The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N.

ABSTRACT: Intrinsically disordered regions within proteins are critical elements in many biomolecular interactions and signaling pathways. Antibacterial toxins of the colicin family, which could provide new antibiotic functions against resistant bacteria, contain disordered N-terminal translocation domains (T-domains) that are essential for receptor binding and the penetration of the Escherichia coli outer membrane. Here we investigate the conformational behavior of the T-domain of colicin N (ColN-T) to understand why such domains are widespread in toxins that target Gram-negative bacteria. Like some other intrinsically disordered proteins in the solution state of the protein, ColN-T shows dual recognition, initially interacting with other domains of the same colicin N molecule and later, during cel

SUBMITTER: Johnson CL 

PROVIDER: S-EPMC5647543 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature