Solution NMR structures of pyrenophora tritici-repentis toxb and its inactive homolog reveal potential determinants of toxin activity

Afua Nyarko, Kiran K. Singarapu, Melania Figueroa, Viola A. Manning, Iovanna Pandelova, Thomas J. Wolpert, Lynda M. Ciuffetti, Elisar Barbar

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

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 languageEnglish (US)
Pages (from-to)25946-25956
Number of pages11
JournalJournal of Biological Chemistry
Volume289
Issue number37
DOIs
StatePublished - Sep 12 2014

Bibliographical note

Publisher Copyright:
© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

Copyright:
Copyright 2015 Elsevier B.V., All rights reserved.

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