Interaction with adenylate cyclase toxin from Bordetella pertussis affects the metal binding properties of calmodulin

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Abstract

Adenylate cyclase toxin domain (CyaA-ACD) is a calmodulin (CaM)-dependent adenylate cyclase involved in Bordetella pertussis pathogenesis. Calcium (Ca2+) and magnesium (Mg2+) concentrations impact CaM-dependent CyaA-ACD activation, but the structural mechanisms remain unclear. In this study, NMR, dynamic light scattering, and native PAGE were used to probe Mg2+-induced transitions in CaM's conformation in the presence of CyaA-ACD. Mg2+ binding was localized to sites I and II, while sites III and IV remained Ca2+ loaded when CaM was bound to CyaA-ACD. 2Mg2+/2Ca2+-loaded CaM/CyaA-ACD was elongated, whereas mutation of site I altered global complex conformation. These data suggest that CyaA-ACD interaction moderates CaM's Ca2+- and Mg2+-binding capabilities, which may contribute to pathobiology.

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Springer, T. I., Emerson, C. C., Johns, C. W., & Finley, N. L. (2017). Interaction with adenylate cyclase toxin from Bordetella pertussis affects the metal binding properties of calmodulin. FEBS Open Bio, 7(1), 25–34. https://doi.org/10.1002/2211-5463.12138

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