ArticleProtein science : a publication of the Protein Society2012
The crystal structure of the Rv0301-Rv0300 VapBC-3 toxin-antitoxin complex from M. tuberculosis reveals a Mg²⁺ ion in the active site and a putative RNA-binding site.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.
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Who cites it
43 citing papers in PubMed, 1 synthesis or guideline pooled it, 55 citations in OpenAlex.
- A Systematic Overview of Type II and III Toxin-Antitoxin Systems with a Focus on Druggability.Toxins · 2018Pooled it
- A DNA damage-activated kinase phosphorylates a transcriptional repressor to control bacterial immune pathway expression.The EMBO journal · 2026Article
- Structural and functional characterization of VapBC52 toxin-antitoxin system from Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- Editorial for Special Issue "Molecular Research in Vaccinology and Vaccine Development".Current issues in molecular biology · 2026Article
- A DNA damage-activated kinase controls bacterial immune pathway expression.bioRxiv : the preprint server for biology · 2026Article
- Understanding the physiological role and cross-interaction network of VapBC35 toxin-antitoxin system from Mycobacterium tuberculosis.Communications biology · 2025Article
- Toxin-antitoxin system gene mutations drivingFrontiers in microbiology · 2024Article
- Focused Overview ofBiomimetics (Basel, Switzerland) · 2023Review
- Impact of Genomic Deletion RD16 on the Expression of theCurrent issues in molecular biology · 2023Article
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- tRNAAntimicrobial agents and chemotherapy · 2022Article
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- Biochemical Characterization of VapC46 Toxin from Mycobacterium tuberculosis.Molecular biotechnology · 2020Article
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- VapC21 Toxin Contributes to Drug-Tolerance and Interacts With Non-cognate VapB32 Antitoxin inFrontiers in microbiology · 2020Article
- The Variety in the Common Theme of Translation Inhibition by Type II Toxin-Antitoxin Systems.Frontiers in genetics · 2020Review
- Bioinformatic and mutational studies of related toxin-antitoxin pairs inThe Journal of biological chemistry · 2019Article
- Structural, functional and biological insights into the role of Mycobacterium tuberculosis VapBC11 toxin-antitoxin system: targeting a tRNase to tackle mycobacterial adaptation.Nucleic acids research · 2018Article
- VapC proteins from Mycobacterium tuberculosis share ribonuclease sequence specificity but differ in regulation and toxicity.PloS one · 2018Article
- Functional details of the Mycobacterium tuberculosis VapBC26 toxin-antitoxin system based on a structural study: insights into unique binding and antibiotic peptides.Nucleic acids research · 2017Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
VapBC pairs account for 45 out of 88 identified toxin-antitoxin (TA) pairs in the Mycobacterium tuberculosis (Mtb) H37Rv genome. A working model suggests that under times of stress, antitoxin molecules are degraded, releasing the toxins to slow the metabolism of the cell, which in the case of VapC toxins is via their RNase activity. Otherwise the TA pairs remain bound to their promoters, autoinhibiting transcription. The crystal structure of Rv0301-Rv0300, an Mtb VapBC TA complex determined at 1.49 Å resolution, suggests a mechanism for these three functions: RNase activity, its inhibition by antitoxin, and its ability to bind promoter DNA. The Rv0301 toxin consists of a core of five parallel beta strands flanked by alpha helices. Three proximal aspartates coordinate a Mg²⁺ ion forming the putative RNase active site. The Rv0300 antitoxin monomer is extended in structure, consisting of an N-terminal beta strand followed by four helices. The last two helices wrap around the toxin and terminate near the putative RNase active site, but with different conformations. In one conformation, the C-terminal arginine interferes with Mg²⁺ ion coordination, suggesting a mechanism by which the antitoxin can inhibit toxin activity. At the N-terminus of the antitoxin, two pairs of Ribbon-Helix-Helix (RHH) motifs are related by crystallographic twofold symmetry. The resulting hetero-octameric complex is similar to the FitAB system, but the two RHH motifs are about 30 Å closer together in the Rv0301-Rv0300 complex, suggesting either a different span of the DNA recognition sequence or a conformational change.
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