5Y6A

Crystal structure of the anti-CRISPR protein, AcrIIA1

5Y6A の概要

• エントリーDOI: 10.2210/pdb5y6a/pdb
• 関連するPDBエントリー: 5Y69
• 分子名称: chain A and B (2 entities in total)
• 機能のキーワード: unknown function, viral protein
• 由来する生物種: Listeria monocytogenes J0161
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34936.12

構造登録者

Ka, D.,An, S.Y.,Suh, J.Y.,Bae, E. (登録日: 2017-08-11, 公開日: 2017-11-29, 最終更新日: 2023-11-22)

主引用文献

Ka, D.,An, S.Y.,Suh, J.Y.,Bae, E.
Crystal structure of an anti-CRISPR protein, AcrIIA1
Nucleic Acids Res., 46:485-492, 2018

PubMed Abstract: Clustered regularly interspaced short palindromic repeats (CRISPRs) and CRISPR-associated (Cas) proteins provide bacteria with RNA-based adaptive immunity against phage infection. To counteract this defense mechanism, phages evolved anti-CRISPR (Acr) proteins that inactivate the CRISPR-Cas systems. AcrIIA1, encoded by Listeria monocytogenes prophages, is the most prevalent among the Acr proteins targeting type II-A CRISPR-Cas systems and has been used as a marker to identify other Acr proteins. Here, we report the crystal structure of AcrIIA1 and its RNA-binding affinity. AcrIIA1 forms a dimer with a novel two helical-domain architecture. The N-terminal domain of AcrIIA1 exhibits a helix-turn-helix motif similar to transcriptional factors. When overexpressed in Escherichia coli, AcrIIA1 associates with RNAs, suggesting that AcrIIA1 functions via nucleic acid recognition. Taken together, the unique structural and functional features of AcrIIA1 suggest its distinct mode of Acr activity, expanding the diversity of the inhibitory mechanisms employed by Acr proteins.

PubMed: 29182776
DOI: 10.1093/nar/gkx1181

実験手法

X-RAY DIFFRACTION (2 Å)