9LO2
Crystal Structure of Anti-CRISPR protein
Summary for 9LO2
| Entry DOI | 10.2210/pdb9lo2/pdb |
| Descriptor | Anti-CRISPR protein, AcrIE7 (2 entities in total) |
| Functional Keywords | anti-crispr protein, viral protein |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 3 |
| Total formula weight | 36043.82 |
| Authors | |
| Primary citation | Kang, J.,Park, C.,Lee, G.,Koo, J.,Oh, H.,Kim, E.H.,Bae, E.,Suh, J.Y. Structural Investigation of the Anti-CRISPR Protein AcrIE7. Proteins, 2025 Cited by PubMed Abstract: The CRISPR-Cas system is an adaptive immune system in prokaryotes that provides protection against bacteriophages. As a countermeasure, bacteriophages have evolved various anti-CRISPR proteins that neutralize CRISPR-Cas immunity. Here, we report the structural and functional investigation of AcrIE7, which inhibits the type I-E CRISPR-Cas system in Pseudomonas aeruginosa. We determined both crystal and solution structures of AcrIE7, which revealed a novel helical fold. In binding assays using various biochemical methods, AcrIE7 did not tightly interact with a single Cas component in the type I-E Cascade complex or the CRISPR adaptation machinery. In contrast, AlphaFold modeling with our experimentally determined AcrIE7 structure predicted that AcrIE7 interacts with Cas3 in the type I-E CRISPR-Cas system in P. aeruginosa. Our findings are consistent with a model where AcrIE7 inhibits Cas3 and also highlight the effectiveness and limitations of AlphaFold modeling. PubMed: 40318042DOI: 10.1002/prot.26832 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.287 Å) |
Structure validation
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