Abstract
The isolated Block V repeats-in-toxin (RTX) peptide domain of adenylate cyclase (CyaA) from Bordetella pertussis reversibly folds into a β-roll secondary structure upon calcium binding. In this review, we discuss how the conformationally dynamic nature of the peptide is being engineered and employed as a switching mechanism to mediate different protein functions and protein-protein interactions. The peptide has been used as a scaffold for diverse applications including: a precipitation tag for bioseparations, a cross-linking domain for protein hydrogel formation and as an alternative scaffold for biomolecular recognition applications. Proteins and peptides such as the RTX domains that exhibit natural stimulus-responsive behavior are valuable building blocks for emerging synthetic biology applications.
Highlights
Bordetella pertussis is a Gram-negative bacteria, first isolated in 1906 and is the causative agent of whooping cough [1]
N-terminal cell-invasive catalytic domain composed of 400 amino acids and a C-terminal 1306 amino acid domain composed of five consecutive RTX domains [4,5,6]
Microrheology experiments were used to quantify hydrogel and we found that elasticity of the hydrogel depended on the calcium concentration
Summary
Bordetella pertussis is a Gram-negative bacteria, first isolated in 1906 and is the causative agent of whooping cough [1]. CyaA belongs to the repeat-in-toxin (RTX) family of proteins and in its active form, this 1706 amino acid enzyme is able to invade eukaryotic cells. It is composed of two domains: an. The catalytic domain of the enzyme is activated upon binding of eukaryotic calmodulin [7]. RTX domains bind calcium and undergo a structural transition, which facilitates the secretion of the attached catalytic domain via the bacterial type I secretion system. With calcium binding starting at the C-terminus of the β-roll and progressing towards the N-terminus [18] Another recent study reported a comprehensive 3D structural characterization of the calcium-bound folded form of CyaA. We will discuss several applications where this peptide has been engineered for new calcium-mediated functions, including as a precipitation tag for bioseparations, a cross-linking domain for protein hydrogel formation and as a structural switch for controllable biomolecular recognition
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
