8JDI
Crystal structure of Cas7-AcrIF25 complex
Summary for 8JDI
| Entry DOI | 10.2210/pdb8jdi/pdb |
| Descriptor | CRISPR-associated protein Csy3, AcrIF25 (2 entities in total) |
| Functional Keywords | dna binding protein-inhibitor complex, dna binding protein/inhibitor |
| Biological source | Pseudomonas aeruginosa UCBPP-PA14 More |
| Total number of polymer chains | 8 |
| Total formula weight | 223134.91 |
| Authors | |
| Primary citation | Trost, C.N.,Yang, J.,Garcia, B.,Hidalgo-Reyes, Y.,Fung, B.C.M.,Wang, J.,Lu, W.T.,Maxwell, K.L.,Wang, Y.,Davidson, A.R. An anti-CRISPR that pulls apart a CRISPR-Cas complex. Nature, 632:375-382, 2024 Cited by PubMed Abstract: In biological systems, the activities of macromolecular complexes must sometimes be turned off. Thus, a wide variety of protein inhibitors has evolved for this purpose. These inhibitors function through diverse mechanisms, including steric blocking of crucial interactions, enzymatic modification of key residues or substrates, and perturbation of post-translational modifications. Anti-CRISPRs-proteins that block the activity of CRISPR-Cas systems-are one of the largest groups of inhibitors described, with more than 90 families that function through diverse mechanisms. Here, we characterize the anti-CRISPR AcrIF25, and we show that it inhibits the type I-F CRISPR-Cas system by pulling apart the fully assembled effector complex. AcrIF25 binds to the predominant CRISPR RNA-binding components of this complex, comprising six Cas7 subunits, and strips them from the RNA. Structural and biochemical studies indicate that AcrIF25 removes one Cas7 subunit at a time, starting at one end of the complex. Notably, this feat is achieved with no apparent enzymatic activity. To our knowledge, AcrIF25 is the first example of a protein that disassembles a large and stable macromolecular complex in the absence of an external energy source. As such, AcrIF25 establishes a paradigm for macromolecular complex inhibitors that may be used for biotechnological applications. PubMed: 38961300DOI: 10.1038/s41586-024-07642-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.372 Å) |
Structure validation
Download full validation report
