Format

Send to

Choose Destination
Nat Struct Mol Biol. 2016 Sep;23(9):868-70. doi: 10.1038/nsmb.3269. Epub 2016 Jul 25.

Structural basis of Cas3 inhibition by the bacteriophage protein AcrF3.

Author information

1
Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, China.
2
National Center for Protein Science Shanghai, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Shanghai Science Research Center, Chinese Academy of Sciences, Shanghai, China.

Abstract

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.

PMID:
27455460
DOI:
10.1038/nsmb.3269
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Nature Publishing Group
Loading ...
Support Center