Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 25946-25956 |
| Number of pages | 11 |
| Journal | Journal of Biological Chemistry |
| Volume | 289 |
| Issue number | 37 |
| DOIs | |
| State | Published - Sep 12 2014 |
Bibliographical note
Publisher Copyright:© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
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