Structural basis of Cas3 inhibition by the bacteriophage protein AcrF3.

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.

journal_name

Nat Struct Mol Biol

authors

Wang X,Yao D,Xu JG,Li AR,Xu J,Fu P,Zhou Y,Zhu Y

doi

10.1038/nsmb.3269

subject

Has Abstract

pub_date

2016-09-01 00:00:00

pages

868-70

issue

9

eissn

1545-9993

issn

1545-9985

pii

nsmb.3269

journal_volume

23

pub_type

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