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4TVX

Crystal structure of the E. coli CRISPR RNA-guided surveillance complex, Cascade

This is a non-PDB format compatible entry.
Summary for 4TVX
Entry DOI10.2210/pdb4tvx/pdb
DescriptorCRISPR system Cascade subunit CasB, CRISPR system Cascade subunit CasC, CRISPR system Cascade subunit CasE, ... (7 entities in total)
Functional Keywordscrispr, rna, surveillance, complex, hydrolase-rna complex, hydrolase/rna
Biological sourceEscherichia coli
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Total number of polymer chains24
Total formula weight804324.65
Authors
Jackson, R.N.,Golden, S.M.,Carter, J.,Wiedenheft, B. (deposition date: 2014-06-28, release date: 2014-08-13, Last modification date: 2024-10-23)
Primary citationJackson, R.N.,Golden, S.M.,van Erp, P.B.,Carter, J.,Westra, E.R.,Brouns, S.J.,van der Oost, J.,Terwilliger, T.C.,Read, R.J.,Wiedenheft, B.
Structural biology. Crystal structure of the CRISPR RNA-guided surveillance complex from Escherichia coli.
Science, 345:1473-1479, 2014
Cited by
PubMed Abstract: 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.
PubMed: 25103409
DOI: 10.1126/science.1256328
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.24 Å)
Structure validation

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