Block V RTX Domain of Adenylate Cyclase from Bordetella pertussis: A Conformationally Dynamic Scaffold for Protein Engineering Applications

Toxins

Scott Banta¹  Beyza Bulutoglu¹ 

[1] Department of Chemical Engineering, Columbia University, 500 W 120th Street, New York, NY 10027, USA;

关键词: protein engineering;    RTX domain;    β-roll domain;    hydrogels;    bioseparations;    biomolecular recognition;   

DOI  :  10.3390/toxins9090289

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown