7VZM
Anti-CRISPR AcrIE4-F7
Summary for 7VZM
| Entry DOI | 10.2210/pdb7vzm/pdb |
| Descriptor | AcrIE4-F7 (1 entity in total) |
| Functional Keywords | crispr inhibitor, viral protein |
| Biological source | Pseudomonas citronellolis |
| Total number of polymer chains | 1 |
| Total formula weight | 13521.67 |
| Authors | Hong, S.H.,Lee, G.,Bae, E.,Suh, J.Y. (deposition date: 2021-11-16, release date: 2022-02-09, Last modification date: 2024-05-15) |
| Primary citation | Hong, S.H.,Lee, G.,Park, C.,Koo, J.,Kim, E.H.,Bae, E.,Suh, J.Y. The structure of AcrIE4-F7 reveals a common strategy for dual CRISPR inhibition by targeting PAM recognition sites. Nucleic Acids Res., 50:2363-2376, 2022 Cited by PubMed Abstract: Bacteria and archaea use the CRISPR-Cas system to fend off invasions of bacteriophages and foreign plasmids. In response, bacteriophages encode anti-CRISPR (Acr) proteins that potently inhibit host Cas proteins to suppress CRISPR-mediated immunity. AcrIE4-F7, which was isolated from Pseudomonas citronellolis, is a fused form of AcrIE4 and AcrIF7 that inhibits both type I-E and type I-F CRISPR-Cas systems. Here, we determined the structure of AcrIE4-F7 and identified its Cas target proteins. The N-terminal AcrIE4 domain adopts a novel α-helical fold that targets the PAM interaction site of the type I-E Cas8e subunit. The C-terminal AcrIF7 domain exhibits an αβ fold like native AcrIF7, which disables target DNA recognition by the PAM interaction site in the type I-F Cas8f subunit. The two Acr domains are connected by a flexible linker that allows prompt docking onto their cognate Cas8 targets. Conserved negative charges in each Acr domain are required for interaction with their Cas8 targets. Our results illustrate a common mechanism by which AcrIE4-F7 inhibits divergent CRISPR-Cas types. PubMed: 35166843DOI: 10.1093/nar/gkac096 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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