کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2048522 1074082 2012 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Crystal structure of Cmr2 suggests a nucleotide cyclase-related enzyme in type III CRISPR-Cas systems
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Crystal structure of Cmr2 suggests a nucleotide cyclase-related enzyme in type III CRISPR-Cas systems
چکیده انگلیسی

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.


► The crystal structure of CRISPR-associated protein Cmr2 was determined.
► Cmr2 is a structural homolog of adenylate cyclase dimer with a putative active site.
► Cmr2 also contains a polymerase thumb-like domain and a Cmr5-like domain.
► Cmr2 is likely an enzyme with novel activity on nucleotides or nucleic acids.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 586, Issue 6, 23 March 2012, Pages 939–945
نویسندگان
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