Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Topics Community

Article

Crystal structure of Mycobacterium tuberculosis VapC20 toxin and its interactions with cognate antitoxin, VapB20, suggest a model for toxin-antitoxin assembly.

The FEBS journal - 1 Dec 2017

Deep Amar, Kaundal Soni, Agarwal Sakshi, Singh Ramandeep, Thakur Krishan Gopal

Abstract excerpt

VapBCs, virulence-associated proteins, are the most abundant type II toxin-antitoxin (TA) systems in prokaryotes. Under normal conditions, toxin and antitoxin interact to form a heterooctameric complex, which upon binding to operator sites, inhibits their own expression. Under stress conditions, the VapB antitoxin is degraded by cellular proteases to release a free VapC toxin, which in turn inhibits cell growth...

Topics

Join the communities discussing this publication.

Bacterial Toxins
Binding Sites
Crystallography, X-Ray
Models, Molecular
Mycobacterium tuberculosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Domains

Sequence Homology, Nucleic Acid

Source

Identifiers

PMID: 28986943
DOI: 10.1111/febs.14289

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of Mycobacterium tuberculosis VapC20 toxin and its interactions with cognate antitoxin, VapB20, suggest a model for toxin-antitoxin assembly.PMID 28986943Read ↗

Functional details of the Mycobacterium tuberculosis VapBC26 toxin-antitoxin system based on a structural study: insights into unique binding and antibiotic peptides.Semantic proximity Read ↗

VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S rRNA.Semantic proximity Read ↗

Comprehensive Functional Analysis of Mycobacterium tuberculosis Toxin-Antitoxin Systems: Implications for Pathogenesis, Stress Responses, and EvolutionSemantic proximity Read ↗

VapCs of Mycobacterium tuberculosis cleave RNAs essential for translationSemantic proximity Read ↗

Structural Determinants for Antitoxin Identity and Insulation of Cross Talk between Homologous Toxin-Antitoxin Systems.Semantic proximity Read ↗

Comparative in silico analysis of vapBC3 toxin-antitoxin system in Mycobacterium Bovis and Mycobacterium tuberculosis.Semantic proximity Read ↗

Regulation of enteric vapBC transcription: induction by VapC toxin dimer-breaking.Semantic proximity Read ↗

Structure, Biology, and Therapeutic Application of Toxin–Antitoxin Systems in Pathogenic BacteriaSemantic proximity Read ↗

Accurate target identification for Mycobacterium tuberculosis endoribonuclease toxins requires expression in their native hostSemantic proximity Read ↗

Analysis of non-typeable Haemophilous influenzae VapC1 mutations reveals structural features required for toxicity and flexibility in the active site.Semantic proximity Read ↗

Structural and biochemical characterization on the cognate and heterologous interactions of the MazEF-mt9 TA systemSemantic proximity Read ↗

Structural analysis of the active site architecture of the VapC toxin from Shigella flexneri.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.