7CHQ

AcrIE2

Summary for 7CHQ

• Entry DOI: 10.2210/pdb7chq/pdb
• Descriptor: anti-CRISPR AcrIE2 (2 entities in total)
• Functional Keywords: acrie2, immune system, crispr cascade inhibitor.
• Biological source: Pseudomonas phage JBD16C
• Total number of polymer chains: 1
• Total formula weight: 10432.38

Authors

Lee, S.Y.,Park, H.H. (deposition date: 2020-07-06, release date: 2021-05-19, Last modification date: 2024-03-27)

Primary citation

Lee, S.Y.,Kim, G.E.,Kim, Y.G.,Park, H.H.
A 1.3 angstrom high-resolution crystal structure of an anti-CRISPR protein, AcrI E2.
Biochem.Biophys.Res.Commun., 533:751-757, 2020

PubMed 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, ββαβββ. 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.

PubMed: 32988588
DOI: 10.1016/j.bbrc.2020.09.067

Experimental method

X-RAY DIFFRACTION (1.33 Å)