6scf

A viral anti-CRISPR subverts type III CRISPR immunity by rapid degradation of cyclic oligoadenylate

spinqualitylabelsall models 6scf, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6scf is a 12 chain structure with sequence from Sulfolobus islandicus rod-shaped virus 1 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Y114_SIRV1 Publication Abstract from PubMed The CRISPR system in bacteria and archaea provides adaptive immunity against mobile genetic elements. Type III CRISPR systems detect viral RNA, resulting in the activation of two regions of the Cas10 protein: an HD nuclease domain (which degrades viral DNA)(1,2) and a cyclase domain (which synthesizes cyclic oligoadenylates from ATP)(3-5). Cyclic oligoadenylates in turn activate defence enzymes with a CRISPR-associated Rossmann fold domain(6), sculpting a powerful antiviral response(7-10) that can drive viruses to extinction(7,8). Cyclic nucleotides are increasingly implicated in host-pathogen interactions(11-13). Here we identify a new family of viral anti-CRISPR (Acr) enzymes that rapidly degrade cyclic tetra-adenylate (cA4). The viral ring nuclease AcrIII-1 is widely distributed in archaeal and bacterial viruses and in proviruses. The enzyme uses a previously unknown fold to bind cA4 specifically, and a conserved active site to rapidly cleave this signalling molecule, allowing viruses to neutralize the type III CRISPR defence system. The AcrIII-1 family has a broad host range, as it targets cA4 signalling molecules rather than specific CRISPR effector proteins. Our findings highlight the crucial role of cyclic nucleotide signalling in the conflict between viruses and their hosts. An anti-CRISPR viral ring nuclease subverts type III CRISPR immunity.,Athukoralage JS, McMahon SA, Zhang C, Gruschow S, Graham S, Krupovic M, Whitaker RJ, Gloster TM, White MF Nature. 2020 Jan;577(7791):572-575. doi: 10.1038/s41586-019-1909-5. Epub 2020 Jan, 15. PMID:31942067 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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