ArticleStructure (London, England : 1993)2012
Structure of the Cmr2 subunit of the CRISPR-Cas RNA silencing complex.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 76 citations in OpenAlex.
- Molecular basis of SAM-AMP synthesis and degradation in the type III-B CRISPR-Cas system.Nature chemical biology · 2026Article
- Structural and functional insights into the adenosine deaminase of the type III-B CRISPR-Cas system.Nucleic acids research · 2026Article
- Article
- Functional and Phylogenetic Diversity of Cas10 Proteins.The CRISPR journal · 2023Article
- HIV infection detection using CRISPR/Cas systems: Present and future prospects.Computational and structural biotechnology journal · 2023Review
- Specificity and sensitivity of an RNA targeting type III CRISPR complex coupled with a NucC endonuclease effector.Nucleic acids research · 2021Article
- Review
- Regulation of the RNA and DNA nuclease activities required for Pyrococcus furiosus Type III-B CRISPR-Cas immunity.Nucleic acids research · 2020Article
- PAM identification by CRISPR-Cas effector complexes: diversified mechanisms and structures.RNA biology · 2019Article
- A Type III-B Cmr effector complex catalyzes the synthesis of cyclic oligoadenylate second messengers by cooperative substrate binding.Nucleic acids research · 2018Article
- A type III-B CRISPR-Cas effector complex mediating massive target DNA destruction.Nucleic acids research · 2017Article
- Harnessing Type I and Type III CRISPR-Cas systems for genome editing.Nucleic acids research · 2016Article
- RNA-activated DNA cleavage by the Type III-B CRISPR-Cas effector complex.Genes & development · 2016Article
- Bipartite recognition of target RNAs activates DNA cleavage by the Type III-B CRISPR-Cas system.Genes & development · 2016Article
- Comparative genomic analyses reveal a vast, novel network of nucleotide-centric systems in biological conflicts, immunity and signaling.Nucleic acids research · 2015Article
- Diversity of CRISPR-Cas immune systems and molecular machines.Genome biology · 2015Review
- Purification, crystallization, crystallographic analysis and phasing of the CRISPR-associated protein Csm2 from Thermotoga maritima.Acta crystallographica. Section F, Structural biology communications · 2015Article
- A Conserved Structural Chassis for Mounting Versatile CRISPR RNA-Guided Immune Responses.Molecular cell · 2015Review
- Crystallization and preliminary X-ray diffraction analysis of the CRISPR-Cas RNA-silencing Cmr complex.Acta crystallographica. Section F, Structural biology communications · 2015Article
- DNA and RNA interference mechanisms by CRISPR-Cas surveillance complexes.FEMS microbiology reviews · 2015Review
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7 authors at 2 institutions in 1 country.
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Abstract
Cmr2 is the largest and an essential subunit of a CRISPR RNA-Cas protein complex (the Cmr complex) that cleaves foreign RNA to protect prokaryotes from invading genetic elements. Cmr2 is thought to be the catalytic subunit of the effector complex because of its N-terminal HD nuclease domain. Here, however, we report that the HD domain of Cmr2 is not required for cleavage by the complex in vitro. The 2.3Å crystal structure of Pyrococcus furiosus Cmr2 (lacking the HD domain) reveals two adenylyl cyclase-like and two α-helical domains. The adenylyl cyclase-like domains are arranged as in homodimeric adenylyl cyclases and bind ADP and divalent metals. However, mutagenesis studies show that the metal- and ADP-coordinating residues of Cmr2 are also not critical for cleavage by the complex. Our findings suggest that another component provides the catalytic function and that the essential role by Cmr2 does not require the identified ADP- or metal-binding or HD domains in vitro.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.