9H2M
Cas9:crRNA:tracrRNA in complex with PAM-containing non-cognate DNA, PAM-unbound conformation, Streptococcus thermophilus DGCC 7710 CRISPR3 system
Summary for 9H2M
| Entry DOI | 10.2210/pdb9h2m/pdb |
| EMDB information | 51812 |
| Descriptor | CRISPR-associated endonuclease Cas9, crRNA (26-MER), tracrRNA (65-MER), ... (6 entities in total) |
| Functional Keywords | cas9, pam, crispr-cas, rna binding protein, dna binding protein |
| Biological source | Streptococcus thermophilus DGCC 7710 More |
| Total number of polymer chains | 5 |
| Total formula weight | 230453.42 |
| Authors | Sasnauskas, G.,Gaizauskaite, U.,Tamulaitiene, G. (deposition date: 2024-10-12, release date: 2026-02-18, Last modification date: 2026-03-18) |
| Primary citation | Gaizauskaite, U.,Tamulaitiene, G.,Silanskas, A.,Gasiunas, G.,Siksnys, V.,Sasnauskas, G. Structural insights into Cas9-mediated prespacer selection in CRISPR-Cas adaptation. Mol.Cell, 86:791-804.e9, 2026 Cited by PubMed Abstract: During CRISPR-Cas adaptation, prokaryotic cells become immunized by the insertion of foreign DNA fragments, termed spacers, into the host genome to serve as templates for RNA-guided immunity. Spacer acquisition relies on the Cas1-Cas2 integrase and accessory proteins, which select DNA sequences flanked by the protospacer adjacent motif (PAM) and insert them into the CRISPR array. It has been shown that in type II-A systems, selection of PAM-proximal prespacers is mediated by the effector nuclease Cas9, which forms a "supercomplex" with the Cas1-Cas2 integrase and the Csn2 protein. Here, we present cryo-electron microscopy structures of the Streptococcus thermophilus type II-A prespacer selection supercomplex in the DNA-scanning and two distinct PAM-bound configurations, providing insights into the mechanism of Cas9-mediated prespacer selection in type II-A CRISPR-Cas systems. Repurposing Cas9 by the CRISPR adaptation machinery for prespacer selection, as characterized here, demonstrates Cas9 plasticity and expands our knowledge of Cas9 biology. PubMed: 41702403DOI: 10.1016/j.molcel.2026.01.022 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.06 Å) |
Structure validation
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