8TIA

CryoEM structure of locally-refined tetramer of Shedu nuclease domain from Bacillus cereus

8TIA の概要

• エントリーDOI: 10.2210/pdb8tia/pdb
• EMDBエントリー: 41281 41282
• 分子名称: Shedu protein SduA (1 entity in total)
• 機能のキーワード: shedu, duf4263, bacterial defense systems, nuclease, anti-plasmid defense system, pd-(d/e)xk nuclease, whirly domain, two-component signaling, dna binding protein
• 由来する生物種: Bacillus cereus B4264
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 104947.04

構造登録者

Gu, Y.,Corbett, K. (登録日: 2023-07-19, 公開日: 2024-07-31, 最終更新日: 2025-05-28)

主引用文献

Gu, Y.,Li, H.,Deep, A.,Enustun, E.,Zhang, D.,Corbett, K.D.
Bacterial Shedu immune nucleases share a common enzymatic core regulated by diverse sensor domains.
Mol.Cell, 85:523-536.e6, 2025

PubMed Abstract: Prokaryotes possess diverse anti-bacteriophage immune systems, including the single-protein Shedu nuclease. Here, we reveal the structural basis for activation of Bacillus cereus Shedu. Two cryoelectron microscopy structures of Shedu show that it switches between inactive and active states through conformational changes affecting active-site architecture, which are controlled by the protein's N-terminal domain (NTD). We find that B. cereus Shedu cleaves near DNA ends with a 3' single-stranded overhang, likely enabling it to specifically degrade the DNA injected by certain bacteriophages. Bioinformatic analysis of Shedu homologs reveals a conserved nuclease domain with remarkably diverse N-terminal regulatory domains: we identify 79 distinct NTD types falling into eight broad classes, including those with predicted nucleic acid binding, enzymatic, and other activities. Together, these data reveal Shedu as a broad family of immune nucleases with a common nuclease core regulated by diverse NTDs that likely respond to a range of signals.

PubMed: 39742666
DOI: 10.1016/j.molcel.2024.12.004

実験手法

ELECTRON MICROSCOPY (2.77 Å)