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FEBS Lett. 2012 Mar 23;586(6):939-45. doi: 10.1016/j.febslet.2012.02.036. Epub 2012 Feb 28.

Crystal structure of Cmr2 suggests a nucleotide cyclase-related enzyme in type III CRISPR-Cas systems.

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1
College of Life Sciences, Beijing Normal University, Beijing 100875, China.

Abstract

CRISPR RNAs (crRNAs) mediate sequence-specific silencing of invading viruses and plasmids in prokaryotes. The crRNA-Cmr protein complex cleaves complementary RNA. We report the crystal structure of Pyrococcus furiosus Cmr2 (Cas10), a component of this Cmr complex and the signature protein in type III CRISPR systems. The structure reveals a nucleotide cyclase domain with a set of conserved catalytic residues that associates with an unexpected deviant cyclase domain like dimeric cyclases. Additionally, two helical domains resemble the thumb domain of A-family DNA polymerase and Cmr5, respectively. Our results suggest that Cmr2 possesses novel enzymatic activity that remains to be elucidated.

PMID:
22449983
DOI:
10.1016/j.febslet.2012.02.036
[Indexed for MEDLINE]
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