7F7P
AcrIIC4
Summary for 7F7P
Entry DOI | 10.2210/pdb7f7p/pdb |
Descriptor | anti-CRISPR protein AcrIIC4 (2 entities in total) |
Functional Keywords | anti-crispr acriic4, inhibitor of crispr-cas 9, immune system |
Biological source | Haemophilus parainfluenzae |
Total number of polymer chains | 2 |
Total formula weight | 22112.94 |
Authors | Kim, G.E.,Park, H.H. (deposition date: 2021-06-30, release date: 2022-05-25, Last modification date: 2024-05-29) |
Primary citation | Kim, G.E.,Lee, S.Y.,Park, H.H. Crystal structure of the anti-CRISPR, AcrIIC4. Protein Sci., 30:2474-2481, 2021 Cited by PubMed Abstract: Clustered regularly interspaced short palindromic repeats (CRISPRs)-CRISPR-associated protein systems are bacterial and archaeal defense mechanisms against invading elements such as phages and viruses. To overcome these defense systems, phages and viruses have developed inhibitors called anti-CRISPRs (Acrs) that are capable of inhibiting the host CRISPR-Cas system via different mechanisms. Although the inhibitory mechanisms of AcrIIC1, AcrIIC2, and AcrIIC3 have been revealed, the inhibitory mechanisms of AcrIIC4 and AcrIIC5 have not been fully understood and structural data are unavailable. In this study, we elucidated the crystal structure of Type IIC anti-CRISPR protein, AcrIIC4. Our structural analysis revealed that AcrIIC4 exhibited a helical bundle fold comprising four helixes. Further biochemical and biophysical analyses showed that AcrIIC4 formed a monomer in solution, and monomeric AcrIIC4 directly interacted with Cas9 and Cas9/sgRNA complex. Discovery of the structure of AcrIIC4 and their interaction mode on Cas9 will help us elucidate the diversity in the inhibitory mechanisms of the Acr protein family. PubMed: 34676610DOI: 10.1002/pro.4214 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
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