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

共 51 条

[31] Processing of X-ray diffraction data collected in oscillation mode [J].

Otwinowski, Z ;

Minor, W .

MACROMOLECULAR CRYSTALLOGRAPHY, PT A, 1997, 276 :307-326

[32] CRISPR elements in Yersinia pestis acquire new repeats by preferential uptake of bacteriophage DNA, and provide additional tools for evolutionary studies [J].

Pourcel, C ;

Salvignol, G ;

Vergnaud, G .

MICROBIOLOGY-SGM, 2005, 151 :653-663

[33] X-ray crystal structure of a CRISPR-associated RAMP superfamily protein, Cmr5, from Thermus thermophilus HB8 [J].

Sakamoto, Keiko ;

Agari, Yoshihiro ;

Agari, Kazuko ;

Yokoyama, Shigeyuki ;

Kuramitsu, Seiki ;

Shinkai, Akeo .

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2009, 75 (02) :528-532

[34] An RNA-induced conformational change required for CRISPR RNA cleavage by the endoribonuclease Cse3 [J].

Sashital, Dipali G. ;

Jinek, Martin ;

Doudna, Jennifer A. .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2011, 18 (06) :680-U77

[35] A short history of SHELX [J].

Sheldrick, George M. .

ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 2008, 64 :112-122

[36] Structures, mechanism, regulation and evolution of class III nucleotidyl cyclases [J].

Sinha, S. C. ;

Sprang, S. R. .

REVIEWS OF PHYSIOLOGY BIOCHEMISTRY AND PHARMACOLOGY, VOL 157, 2007, 157 :105-140

[37] Cas3 is a single-stranded DNA nuclease and ATP-dependent helicase in the CRISPR/Cas immune system [J].

Sinkunas, Tomas ;

Gasiunas, Giedrius ;

Fremaux, Christophe ;

Barrangou, Rodolphe ;

Horvath, Philippe ;

Siksnys, Virginijus .

EMBO JOURNAL, 2011, 30 (07) :1335-1342

[38] Bicarbonate activation of adenylyl cyclase via promotion of catalytic active site closure and metal recruitment [J].

Steegborn, C ;

Litvin, TN ;

Levin, LR ;

Buck, J ;

Wu, H .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2005, 12 (01) :32-37

[39] DNA polymerases: Structural diversity and common mechanisms [J].

Steitz, TA .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (25) :17395-17398

[40] Identification of 86 candidates for small non-messenger RNAs from the archaeon Archaeoglobus fulgidus [J].

Tang, TH ;

Bachellerie, JP ;

Rozhdestvensky, T ;

Bortolin, ML ;

Huber, H ;

Drungowski, M ;

Elge, T ;

Brosius, J ;

Hüttenhofer, A .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (11) :7536-7541

← 1 2 3 4 5 6 →