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| Autori principali: | , , , , , , , |
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| Natura: | Artículo Open Access |
| Pubblicazione: |
Wiley
2025
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| Soggetti: | |
| Accesso online: | https://onlinelibrary.wiley.com/doi/10.1002/prot.26832 |
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Sommario:
- Structural Investigation of the Anti‐ CRISPR Protein AcrIE7 Jeehee Kang Changkon Park Gyujin Lee Jasung Koo Hyejin Oh Eun‐Hee Kim Euiyoung Bae Jeong‐Yong Suh Proteins: Structure, Function, and Bioinformatics ABSTRACT The CRISPR‐Cas system is an adaptive immune system in prokaryotes that provides protection against bacteriophages. As a countermeasure, bacteriophages have evolved various anti‐CRISPR proteins that neutralize CRISPR‐Cas immunity. Here, we report the structural and functional investigation of AcrIE7, which inhibits the type I‐E CRISPR‐Cas system in Pseudomonas aeruginosa . We determined both crystal and solution structures of AcrIE7, which revealed a novel helical fold. In binding assays using various biochemical methods, AcrIE7 did not tightly interact with a single Cas component in the type I‐E Cascade complex or the CRISPR adaptation machinery. In contrast, AlphaFold modeling with our experimentally determined AcrIE7 structure predicted that AcrIE7 interacts with Cas3 in the type I‐E CRISPR‐Cas system in P. aeruginosa . Our findings are consistent with a model where AcrIE7 inhibits Cas3 and also highlight the effectiveness and limitations of AlphaFold modeling. 10.1002/prot.26832 http://onlinelibrary.wiley.com/termsAndConditions#vor