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6SCF

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

Summary for 6SCF
Entry DOI10.2210/pdb6scf/pdb
Related2x4i
DescriptorUncharacterized protein, cyclic oligoadenylate (3 entities in total)
Functional Keywordscrispr cyclic oligoadenylate dna anti-crispr viral, dna
Biological sourceSulfolobus islandicus rod-shaped virus 1
More
Total number of polymer chains12
Total formula weight134747.09
Authors
McMahon, S.A.,Athukoralage, J.S.,Graham, S.,White, M.F.,Gloster, T.M. (deposition date: 2019-07-24, release date: 2019-10-30, Last modification date: 2024-10-16)
Primary citationAthukoralage, J.S.,McMahon, S.A.,Zhang, C.,Gruschow, S.,Graham, S.,Krupovic, M.,Whitaker, R.J.,Gloster, T.M.,White, M.F.
An anti-CRISPR viral ring nuclease subverts type III CRISPR immunity.
Nature, 577:572-575, 2020
Cited by
PubMed Abstract: 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) and a cyclase domain (which synthesizes cyclic oligoadenylates from ATP). Cyclic oligoadenylates in turn activate defence enzymes with a CRISPR-associated Rossmann fold domain, sculpting a powerful antiviral response that can drive viruses to extinction. Cyclic nucleotides are increasingly implicated in host-pathogen interactions. Here we identify a new family of viral anti-CRISPR (Acr) enzymes that rapidly degrade cyclic tetra-adenylate (cA). 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 cA 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 cA 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.
PubMed: 31942067
DOI: 10.1038/s41586-019-1909-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.55 Å)
Structure validation

226707

數據於2024-10-30公開中

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