6IYA

Structure of the DNA binding domain of antitoxin CopASO

Summary for 6IYA

• Entry DOI: 10.2210/pdb6iya/pdb
• Descriptor: Transcriptional regulator CopG family (2 entities in total)
• Functional Keywords: antitoxin, rhh, dna binding
• Biological source: Shewanella oneidensis
• Total number of polymer chains: 6
• Total formula weight: 47964.86

Authors

Zhao, R.,Li, F.,Liu, L.,Zhang, X. (deposition date: 2018-12-14, release date: 2019-01-16, Last modification date: 2023-11-22)

Primary citation

Zhao, R.,Li, Q.,Zhang, J.,Li, F.,Yao, J.,Zhang, J.,Liu, L.,Wang, X.,Zhang, X.
Structure and allosteric coupling of type II antitoxin CopASO.
Biochem.Biophys.Res.Commun., 514:1122-1127, 2019

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, a newly identified type II antitoxin in Shewanella oneidensis, were investigated. Our data show that CopA 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.

PubMed: 31101334
DOI: 10.1016/j.bbrc.2019.05.049

Experimental method

X-RAY DIFFRACTION (3 Å)