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.

Links

Publisher Full Text

Authors

Zhu X, Ye K

Institution

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

Source

FEBS letters 586:6 2012 Mar 23 pg 939-45

MeSH

Amino Acid Sequence
Archaeal Proteins
Catalytic Domain
Crystallography, X-Ray
Models, Molecular
Molecular Sequence Data
Protein Structure, Tertiary
Pyrococcus furiosus
RNA
RNA-Binding Proteins
Sequence Alignment

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22449983