7FA3

Selenomethionine-derived structure of Aca1 in Pseudomonas phage JBD30

「7C0B」から置き換えられました

7FA3 の概要

• エントリーDOI: 10.2210/pdb7fa3/pdb
• 分子名称: Aca1 (2 entities in total)
• 機能のキーワード: crispr, anti-crispr, anti-crispr-associated, dna binding, autoregulation, transcription
• 由来する生物種: Pseudomonas phage JBD30
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18826.79

構造登録者

Liu, Y.,Zhang, L.,Wu, B.,Huang, H. (登録日: 2021-07-05, 公開日: 2021-07-21, 最終更新日: 2024-10-16)

主引用文献

Liu, Y.,Zhang, L.,Guo, M.,Chen, L.,Wu, B.,Huang, H.
Structural basis for anti-CRISPR repression mediated by bacterial operon proteins Aca1 and Aca2.
J.Biol.Chem., 297:101357-101357, 2021

PubMed Abstract: It has been shown that phages have evolved anti-CRISPR (Acr) proteins to inhibit host CRISPR-Cas systems. Most acr genes are located upstream of anti-CRISPR-associated (aca) genes, which is instrumental for identifying these acr genes. Thus far, eight Aca families (Aca1-Aca8) have been identified, all proteins of which share low sequence homology and bind to different target DNA sequences. Recently, Aca1 and Aca2 proteins were discovered to function as repressors by binding to acr-aca promoters, thus implying a potential anti-anti-CRISPR mechanism. However, the structural basis for the repression roles of Aca proteins is still unknown. Here, we elucidated apo-structures of Aca1 and Aca2 proteins and their complex structures with their cognate operator DNA in two model systems, the Pseudomonas phage JBD30 and the Pectobacterium carotovorum template phage ZF40. In combination with biochemical and cellular assays, our study unveils dimerization and DNA-recognition mechanisms of Aca1 and Aca2 family proteins, thus revealing the molecular basis for Aca1-and Aca2-mediated anti-CRISPR repression. Our results also shed light on understanding the repression roles of other Aca family proteins and autoregulation roles of acr-aca operons.

PubMed: 34756887
DOI: 10.1016/j.jbc.2021.101357

実験手法

X-RAY DIFFRACTION (1.847 Å)