A high-resolution (1.2 Å) crystal structure of the anti-CRISPR protein AcrIF9

FEBS Open Bio. 2020 Dec;10(12):2532-2540. doi: 10.1002/2211-5463.12986. Epub 2020 Nov 5.

Abstract

Prokaryotic adaptive immunity by CRISPR-Cas systems, which confer resistance to foreign genetic elements, has been used by bacteria to combat viruses. To cope, viruses evolved multiple anti-CRISPR proteins, which can inhibit system function through various mechanisms. Although the structures and mechanisms of several anti-CRISPR proteins have been elucidated, those of the AcrIF9 family have not yet been identified. To understand the molecular basis underlying AcrIF9 anti-CRISPR function, we determined the 1.2 Å crystal structure of AcrIF9. Structural and biochemical studies showed that AcrIF9 exists in monomeric form in solution and can directly interact with DNA using a positively charged cleft. Based on analysis of the structure, we suggest part of the anti-CRISPR molecular mechanism by AcrIF9.

Keywords: AcrIF9; CRISPR-Cas system; adaptive immunity; anti-CRISPR proteins; crystal structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism
  • CRISPR-Associated Proteins / chemistry*
  • CRISPR-Associated Proteins / isolation & purification
  • CRISPR-Associated Proteins / metabolism
  • Crystallography, X-Ray
  • Models, Molecular
  • Protein Conformation
  • Pseudomonas aeruginosa / chemistry*

Substances

  • Bacterial Proteins
  • CRISPR-Associated Proteins