8XEW
Cryo-EM structure of defence-associatedsirtuin 2 (DSR2) H171A protein
8XEW の概要
エントリーDOI | 10.2210/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 | |
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: 39083599DOI: 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) |
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