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• W2945492572 abstract "Toxin-antitoxin (TA) systems play critical roles in the environment adaptation of bacteria. Allosteric coupling between the N-terminal DNA-binding domain and the C-terminal toxin-binding domain of antitoxins contributes to conditional cooperativity in the functioning of type II TA. Herein, using circular dichroism (CD), nuclear magnetic resonance (NMR), X-ray crystallography, and size exclusion chromatography (SEC), the structure and DNA binding of CopASO, a newly identified type II antitoxin in Shewanella oneidensis, were investigated. Our data show that CopASO is a typical RHH antitoxin with an ordered N-terminal domain and a disordered C-terminal domain, and furthermore indicate that the C-terminal domain facilitates DNA binding of the N-terminal domain, which in turn induces the C-terminal domain to fold and associate." @default.
• W2945492572 created "2019-05-29" @default.
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• W2945492572 date "2019-07-01" @default.
• W2945492572 modified "2023-10-16" @default.
• W2945492572 title "Structure and allosteric coupling of type Ⅱ antitoxin CopASO" @default.
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• W2945492572 doi "https://doi.org/10.1016/j.bbrc.2019.05.049" @default.
• W2945492572 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31101334" @default.
• W2945492572 hasPublicationYear "2019" @default.
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