☆ 4.5 Article

Structural basis of Cas3 inhibition by the bacteriophage protein AcrF3

NATURE STRUCTURAL & MOLECULAR BIOLOGY (2016)

期刊

NATURE STRUCTURAL & MOLECULAR BIOLOGY

卷 23, 期 9, 页码 868-870

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NATURE PUBLISHING GROUP

DOI: 10.1038/nsmb.3269

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Biochemistry & Molecular Biology Biophysics Cell Biology

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National Natural Science Foundation of China [81322024, 81561130162, 31370722, 81530068, 81501717]
Natural Science Foundation of Zhejiang Province [LR13C05001]
Royal Society [NA140239]

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Bacteriophages express proteins that inactivate the CRISPR-Cas bacterial immune system. Here we report the crystal structure of the anti-CRISPR protein AcrF3 in complex with Pseudomonas aeruginosa Cas3 (PaCas3). AcrF3 forms a homodimer that locks PaCas3 in an ADP-bound form, blocks the entrance of the DNA-binding tunnel in the helicase domain, and masks the linker region and C-terminal domain of PaCas3, thereby preventing recruitment by Cascade and inhibiting the type I-F CRISPR-Cas system.

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