ArticleThe FEBS journal2023
Crystal structures of free and ligand-bound forms of the TetR/AcrR-like regulator SCO3201 from Streptomyces coelicolor suggest a novel allosteric mechanism.
Article in The FEBS journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Identification and distribution of a downregulatory signaling alkyloxazole inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural basis for inhibition of TcrXyn10A xylanase by nonspecific xylose binding at subsite - 2.Scientific reports · 2026Article
- Molecular basis of antibiotic sensing by the TetR family regulator CecR - a structural perspective.The FEBS journal · 2026Article
- TetR family regulator AbrT controls lincomycin production and morphological development in Streptomyces lincolnensis.Microbial cell factories · 2024Article
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5 authors.
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Abstract
TetR/AcrR-like transcription regulators enable bacteria to sense a wide variety of chemical compounds and to dynamically adapt the expression levels of specific genes in response to changing growth conditions. Here, we describe the structural characterisation of SCO3201, an atypical TetR/AcrR family member from Streptomyces coelicolor that strongly represses antibiotic production and morphological development under conditions of overexpression. We present crystal structures of SCO3201 in its ligand-free state as well as in complex with an unknown inducer, potentially a polyamine. In the ligand-free state, the DNA-binding domains of the SCO3201 dimer are held together in an unusually compact conformation and, as a result, the regulator cannot span the distance between the two half-sites of its operator. Interaction with the ligand coincides with a major structural rearrangement and partial conversion of the so-called hinge helix (α4) to a 3
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