Abstract
Background: VahC toxin from Aeromonas hydrophila inactivates actin by transferring ADP-ribose from NAD+. Results: The crystal structure of VahC reveals new insights into the interaction of the actin substrate with the actin-targeting toxins, and consequently, potent inhibitors have been developed. Conclusion: Broad spectrum inhibitors have been developed against actin-targeting toxins from the ADP-ribosyltransferase family. Significance: This new insight provides impetus for therapeutic development for treating bacterial diseases. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Shniffer, A., Visschedyk, D. D., Ravulapalli, R., Suarez, G., Turgeon, Z. J., Petrie, A. A., … Merrill, A. R. (2012). Characterization of an actin-targeting ADP-ribosyltransferase from Aeromonas hydrophila. Journal of Biological Chemistry, 287(44), 37030–37041. https://doi.org/10.1074/jbc.M112.397612
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