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

被引：45

作者：

Zhu, Xing ^{[1
,2
]}

Ye, Keqiong ^{[1
]}

机构：

[1] Natl Inst Biol Sci, Beijing 102206, Peoples R China

[2] Beijing Normal Univ, Coll Life Sci, Beijing 100875, Peoples R China

来源：

FEBS LETTERS | 2012年 / 586卷 / 06期

关键词：

CRISPR; Nucleotide cyclase; X-ray crystallography; ADENYLYL-CYCLASE; IMMUNE-SYSTEM; RNA CLEAVAGE; DNA; PROTEIN; BACTERIA; REPEATS; RECOGNITION; EVOLUTION; SEQUENCE;

D O I：

10.1016/j.febslet.2012.02.036

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：939 / 945

页数：7

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