7DTR
Structure of an AcrIF protein
Summary for 7DTR
| Entry DOI | 10.2210/pdb7dtr/pdb |
| Descriptor | AcrIF24 (2 entities in total) |
| Functional Keywords | hth motif, protein interaction, viral protein |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 1 |
| Total formula weight | 18587.83 |
| Authors | Yue, F.,Peipei, Y. (deposition date: 2021-01-06, release date: 2022-01-19, Last modification date: 2024-05-29) |
| 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 | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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