2Y8Y

Structure B of CRISPR endoribonuclease Cse3 bound to 19 nt RNA

Summary for 2Y8Y

• Entry DOI: 10.2210/pdb2y8y/pdb
• Related: 1WJ9 2Y8W 2Y9H
• Descriptor: CSE3, 5'-R(*UP*CP*CP*CP*CP*AP*CP*GP*CP*GP*UP*GP*UP*GP *GP*GP*DGP*AP*U)-3' (3 entities in total)
• Functional Keywords: hydrolase-rna complex, ferredoxin-like, hydrolase/rna
• Biological source: THERMUS THERMOPHILUS
• Total number of polymer chains: 2
• Total formula weight: 30119.62

Authors

Sashital, D.G.,Jinek, M.,Doudna, J.A. (deposition date: 2011-02-11, release date: 2011-05-18, Last modification date: 2024-01-31)

Primary citation

Sashital, D.G.,Jinek, M.,Doudna, J.A.
An RNA-Induced Conformational Change Required for Crispr RNA Cleavage by the Endoribonuclease Cse3.
Nat.Struct.Mol.Biol., 18:680-, 2011

PubMed Abstract: Clustered regularly interspaced short palindromic repeat (CRISPR) chromosomal loci found in prokaryotes provide an adaptive immune system against bacteriophages and plasmids. CRISPR-specific endoRNases produce short RNA molecules (crRNAs) from CRISPR transcripts, which harbor sequences complementary to invasive nucleic acid elements and ensure their selective targeting by CRISPR-associated (Cas) proteins. The extreme sequence divergence of CRISPR-specific endoRNases and their RNA substrates has obscured homology-based comparison of RNA recognition and cleavage mechanisms. Here, we show that Cse3 type CRISPR-specific endoRNases bind a hairpin structure and residues downstream of the cleavage site within the repetitive segment of cognate CRISPR RNA. Cocrystal structures of Cse3-RNA complexes reveal an RNA-induced conformational change in the enzyme active site that aligns the RNA strand for site-specific cleavage. These studies provide insight into a catalytically essential RNA recognition mechanism by a large class of CRISPR-related endoRNases.

PubMed: 21572442
DOI: 10.1038/NSMB.2043

Experimental method

X-RAY DIFFRACTION (1.44 Å)