8K28
ICP1 Csy-dsDNA complex (form 1)
Summary for 8K28
| Entry DOI | 10.2210/pdb8k28/pdb |
| EMDB information | 36831 |
| Descriptor | Csy1, Csy2, Csy3, ... (7 entities in total) |
| Functional Keywords | immune system-rna-dna complex, rna binding protein/dna/rna, rna binding protein-dna-rna complex |
| Biological source | Vibrio phage ICP1_2004_A More |
| Total number of polymer chains | 12 |
| Total formula weight | 304129.91 |
| Authors | Zhang, L.X.,Feng, Y. (deposition date: 2023-07-12, release date: 2024-07-17, Last modification date: 2026-01-28) |
| Primary citation | Zhang, L.,Wang, H.,Zeng, J.,Cao, X.,Gao, Z.,Liu, Z.,Li, F.,Wang, J.,Zhang, Y.,Yang, M.,Feng, Y. Cas1 mediates the interference stage in a phage-encoded CRISPR-Cas system. Nat.Chem.Biol., 20:1471-1481, 2024 Cited by PubMed Abstract: Clustered regularly interspaced short palindromic repeats (CRISPR)-Cas systems are prokaryotic adaptive immune systems against invading phages and other mobile genetic elements. Notably, some phages, including the Vibrio cholerae-infecting ICP1 (International Center for Diarrheal Disease Research, Bangladesh cholera phage 1), harbor CRISPR-Cas systems to counteract host defenses. Nevertheless, ICP1 Cas8f lacks the helical bundle domain essential for recruitment of helicase-nuclease Cas2/3 during target DNA cleavage and how this system accomplishes the interference stage remains unknown. Here, we found that Cas1, a highly conserved component known to exclusively work in the adaptation stage, also mediates the interference stage through connecting Cas2/3 to the DNA-bound CRISPR-associated complex for antiviral defense (Cascade; CRISPR system yersinia, Csy) of the ICP1 CRISPR-Cas system. A series of structures of Csy, Csy-dsDNA (double-stranded DNA), Cas1-Cas2/3 and Csy-dsDNA-Cas1-Cas2/3 complexes reveal the whole process of Cas1-mediated target DNA cleavage by the ICP1 CRISPR-Cas system. Together, these data support an unprecedented model in which Cas1 mediates the interference stage in a phage-encoded CRISPR-Cas system and the study also sheds light on a unique model of primed adaptation. PubMed: 38977786DOI: 10.1038/s41589-024-01659-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.54 Å) |
Structure validation
Download full validation report
