The solution structure of an anti-CRISPR protein

Karen L. Maxwell (), Bianca Garcia, Joseph Bondy-Denomy, Diane Bona, Yurima Hidalgo-Reyes and Alan R. Davidson ()
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Karen L. Maxwell: Donnelly Centre for Cellular and Biomolecular Research, 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

Nature Communications, 2016, vol. 7, issue 1, 1-5

Abstract: 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.

Date: 2016
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13134

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DOI: 10.1038/ncomms13134

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