4ZT0
Crystal structure of catalytically-active Streptococcus pyogenes Cas9 in complex with single-guide RNA at 2.9 Angstrom resolution
Summary for 4ZT0
| Entry DOI | 10.2210/pdb4zt0/pdb |
| Related | 4ZT9 |
| Descriptor | CRISPR-associated endonuclease Cas9, single-guide RNA (2 entities in total) |
| Functional Keywords | crispr-cas9, bacteria adaptive immunity, dna endonuclease, hydrolase-rna complex, genome editing and regulation, hydrolase/rna |
| Biological source | Streptococcus pyogenes More |
| Total number of polymer chains | 4 |
| Total formula weight | 374612.00 |
| Authors | Jiang, F.,Doudna, J.A. (deposition date: 2015-05-14, release date: 2015-07-08, Last modification date: 2024-11-06) |
| Primary citation | Jiang, F.,Zhou, K.,Ma, L.,Gressel, S.,Doudna, J.A. A Cas9-guide RNA complex preorganized for target DNA recognition. Science, 348:1477-1481, 2015 Cited by PubMed Abstract: Bacterial adaptive immunity uses CRISPR (clustered regularly interspaced short palindromic repeats)-associated (Cas) proteins together with CRISPR transcripts for foreign DNA degradation. In type II CRISPR-Cas systems, activation of Cas9 endonuclease for DNA recognition upon guide RNA binding occurs by an unknown mechanism. Crystal structures of Cas9 bound to single-guide RNA reveal a conformation distinct from both the apo and DNA-bound states, in which the 10-nucleotide RNA "seed" sequence required for initial DNA interrogation is preordered in an A-form conformation. This segment of the guide RNA is essential for Cas9 to form a DNA recognition-competent structure that is poised to engage double-stranded DNA target sequences. We construe this as convergent evolution of a "seed" mechanism reminiscent of that used by Argonaute proteins during RNA interference in eukaryotes. PubMed: 26113724DOI: 10.1126/science.aab1452 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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