Disorder-to-order transition in the CyaA toxin RTX domain: implications for toxin secretion.

ABSTRACT: The past decade has seen a fundamental reappraisal of the protein structure-to-function paradigm because it became evident that a significant fraction of polypeptides are lacking ordered structures under physiological conditions. Ligand-induced disorder-to-order transition plays a key role in the biological functions of many proteins that contain intrinsically disordered regions. This trait is exhibited by RTX (Repeat in ToXin) motifs found in more than 250 virulence factors secreted by Gram-negative pathogenic bacteria. We have investigated several RTX-containing polypeptides of different lengths, all derived from the Bordetella pertussis adenylate cyclase toxin, CyaA. Using a combination of experimental approaches, we showed that the RTX proteins exhibit the hallmarks of intrinsically di

SUBMITTER: Sotomayor-Perez AC 

PROVIDER: S-EPMC4303809 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature