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The solution structure of an anti-CRISPR protein

Author

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  • Karen L. Maxwell

    (Donnelly Centre for Cellular and Biomolecular Research, University of Toronto
    University of Toronto)

  • Bianca Garcia

    (University of Toronto)

  • Joseph Bondy-Denomy

    (University of Toronto)

  • Diane Bona

    (Donnelly Centre for Cellular and Biomolecular Research, University of Toronto)

  • Yurima Hidalgo-Reyes

    (University of Toronto)

  • Alan R. Davidson

    (University of Toronto
    University of Toronto)

Abstract

Bacterial CRISPR–Cas adaptive immune systems use small guide RNAs to protect against phage infection and invasion by foreign genetic elements. We previously demonstrated that a group of Pseudomonas aeruginosa phages encode anti-CRISPR proteins that inactivate the type I-F and I-E CRISPR–Cas systems using distinct mechanisms. Here, we present the three-dimensional structure of an anti-CRISPR protein and map a functional surface that is critical for its potent inhibitory activity. The interaction of the anti-CRISPR protein with the CRISPR–Cas complex through this functional surface is proposed to prevent the binding of target DNA.

Suggested Citation

  • Karen L. Maxwell & Bianca Garcia & Joseph Bondy-Denomy & Diane Bona & Yurima Hidalgo-Reyes & Alan R. Davidson, 2016. "The solution structure of an anti-CRISPR protein," Nature Communications, Nature, vol. 7(1), pages 1-5, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13134
    DOI: 10.1038/ncomms13134
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