulator that represses catalase production in Corynebacterium diphtheriae.PloS one · 2012Article
- Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.Applied and environmental microbiology · 2011Article
- Expression, purification, crystallization and preliminary X-ray analysis of the DNA-binding domain of Rhodobacter capsulatus MopB.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Molecular characterization of GrlA, a specific positive regulator of ler expression in enteropathogenic Escherichia coli.Journal of bacteriology · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The LysR-type transcriptional regulators (LTTRs) comprise the largest family of prokaryotic transcription factors. These proteins are composed of an N-terminal DNA binding domain (DBD) and a C-terminal cofactor binding domain. To date, no structure of the DBD has been solved. According to the SUPERFAMILY and MODBASE databases, a reliable homology model of LTTR DBDs may be built using the structure of the Escherichia coli ModE transcription factor, containing a winged helix- turn-helix (HTH) motif, as a template. The remote, but statistically significant, sequence similarity between ModE and LTTR DBDs and an alignment generated using SUPERFAMILY and MODBASE methods was independently confirmed by alignment of sequence profiles representing ModE and LTTR family DBDs. Using the crystal structure of the E.coli OxyR C-terminal domain and the DBD alignments we constructed a structural model of the full-length dimer of this LTTR family member and used it to investigate the mode of protein-DNA interaction. We also applied the model to interpret, in a structural context, the results of numerous biochemical studies of mutated LTTRs. A comparison of the LTTR DBD model with the structures of other HTH proteins also provides insights into the interaction of LTTRs with the C-terminal domain of the RNA polymerase alpha subunit.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.