A 1.3 Å high-resolution crystal structure of an anti-CRISPR protein, AcrI E2.
Biochem Biophys Res Commun
; 533(4): 751-757, 2020 12 17.
Article
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| MEDLINE
| ID: mdl-32988588
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 ß-sheets (ß1â¼ß5) surrounding one α-helix (α1) in the order, ß2ß1α1ß5ß4ß3. Structural comparison of AcrIE2 with a structural homolog called AcrIF9 showed that AcrIE2 contained a long and flexible ß4-ß5 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.
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MEDLINE
Asunto principal:
Pseudomonas aeruginosa
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Proteínas Virales
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Proteínas Asociadas a CRISPR
Idioma:
En
Año:
2020
Tipo del documento:
Article