Structure and Proposed Activity of a Member of the VapBC Family of Toxin-Antitoxin Systems
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 284, Issue: 1, Page: 276-283
2009
- 114Citations
- 85Captures
- 2Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations114
- Citation Indexes114
- 114
- CrossRef107
- Captures85
- Readers85
- 76
- Mentions2
- News Mentions1
- 1
- References1
- 1
Most Recent News
Chromosomal bacterial type II toxin-antitoxin systems
Introduction Prokaryotic chromosomes contain genetic modules encoding 2 components: a stable toxin and its cognate labile antitoxin. These modules are called toxin-antitoxin (TA) systems (Gerdes
Article Description
In prokaryotes, cognate toxin-antitoxin pairs have long been known, but no three-dimensional structure has been available for any given complex from Mycobacterium tuberculosis. Here we report the crystal structure and activity of a member of the VapBC family of complexes from M. tuberculosis. The toxin VapC-5 is a compact, 150 residues, two domain α/β protein. Bent around the toxin is the VapB-5 antitoxin, a 33-residue α-helix. Assays suggest that the toxin is an Mg-enabled endoribonuclease, inhibited by the antitoxin. The lack of DNase activity is consistent with earlier suggestions that the complex represses its own operon. Furthermore, analysis of the interactions in the binding of the antitoxin to the toxin suggest that exquisite control is required to protect the bacteria cell from toxic VapC-5.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820683156; http://dx.doi.org/10.1074/jbc.m805061200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=58649099643&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/18952600; http://www.jbc.org/lookup/doi/10.1074/jbc.M805061200; https://syndication.highwire.org/content/doi/10.1074/jbc.M805061200; https://linkinghub.elsevier.com/retrieve/pii/S0021925820683156; https://dx.doi.org/10.1074/jbc.m805061200
American Society for Biochemistry & Molecular Biology (ASBMB)
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