2XLK

Crystal structure of the Csy4-crRNA complex, orthorhombic form

Summary for 2XLK

• Entry DOI: 10.2210/pdb2xlk/pdb
• Related: 2XLI 2XLJ
• Descriptor: CSY4 ENDORIBONUCLEASE, 5'-R(*CP*UP*GP*CP*CP*GP*UP*AP*UP*AP*GP*GP*CP*A*DG*C)-3' (3 entities in total)
• Functional Keywords: hydrolase-rna complex, endoribonuclease, crispr, hydrolase/rna
• Biological source: PSEUDOMONAS AERUGINOSA; More
• Total number of polymer chains: 4
• Total formula weight: 53926.19

Authors

Haurwitz, R.E.,Jinek, M.,Wiedenheft, B.,Zhou, K.,Doudna, J.A. (deposition date: 2010-07-21, release date: 2010-09-22, Last modification date: 2023-12-20)

Primary citation

Haurwitz, R.E.,Jinek, M.,Wiedenheft, B.,Zhou, K.,Doudna, J.A.
Sequence- and Structure-Specific RNA Processing by a Crispr Endonuclease.
Science, 329:1355-, 2010

PubMed Abstract: Many bacteria and archaea contain clustered regularly interspaced short palindromic repeats (CRISPRs) that confer resistance to invasive genetic elements. Central to this immune system is the production of CRISPR-derived RNAs (crRNAs) after transcription of the CRISPR locus. Here, we identify the endoribonuclease (Csy4) responsible for CRISPR transcript (pre-crRNA) processing in Pseudomonas aeruginosa. A 1.8 angstrom crystal structure of Csy4 bound to its cognate RNA reveals that Csy4 makes sequence-specific interactions in the major groove of the crRNA repeat stem-loop. Together with electrostatic contacts to the phosphate backbone, these enable Csy4 to bind selectively and cleave pre-crRNAs using phylogenetically conserved serine and histidine residues in the active site. The RNA recognition mechanism identified here explains sequence- and structure-specific processing by a large family of CRISPR-specific endoribonucleases.

PubMed: 20829488
DOI: 10.1126/SCIENCE.1192272

Experimental method

X-RAY DIFFRACTION (1.805 Å)