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Toxins 2017, 9(9), 289; https://doi.org/10.3390/toxins9090289

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

Department of Chemical Engineering, Columbia University, 500 W 120th Street, New York, NY 10027, USA
Current address: Center for Engineering in Medicine, Harvard Medical School and Massachusetts General Hospital, 51 Blossom Street, Boston, MA 02114, USA; bbulutoglu@mgh.harvard.edu.
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Author to whom correspondence should be addressed.
Academic Editor: Alexandre Chenal
Received: 30 August 2017 / Revised: 12 September 2017 / Accepted: 12 September 2017 / Published: 17 September 2017
(This article belongs to the Special Issue Adenylate Cyclase (CyaA) Toxin)
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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. View Full-Text
Keywords: protein engineering; RTX domain; β-roll domain; hydrogels; bioseparations; biomolecular recognition protein engineering; RTX domain; β-roll domain; hydrogels; bioseparations; biomolecular recognition
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Bulutoglu, B.; Banta, S. Block V RTX Domain of Adenylate Cyclase from Bordetella pertussis: A Conformationally Dynamic Scaffold for Protein Engineering Applications. Toxins 2017, 9, 289.

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