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

doi:10.1093/nar/gkx489

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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 - 21 Aug 2017

Kang Sung-Min, Kim Do-Hee, Lee Ki-Young, Park Sung Jean, Yoon Hye-Jin, Lee Sang Jae, Im Hookang, Lee Bong-Jin

Abstract excerpt

Toxin-antitoxin (TA) systems are essential for bacterial persistence under stressful conditions. In particular, Mycobacterium tuberculosis express VapBC TA genes that encode the stable VapC toxin and the labile VapB antitoxin. Under normal conditions, these proteins interact to form a non-toxic TA complex, but the toxin is activated by release from the antitoxin in response to unfavorable conditions. Here, we...

Topics

Amino Acid Sequence
Antimicrobial Cationic Peptides
Bacterial Proteins
Bacterial Toxins
Calorimetry
Crystallography, X-Ray
DNA-Binding Proteins
Hydrophobic and Hydrophilic Interactions
Magnesium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Manganese

Mass Spectrometry

Membrane Glycoproteins

Models, Molecular

Mutation

Mycobacterium tuberculosis

Protein Binding

Protein Multimerization

Protein Structure, Secondary

Source

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Identifiers

PMID: 28575388
DOI: 10.1093/nar/gkx489
PMCID: PMC5737657

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