ArticleProtein science : a publication of the Protein Society2016
Structural features of Cas2 from Thermococcus onnurineus in CRISPR-cas system type IV.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Insights into the inhibition of protospacer integration via direct interaction between Cas2 and AcrVA5.Nature communications · 2024Article
- Structural and functional analyses of Burkholderia pseudomallei BPSL1038 reveal a Cas-2/VapD nuclease sub-family.Communications biology · 2023Article
- Structural and functional characterization of Cas2 of CRISPR-Cas subtype I-C lacking the CRISPR component.Frontiers in molecular biosciences · 2022Article
- Global phylogenomic novelty of the Cas1 gene from hot spring microbial communities.Frontiers in microbiology · 2022Article
- Characterization of 67 Confirmed Clustered Regularly Interspaced Short Palindromic Repeats Loci in 52 Strains ofFrontiers in microbiology · 2021Article
- Structure of the DNA-Bound Spacer Capture Complex of a Type II CRISPR-Cas System.Molecular cell · 2019Article
- Structural and dynamic insights into the role of conformational switching in the nuclease activity of theStructural dynamics (Melville, N.Y.) · 2017Article
- RNA activation-independent DNA targeting of the Type III CRISPR-Cas system by a Csm complex.EMBO reports · 2017Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CRISPR-Cas is RNA-based prokaryotic immune systems that defend against exogenous genetic elements such as plasmids and viruses. Cas1 and Cas2 are highly conserved components that play an essential part in the adaptation stage of all CRISPR-Cas systems. Characterization of CRISPR-Cas genes in Thermococcus onnurineus reveals the association of the Cas2 gene with the putative type IV system that lacks Cas1 or its homologous genes. Here, we present a crystal structure of T. onnurineus Cas2 (Ton_Cas2) that exhibits a deep and wide cleft at an interface lined with positive residues (Arg16, Lys18, Lys19, Arg22, and Arg23). The obvious DNA recognizing loops in Cas2 from E. coli (Eco_Cas2) are absent in Ton_Cas2 and have significantly different shapes and electrostatic potential distributions around the putative nucleotide binding region. Furthermore, Ton_Cas2 lacks the hairpin motif at the C-terminus that is responsible for Cas1 binding in Eco_Cas2. These structural features could be a unique signature and indicate an altered functional mechanism in the adaptation stage of Cas2 in type IV CRISPR-Cas systems.
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