9xxw

Structure of a putative anti-CRISPR from Streptobacillus moniliformis, ACZ01644

spinqualitylabelsall models 9xxw, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9xxw is a 2 chain structure with sequence from Streptobacillus moniliformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.98Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D1AV84_STRM9 Publication Abstract from PubMed The CRISPR-Cas system provides adaptive immunity in bacteria and archaea against invading genetic elements, while anti-CRISPR (Acr) proteins have evolved in phages to counteract this defense. Here, we report the first structural and biochemical characterization of ACZ01644, a protein previously predicted to be an Acr. The crystal structure of ACZ01644 reveals a unique cone-shaped architecture composed of five alpha-helices and five beta-strands forming a compact core, which represents a fold distinct from any known Acr family. Biochemical analyses demonstrated that ACZ01644 assembles as a trimer in solution, suggesting a potential functional relevance of this oligomeric state. However, in vitro assays revealed that ACZ01644 does not inhibit Cas9-mediated DNA cleavage, indicating that its inhibitory activity, if present, may involve other CRISPR subtypes or yet unidentified cofactors. Our findings reveal an unprecedented structural scaffold among putative Acr proteins and provide a foundation for future studies to elucidate its biological role in CRISPR-Cas regulation. Structural analysis of predicted anti-CRISPR, ACZ01644.,Park SE, Jeong JH, Kim YG, Park HH Biochem Biophys Res Commun. 2026 Jan 25;797:153199. doi: , 10.1016/j.bbrc.2025.153199. Epub 2025 Dec 22. PMID:41453247 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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