Journal
SCIENCE
Volume 345, Issue 6203, Pages 1473-1479Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1256328
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Funding
- European Union under REA grant [327606]
- Netherlands Organization of Scientific Research [864.11.005]
- Vici grant [865.05.001]
- Wellcome Trust [082961/Z/07/Z]
- NIH [GM063210, F32 GM108436, P20GM103500, R01GM108888]
- Howard Hughes Medical Institute [52006931]
- NSF Experimental Program to Stimulate Competitive Research [EPS-110134]
- M. J. Murdock Charitable Trust
- Montana State University Agricultural Experiment Station
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Clustered regularly interspaced short palindromic repeats (CRISPRs) are essential components of RNA-guided adaptive immune systems that protect bacteria and archaea from viruses and plasmids. In Escherichia coli, short CRISPR-derived RNAs (crRNAs) assemble into a 405-kilodalton multisubunit surveillance complex called Cascade (CRISPR-associated complex for antiviral defense). Here we present the 3.24 angstrom resolution x-ray crystal structure of Cascade. Eleven proteins and a 61-nucleotide crRNA assemble into a seahorse-shaped architecture that binds double-stranded DNA targets complementary to the crRNA-guide sequence. Conserved sequences on the 3' and 5' ends of the crRNA are anchored by proteins at opposite ends of the complex, whereas the guide sequence is displayed along a helical assembly of six interwoven subunits that present five-nucleotide segments of the crRNA in pseudo-A-form configuration. The structure of Cascade suggests a mechanism for assembly and provides insights into the mechanisms of target recognition.
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