Download MendeleyStructure and allosteric coupling of type II antitoxin CopASO.
Zhao, R., Li, Q., Zhang, J., Li, F., Yao, J., Zhang, J., Liu, L., Wang, X., Zhang, X.(2019) Biochem Biophys Res Commun 514: 1122-1127
- PubMed: 31101334
- DOI: https://doi.org/10.1016/j.bbrc.2019.05.049
- Primary Citation of Related Structures:
6IYA - PubMed 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 CopA SO , a newly identified type II antitoxin in Shewanella oneidensis, were investigated. Our data show that CopA SO 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.
Organizational Affiliation:
School of Life Sciences, Anhui University, Hefei, Anhui, 230601, China; Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis, Hefei, Anhui, 230601, China; Anhui Key Laboratory of Modern Biomanufacturing, Hefei, Anhui, 230601, China.
