7B5J
Anti-CRISPR associated (Aca) protein, Aca2
7B5J の概要
| エントリーDOI | 10.2210/pdb7b5j/pdb |
| 分子名称 | Anti-CRISPR associated (Aca) protein, Aca2, GLYCEROL (3 entities in total) |
| 機能のキーワード | rna-binding, dna-binding, anti-crispr, regulator, rna binding protein, anti-crispr associated (aca) protein, dna binding protein |
| 由来する生物種 | Pectobacterium phage ZF40 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 26511.80 |
| 構造登録者 | Usher, B.,Birkholz, N.,Fineran, P.C.,Blower, T.R. (登録日: 2020-12-03, 公開日: 2021-06-23, 最終更新日: 2024-06-19) |
| 主引用文献 | Usher, B.,Birkholz, N.,Beck, I.N.,Fagerlund, R.D.,Jackson, S.A.,Fineran, P.C.,Blower, T.R. Crystal structure of the anti-CRISPR repressor Aca2. J.Struct.Biol., 213:107752-107752, 2021 Cited by PubMed Abstract: Bacteria use adaptive CRISPR-Cas immune mechanisms to protect from invasion by bacteriophages and other mobile genetic elements. In response, bacteriophages and mobile genetic elements have co-evolved anti-CRISPR proteins to inhibit the bacterial defense. We and others have previously shown that anti-CRISPR associated (Aca) proteins can regulate this anti-CRISPR counter-attack. Here, we report the first structure of an Aca protein, the Aca2 DNA-binding transcriptional autorepressor from Pectobacterium carotovorum bacteriophage ZF40, determined to 1.34 Å. Aca2 presents a conserved N-terminal helix-turn-helix DNA-binding domain and a previously uncharacterized C-terminal dimerization domain. Dimerization positions the Aca2 recognition helices for insertion into the major grooves of target DNA, supporting its role in regulating anti-CRISPRs. Furthermore, database comparisons identified uncharacterized Aca2 structural homologs in pathogenic bacteria, suggesting that Aca2 represents the first characterized member of a more widespread family of transcriptional regulators. PubMed: 34116143DOI: 10.1016/j.jsb.2021.107752 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.34 Å) |
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