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Structures of CRISPR Cas3 offer mechanistic insights into Cascade-activated DNA unwinding and degradation.

<div class='caption-title'>Overall structure of ss-DNA-bound T. fusca Cas3 protein</div>
<div class='caption-title'>Domain interfaces inside Cas3</div>
<div class='caption-title'>Substrate recognition and catalysis in the Cas3 HD nuclease</div>
Huo Y, Nam KH, Ding F, Lee H, Wu L, Xiao Y, Farchione MD, Zhou S, Rajashankar K, Kurinov I, Zhang R, Ke A
OpenAccess logo Nat Struct Mol Biol 21 771-7 (2014)
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Cited: 111 times
EuropePMC logo PMID: 25132177

Abstract

CRISPR drives prokaryotic adaptation to invasive nucleic acids such as phages and plasmids, using an RNA-mediated interference mechanism. Interference in type I CRISPR-Cas systems requires a targeting Cascade complex and a degradation machine, Cas3, which contains both nuclease and helicase activities. Here we report the crystal structures of Thermobifida fusca Cas3 bound to single-stranded (ss) DNA substrate and show that it is an obligate 3'-to-5' ssDNase that preferentially accepts substrate directly from the helicase moiety. Conserved residues in the HD-type nuclease coordinate two irons for ssDNA cleavage. We demonstrate ATP coordination and conformational flexibility of the SF2-type helicase domain. Cas3 is specifically guided toward Cascade-bound target DNA by a PAM sequence, through physical interactions with both the nontarget substrate strand and the CasA protein. The sequence of recognition events ensures well-controlled DNA targeting and degradation of foreign DNA by Cascade and Cas3.

Reviews - 4qqw mentioned but not cited (4)

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Articles - 4qqw mentioned but not cited (9)

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