7FIA
Structure of AcrIF23
Summary for 7FIA
Entry DOI | 10.2210/pdb7fia/pdb |
Descriptor | AcrIF23 (2 entities in total) |
Functional Keywords | inhibitor, viral protein |
Biological source | Pseudomonas aeruginosa |
Total number of polymer chains | 1 |
Total formula weight | 17716.77 |
Authors | |
Primary citation | Ren, J.,Wang, H.,Yang, L.,Li, F.,Wu, Y.,Luo, Z.,Chen, Z.,Zhang, Y.,Feng, Y. Structural and mechanistic insights into the inhibition of type I-F CRISPR-Cas system by anti-CRISPR protein AcrIF23. J.Biol.Chem., 298:102124-102124, 2022 Cited by PubMed Abstract: Prokaryotes evolved clustered regularly interspaced short palindromic repeats (CRISPR) and CRISPR-associated (Cas) proteins as a kind of adaptive immune defense against mobile genetic elements including harmful phages. To counteract this defense, many mobile genetic elements in turn encode anti-CRISPR proteins (Acrs) to inactivate the CRISPR-Cas system. While multiple mechanisms of Acrs have been uncovered, it remains unknown whether other mechanisms are utilized by uncharacterized Acrs. Here, we report a novel mechanism adopted by recently identified AcrIF23. We show that AcrIF23 interacts with the Cas2/3 helicase-nuclease in the type I-F CRISPR-Cas system, similar to AcrIF3. The structure of AcrIF23 demonstrated a novel fold and structure-based mutagenesis identified a surface region of AcrIF23 involved in both Cas2/3-binding and its inhibition capacity. Unlike AcrIF3, however, we found AcrIF23 only potently inhibits the DNA cleavage activity of Cas2/3 but does not hinder the recruitment of Cas2/3 to the CRISPR RNA-guided surveillance complex (the Csy complex). Also, in contrast to AcrIF3 which hinders substrate DNA recognition by Cas2/3, we show AcrIF23 promotes DNA binding to Cas2/3. Taken together, our study identifies a novel anti-CRISPR mechanism used by AcrIF23 and highlights the diverse mechanisms adopted by Acrs. PubMed: 35697070DOI: 10.1016/j.jbc.2022.102124 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.13 Å) |
Structure validation
Download full validation report
