ArticleProtein science : a publication of the Protein Society2014
Crystal structure of the transcriptional regulator Rv1219c of Mycobacterium tuberculosis.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 35 citations in OpenAlex.
- Beyond antibiotics: CRISPR/Cas9 triumph over biofilm-associated antibiotic resistance infections.Frontiers in cellular and infection microbiology · 2024Review
- Mycobacterium tuberculosis response to cholesterol is integrated with environmental pH and potassium levels via a lipid metabolism regulator.PLoS genetics · 2024Article
- Genome-wide association studies of global Mycobacterium tuberculosis resistance to 13 antimicrobials in 10,228 genomes identify new resistance mechanisms.PLoS biology · 2022Article
- The Association between Biofilm Formation and Antimicrobial Resistance with Possible Ingenious Bio-Remedial Approaches.Antibiotics (Basel, Switzerland) · 2022Review
- Critical discussion on drug efflux in Mycobacterium tuberculosis.FEMS microbiology reviews · 2022Review
- Transcriptional regulation and drug resistance inFrontiers in cellular and infection microbiology · 2022Review
- Gene expression profile analysis and target gene discovery of Mycobacterium tuberculosis biofilm.Applied microbiology and biotechnology · 2021Article
- The ATP-Binding Cassette (ABC) Transport Systems inBiology · 2020Review
- Crystal structure of the Mycobacterium tuberculosis transcriptional regulator Rv0302.Protein science : a publication of the Protein Society · 2015Article
- Structural Basis for the Regulation of the MmpL Transporters of Mycobacterium tuberculosis.The Journal of biological chemistry · 2015Article
- Molecular mechanisms of antibiotic resistance.Nature reviews. Microbiology · 2015Review
- Oleoyl coenzyme A regulates interaction of transcriptional regulator RaaS (Rv1219c) with DNA in mycobacteria.The Journal of biological chemistry · 2014Article
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
The Rv1217c-Rv1218c multidrug efflux system, which belongs to the ATP-binding cassette superfamily, recognizes and actively extrudes a variety of structurally unrelated toxic chemicals and mediates the intrinsic resistance to these antimicrobials in Mycobacterium tuberculosis. The expression of Rv1217c-Rv1218c is controlled by the TetR-like transcriptional regulator Rv1219c, which is encoded by a gene immediately upstream of rv1218c. To elucidate the structural basis of Rv1219c regulation, we have determined the crystal structure of Rv1219c, which reveals a dimeric two-domain molecule with an entirely helical architecture similar to members of the TetR family of transcriptional regulators. The N-terminal domains of the Rv1219c dimer are separated by a large center-to-center distance of 64 Å. The C-terminal domain of each protomer possesses a large cavity. Docking of small compounds to Rv1219c suggests that this large cavity forms a multidrug binding pocket, which can accommodate a variety of structurally unrelated antimicrobial agents. The internal wall of the multidrug binding site is surrounded by seven aromatic residues, indicating that drug binding may be governed by aromatic stacking interactions. In addition, fluorescence polarization reveals that Rv1219c binds drugs in the micromolar range.
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