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8XEW

Cryo-EM structure of defence-associatedsirtuin 2 (DSR2) H171A protein

8XEW の概要
エントリーDOI10.2210/pdb8xew/pdb
EMDBエントリー38297
分子名称DSR2 H171A (1 entity in total)
機能のキーワードcryo-em, defence-associated sirtuin 2 (dsr2) protein, sir2, cell invasion
由来する生物種Bacillus sp. DSM 5850
タンパク質・核酸の鎖数4
化学式量合計474274.91
構造登録者
Li, Y.,Zhang, H.,Zheng, Q.,Wu, Y.,Li, S. (登録日: 2023-12-13, 公開日: 2024-10-23)
主引用文献Zhang, H.,Li, Y.,Li, L.,Chen, L.,Zhu, C.,Sun, L.,Dong, P.,Jing, D.,Yang, J.,Fu, L.,Xiao, F.,Xia, N.,Li, S.,Zheng, Q.,Wu, Y.
Structural insights into activation mechanisms on NADase of the bacterial DSR2 anti-phage defense system.
Sci Adv, 10:eadn5691-eadn5691, 2024
Cited by
PubMed Abstract: As a sirtuin (SIR2) family protein, defense-associated sirtuin2 (DSR2) has been demonstrated to participate in bacterial anti-phage resistance via depleting nicotinamide adenine dinucleotide (NAD) of infected cells, which can be activated by tail tube protein (TTP) and inhibited by DSR anti-defense 1 (DSAD1) of diverse phages. However, the regulating mechanism remains elusive. Here, we determined the cryo-electron microscopy structure of apo DSR2, as well as the respective complex structures with TTP and DSAD1. Structural analyses and biochemical studies reveal that DSR2 forms a tetramer with a SIR2 central core and two distinct conformations. Monomeric TTP preferentially binds to the closed conformation of DSR2, inducing conformational distortions on SIR2 tetramer assembly to activate its NADase activity. DSAD1 combines with the open conformation of DSR2, directly or allosterically inhibiting TTP activation on DSR2 NAD hydrolysis. Our findings decipher the detailed molecule mechanisms for DSR2 NADase activity regulation and lay a foundation for in-depth understanding of the DSR2 anti-phage defense system.
PubMed: 39083599
DOI: 10.1126/sciadv.adn5691
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.92 Å)
構造検証レポート
Validation report summary of 8xew
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-16に公開中

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