7WE6
Structure of Csy-AcrIF24-dsDNA
Summary for 7WE6
Entry DOI | 10.2210/pdb7we6/pdb |
EMDB information | 32440 |
Descriptor | CRISPR type I-F/YPEST-associated protein Csy2, CRISPR-associated protein Csy3, Type I-F CRISPR-associated endoribonuclease Cas6/Csy4, ... (8 entities in total) |
Functional Keywords | complex, inhibitor, immune system, immune system-rna complex, viral protein |
Biological source | Pseudomonas aeruginosa More |
Total number of polymer chains | 26 |
Total formula weight | 820541.35 |
Authors | |
Primary citation | Yang, L.,Zhang, L.,Yin, P.,Ding, H.,Xiao, Y.,Zeng, J.,Wang, W.,Zhou, H.,Wang, Q.,Zhang, Y.,Chen, Z.,Yang, M.,Feng, Y. Insights into the inhibition of type I-F CRISPR-Cas system by a multifunctional anti-CRISPR protein AcrIF24. Nat Commun, 13:1931-1931, 2022 Cited by PubMed Abstract: CRISPR-Cas systems are prokaryotic adaptive immune systems and phages use anti-CRISPR proteins (Acrs) to counteract these systems. Here, we report the structures of AcrIF24 and its complex with the crRNA-guided surveillance (Csy) complex. The HTH motif of AcrIF24 can bind the Acr promoter region and repress its transcription, suggesting its role as an Aca gene in self-regulation. AcrIF24 forms a homodimer and further induces dimerization of the Csy complex. Apart from blocking the hybridization of target DNA to the crRNA, AcrIF24 also induces the binding of non-sequence-specific dsDNA to the Csy complex, similar to AcrIF9, although this binding seems to play a minor role in AcrIF24 inhibitory capacity. Further structural and biochemical studies of the Csy-AcrIF24-dsDNA complexes and of AcrIF24 mutants reveal that the HTH motif of AcrIF24 and the PAM recognition loop of the Csy complex are structural elements essential for this non-specific dsDNA binding. Moreover, AcrIF24 and AcrIF9 display distinct characteristics in inducing non-specific DNA binding. Together, our findings highlight a multifunctional Acr and suggest potential wide distribution of Acr-induced non-specific DNA binding. PubMed: 35411005DOI: 10.1038/s41467-022-29581-1 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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