ArticleActa crystallographica. Section D, Biological crystallography2009
Structure of Thermotoga maritima TM0439: implications for the mechanism of bacterial GntR transcription regulators with Zn2+-binding FCD domains.
Article in Acta crystallographica. Section D, Biological crystallography, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 37 citations in OpenAlex.
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- Molecular Strategies of Carbohydrate Binding to Intrinsically Disordered Regions in Bacterial Transcription Factors.International journal of molecular sciences · 2026Article
- STK-mediated FadR phosphorylation regulates the acid resistance and virulence of Streptococcus suis.PLoS pathogens · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Gonococcal Clinical Strains Bearing a CommonmBio · 2022Article
- Cell-Free Protein Synthesis by Diversifying Bacterial Transcription Machinery.Biotech (Basel (Switzerland)) · 2021Article
- Characterization of an operon required for growth on cellobiose inMicrobiology (Reading, England) · 2021Article
- Transcription factor allosteric regulation through substrate coordination to zinc.NAR genomics and bioinformatics · 2021Article
- Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism.Nature communications · 2021Article
- Molecular Cloning, Purification and Characterization of Mce1R of Mycobacterium tuberculosis.Molecular biotechnology · 2021Article
- Characterization of the first tetrameric transcription factor of the GntR superfamily with allosteric regulation from the bacterial pathogen Agrobacterium fabrum.Nucleic acids research · 2021Article
- Structural and Functional Analyses of the Transcription Repressor DgoR FromFrontiers in microbiology · 2020Article
- Transcriptional regulation of a gonococcal gene encoding a virulence factor (L-lactate permease).PLoS pathogens · 2019Article
- Identification of a GntR family regulator BusRExtremophiles : life under extreme conditions · 2019Article
- A GntR-Like Transcription Factor HypR Regulates Expression of Genes Associated With L-Hydroxyproline Utilization inFrontiers in microbiology · 2019Article
- MouR controls the expression of the Listeria monocytogenes Agr system and mediates virulence.Nucleic acids research · 2018Article
- Article
- Metallochaperones and metalloregulation in bacteria.Essays in biochemistry · 2017Review
- Expanding the Cyanobacterial Nitrogen Regulatory Network: The GntR-Like Regulator PlmA Interacts with the PII-PipX Complex.Frontiers in microbiology · 2016Article
- Functional Analysis of the Citrate Activator CitO from Enterococcus faecalis Implicates a Divalent Metal in Ligand Binding.Frontiers in microbiology · 2016Article
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11 authors at 5 institutions in 1 country.
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Abstract
The GntR superfamily of dimeric transcription factors, with more than 6200 members encoded in bacterial genomes, are characterized by N-terminal winged-helix DNA-binding domains and diverse C-terminal regulatory domains which provide a basis for the classification of the constituent families. The largest of these families, FadR, contains nearly 3000 proteins with all-alpha-helical regulatory domains classified into two related Pfam families: FadR_C and FCD. Only two crystal structures of FadR-family members, those of Escherichia coli FadR protein and LldR from Corynebacterium glutamicum, have been described to date in the literature. Here, the crystal structure of TM0439, a GntR regulator with an FCD domain found in the Thermotoga maritima genome, is described. The FCD domain is similar to that of the LldR regulator and contains a buried metal-binding site. Using atomic absorption spectroscopy and Trp fluorescence, it is shown that the recombinant protein contains bound Ni(2+) ions but that it is able to bind Zn(2+) with K(d) < 70 nM. It is concluded that Zn(2+) is the likely physiological metal and that it may perform either structural or regulatory roles or both. Finally, the TM0439 structure is compared with two other FadR-family structures recently deposited by structural genomics consortia. The results call for a revision in the classification of the FadR family of transcription factors.
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