Evidence map›Paper›PMID 29182776›Full record

ArticleNucleic acids research2018

Crystal structure of an anti-CRISPR protein, AcrIIA1.

Donghyun Ka, So Young An, Jeong-Yong Suh, Euiyoung Bae

Abstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed.

  1. Article
  2. Genomic islands inNAR genomics and bioinformatics · 2025
    Article
  3. AcrIE7 inhibits the CRISPR-Cas system by directly binding to the R-loop single-stranded DNA.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. CRISPR in Nucleic Acids Research: the sequel.Nucleic acids research · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Atomic-scale insights into allosteric inhibition and evolutional rescue mechanism ofComputational and structural biotechnology journal · 2021
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Anti-CRISPRs: Protein Inhibitors of CRISPR-Cas Systems.Annual review of biochemistry · 2020
    Review
  17. Article
  18. Review
  19. Inhibition mechanisms of AcrF9, AcrF8, and AcrF6 against type I-F CRISPR-Cas complex revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. Structural insight into multistage inhibition of CRISPR-Cas12a by AcrVA4.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Donghyun KaDepartment of Agricultural Biotechnology, Seoul National University, Seoul 08826, Korea.
So Young AnDepartment of Agricultural Biotechnology, Seoul National University, Seoul 08826, Korea.
Jeong-Yong SuhDepartment of Agricultural Biotechnology, Seoul National University, Seoul 08826, Korea.
Euiyoung BaeDepartment of Agricultural Biotechnology, Seoul National University, Seoul 08826, Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clustered regularly interspaced short palindromic repeats (CRISPRs) and CRISPR-associated (Cas) proteins provide bacteria with RNA-based adaptive immunity against phage infection. To counteract this defense mechanism, phages evolved anti-CRISPR (Acr) proteins that inactivate the CRISPR-Cas systems. AcrIIA1, encoded by Listeria monocytogenes prophages, is the most prevalent among the Acr proteins targeting type II-A CRISPR-Cas systems and has been used as a marker to identify other Acr proteins. Here, we report the crystal structure of AcrIIA1 and its RNA-binding affinity. AcrIIA1 forms a dimer with a novel two helical-domain architecture. The N-terminal domain of AcrIIA1 exhibits a helix-turn-helix motif similar to transcriptional factors. When overexpressed in Escherichia coli, AcrIIA1 associates with RNAs, suggesting that AcrIIA1 functions via nucleic acid recognition. Taken together, the unique structural and functional features of AcrIIA1 suggest its distinct mode of Acr activity, expanding the diversity of the inhibitory mechanisms employed by Acr proteins.

Indexed as

Models, MolecularProtein DomainsAmino Acid SequenceCRISPR-Cas SystemsCrystallography, X-RayEscherichia coliHelix-Turn-Helix MotifsListeria monocytogenesMutationProphagesProtein BindingProtein MultimerizationRNAViral ProteinsRNAViral Proteins

Identifiers

PMID29182776
PMCPMC5758886

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.