ArticleFEBS open bio2019
The crystal structure of AcrR from Mycobacterium tuberculosis reveals a one-component transcriptional regulation mechanism.
Article in FEBS open bio, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Immunoinformatics and structural aided approach to develop multi-epitope based subunit vaccine against Mycobacterium tuberculosis.Scientific reports · 2024Article
- The pH-responsive SmrR-SmrT system modulatesInfection and immunity · 2024Article
- Carbon Monoxide-Sensing Transcription Factors: Regulators of Microbial Carbon Monoxide Oxidation Pathway Gene Expression.Journal of bacteriology · 2023Review
- Local Regulator AcrR Regulates Persister Formation by Repression of AcrAB Efflux Pump during Exponential Growth in Aeromonas veronii.Antimicrobial agents and chemotherapy · 2023Article
- Evolutionary Conserved Short Linear Motifs Provide Insights into the Cellular Response to Stress.Antioxidants (Basel, Switzerland) · 2022Article
- Interplay between Non-Coding RNA Transcription, Stringent/Relaxed Phenotype and Antibiotic Production inAntibiotics (Basel, Switzerland) · 2021Article
- The molecular basis of extensively drug-resistant Salmonella Typhi isolates from pediatric septicemia patients.PloS one · 2021Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcriptional regulator proteins are closely involved in essential survival strategies in bacteria. AcrR is a one-component allosteric repressor of the genes associated with lipid transport and antibiotic resistance. When fatty acid ligands bind to the C-terminal ligand-binding cavity of AcrR, a conformational change in the N-terminal operator-binding region of AcrR is triggered, which releases the repressed DNA and initiates transcription. This paper focuses on the structural transition mechanism of AcrR of Mycobacterium tuberculosis upon DNA and ligand binding. AcrR loses its structural integrity upon ligand-mediated structural alteration and bends toward the promoter DNA in a more compact form, initiating a rotational motion. Our functional characterization of AcrR and description of the ligand- and DNA-recognition mechanism may facilitate the discovery of new therapies for tuberculosis.
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Registered trials
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