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

doi:10.1074/jbc.M114.569103

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

Plant Pathology

Research output: Contribution to journal › Article › peer-review

31 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 language	English (US)
Pages (from-to)	25946-25956
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	289
Issue number	37
DOIs	https://doi.org/10.1074/jbc.M114.569103
State	Published - Sep 12 2014

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

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

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.",

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AU - Nyarko, Afua

AU - Singarapu, Kiran K.

AU - Figueroa, Melania

AU - Manning, Viola A.

AU - Pandelova, Iovanna

AU - Wolpert, Thomas J.

AU - Ciuffetti, Lynda M.

AU - Barbar, Elisar

PY - 2014/9/12

Y1 - 2014/9/12

N2 - 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.

AB - 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.

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

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