期刊
SCIENCE
卷 345, 期 6203, 页码 1479-1484出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1256996
关键词
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资金
- NIH [GM097330, P41GM103473, P41GM103393]
- Office of Biological and Environmental Research of U.S. Department of Energy (DOE)
- Office of Basic Energy Sciences of U.S. Department of Energy (DOE)
- National Center for Research Resources [P41RR012408]
- DOE Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research
In prokaryotes, RNA derived from type I and type III CRISPR loci direct large ribonucleoprotein complexes to destroy invading bacteriophage and plasmids. In Escherichia coli, this 405-kilodalton complex is called Cascade. We report the crystal structure of Cascade bound to a single-stranded DNA (ssDNA) target at a resolution of 3.03 angstroms. The structure reveals that the CRISPR RNA and target strands do not form a double helix but instead adopt an underwound ribbon-like structure. This noncanonical structure is facilitated by rotation of every sixth nucleotide out of the RNA-DNA hybrid and is stabilized by the highly interlocked organization of protein subunits. These studies provide insight into both the assembly and the activity of this complex and suggest a mechanism to enforce fidelity of target binding.
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