Summary for 9IRG
| Entry DOI | 10.2210/pdb9irg/pdb |
| EMDB information | 60813 |
| Descriptor | CRISPR-associated protein Csy3, RNA (162-MER) (2 entities in total) |
| Functional Keywords | rna binding protein/rna, rna binding protein-rna complex |
| Biological source | Pectobacterium atrosepticum SCRI1043 More |
| Total number of polymer chains | 27 |
| Total formula weight | 1013137.54 |
| Authors | |
| Primary citation | Gao, X.,Zhu, K.,Zhang, W.,Wang, L.,Wang, L.,Hua, L.,Niu, T.,Qin, B.,Yu, X.,Zhu, H.,Cui, S. RNA anti-CRISPRs deplete Cas proteins to inhibit the CRISPR-Cas system. Mol.Cell, 2025 Cited by PubMed Abstract: RNA-based anti-CRISPRs (Racrs) interfere with the type I-F CRISPR-Cas system by mimicking the repeats found in CRISPR arrays. Here, we determined the cryo-electron microscopy (cryo-EM) structures of the type I-F crRNA-guided surveillance complex (Csy complex) from Pectobacterium atrosepticum and three RacrIF1-induced aberrant subcomplexes. Additionally, we observed that Cas7f proteins could bind to non-specific nucleic acids, forming right-handed superhelical filaments composed of different Cas7 copies. Mechanistically, RacrIF1 lacks the specific S-conformation observed in the corresponding position of the 5' handle in canonical CRISPR complexes, and it instead adopts a periodic "5 + 1" pattern. This conformation creates severe steric hindrance for Cas5f-Cas8f heterodimer and undermines their binding. Furthermore, Cas7f nonspecifically binds nucleic acids and can form infinite superhelical filaments along Racrs molecules. This oligomerization sequesters Cas6f and Cas7f from binding, therefore blocking the formation of functional CRISPR-Cas effector complexes and ultimately blocking antiviral immunity. Our study provides a structural basis underlying Racrs-mediated CRISPRs inhibition. PubMed: 41475348DOI: 10.1016/j.molcel.2025.12.005 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.59 Å) |
Structure validation
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