A 1.3 Å high-resolution crystal structure of an anti-CRISPR protein, AcrI E2
- Authors
- Lee, So Yeon; Kim, Gi Eob; Kim, Yeon-Gil; Park, Hyun Ho
- Issue Date
- Dec-2020
- Publisher
- Elsevier B.V.
- Keywords
- AcrIE2; Adaptive immunity; anti-CRISPR proteins; CRISPR-Cas system; Crystal structure
- Citation
- Biochemical and Biophysical Research Communications, v.533, no.4, pp 751 - 757
- Pages
- 7
- Journal Title
- Biochemical and Biophysical Research Communications
- Volume
- 533
- Number
- 4
- Start Page
- 751
- End Page
- 757
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/53456
- DOI
- 10.1016/j.bbrc.2020.09.067
- ISSN
- 0006-291X
1090-2104
- Abstract
- As a result of bacterial infection with viruses, bacteria have developed CRISPR-Cas as an adaptive immune system, which allows them to destroy the viral genetic material introduced via infection. However, viruses have also evolved to develop multiple anti-CRISPR proteins, which are capable of inactivating the CRISPR-Cas adaptive immune system to combat bacteria. In this study, we aimed to elucidate the molecular mechanisms associated with anti-CRISPR proteins by determining a high-resolution crystal structure (1.3 Å) of Type I-E anti-CRISPR protein called AcrIE2. Our structural analysis revealed that AcrIE2 was composed of unique folds comprising five antiparallel β-sheets (β1∼β5) surrounding one α-helix (α1) in the order, β2β1α1β5β4β3. Structural comparison of AcrIE2 with a structural homolog called AcrIF9 showed that AcrIE2 contained a long and flexible β4-β5 connecting loop and a distinct surface feature. These results indicated that the inhibitory mechanism of AcrIE2 might be different from that of AcrIF9. This unique structure of AcrIE2 indicates its special mode of CRISPR-Cas inhibitory activity. Therefore, this study helps us understand the diversity in the inhibitory mechanisms of Acr family. © 2020 Elsevier Inc.
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