2.09 Å Resolution structure of E. coli HigBA toxin-antitoxin complex reveals an ordered DNA-binding domain and intrinsic dynamics in antitoxin

• Published in: Biochemical journal Vol. 477; no. 20; p. 4001
• Main Authors: Jadhav, Pankaj Vilas, Sinha, Vikrant Kumar, Chugh, Saurabh, Kotyada, Chaithanya, Bachhav, Digvijay, Singh, Ramandeep, Rothweiler, Ulli, Singh, Mahavir
• Format: Journal Article
• Language: English
• Published: England 30.10.2020
• Subjects: Antitoxins - chemistry; Antitoxins - genetics; Antitoxins - metabolism; Circular Dichroism; Crystallography, X-Ray; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Escherichia coli - chemistry; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Dynamics Simulation; Operon - genetics; Promoter Regions, Genetic; Protein Binding; Protein Domains - genetics; Protein Multimerization; Recombinant Proteins; Up-Regulation; protein–protein interactions; HigBA; protein–DNA; antibiotic resistance; X-ray structure; toxin–antitoxin

The toxin-antitoxin (TA) systems are small operon systems that are involved in important physiological processes in bacteria such as stress response and persister cell formation. Escherichia coli HigBA complex belongs to the type II TA systems and consists of a protein toxin called HigB and a protei...