Structural highlights
Publication Abstract from PubMed
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.
Structure and allosteric coupling of type antitoxin CopASO.,Zhao R, Li Q, Zhang J, Li F, Yao J, Zhang J, Liu L, Wang X, Zhang X Biochem Biophys Res Commun. 2019 Jul 5;514(4):1122-1127. doi:, 10.1016/j.bbrc.2019.05.049. Epub 2019 May 14. PMID:31101334[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhao R, Li Q, Zhang J, Li F, Yao J, Zhang J, Liu L, Wang X, Zhang X. Structure and allosteric coupling of type antitoxin CopASO. Biochem Biophys Res Commun. 2019 Jul 5;514(4):1122-1127. doi:, 10.1016/j.bbrc.2019.05.049. Epub 2019 May 14. PMID:31101334 doi:http://dx.doi.org/10.1016/j.bbrc.2019.05.049
