Background: ToxB is a proteinaceous toxin but its homolog toxb has no toxic activity.
Results: Both adopt a β-sandwich fold stabilized by two disulfide bonds but differ in the dynamics of one sandwich half.
Conclusion: Toxicity is correlated with decreased compactness, increased flexibility, and polymorphism in an active site loop.
Significance: ToxB activity depends on interplay between internal dynamics and interactions with putative targets.
Bibliographical notePublisher Copyright:
© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
Copyright 2015 Elsevier B.V., All rights reserved.