EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Molecular and structural basis of an ATPase-nuclease dual-enzyme anti-phage defense complex.
ジャーナル・号・ページ	Cell Res, Year 2024
掲載日	2024年6月4日
著者	Qiyin An / Yong Wang / Zhenhua Tian / Jie Han / Jinyue Li / Fumeng Liao / Feiyang Yu / Haiyan Zhao / Yancheng Wen / Heng Zhang / Zengqin Deng /
PubMed 要旨	Coupling distinct enzymatic effectors emerges as an efficient strategy for defense against phage infection in bacterial immune responses, such as the widely studied nuclease and cyclase activities in ...Coupling distinct enzymatic effectors emerges as an efficient strategy for defense against phage infection in bacterial immune responses, such as the widely studied nuclease and cyclase activities in the type III CRISPR-Cas system. However, concerted enzymatic activities in other bacterial defense systems are poorly understood. Here, we biochemically and structurally characterize a two-component defense system DUF4297-HerA, demonstrating that DUF4297-HerA confers resistance against phage infection by cooperatively cleaving dsDNA and hydrolyzing ATP. DUF4297 alone forms a dimer, and HerA alone exists as a nonplanar split spiral hexamer, both of which exhibit extremely low enzymatic activity. Interestingly, DUF4297 and HerA assemble into an approximately 1 MDa supramolecular complex, where two layers of DUF4297 (6 DUF4297 molecules per layer) linked via inter-layer dimerization of neighboring DUF4297 molecules are stacked on top of the HerA hexamer. Importantly, the complex assembly promotes dimerization of DUF4297 molecules in the upper layer and enables a transition of HerA from a nonplanar hexamer to a planar hexamer, thus activating their respective enzymatic activities to abrogate phage infection. Together, our findings not only characterize a novel dual-enzyme anti-phage defense system, but also reveal a unique activation mechanism by cooperative complex assembly in bacterial immunity.
リンク	Cell Res / PubMed:38834762
手法	EM (単粒子)
解像度	2.73 - 3.14 Å
構造データ	38203 8xau EMDB-38203, PDB-8xau: Cryo-EM structure of HerA 手法: EM (単粒子) / 解像度: 3.14 Å 38204 8xav EMDB-38204, PDB-8xav: Cryo-EM structure of an anti-phage defense complex 手法: EM (単粒子) / 解像度: 2.87 Å 38205 8xaw EMDB-38205, PDB-8xaw: Cryo-EM structure of an anti-phage defense complex bound to AMPPNP and DNA at state 1 手法: EM (単粒子) / 解像度: 2.73 Å 38206 8xax EMDB-38206, PDB-8xax: Cryo-EM structure of an anti-phage defense complex bound to AMPPNP and DNA at state 2 手法: EM (単粒子) / 解像度: 2.92 Å 38207 8xay EMDB-38207, PDB-8xay: Cryo-EM structure of an anti-phage defense complex bound to ATPrS and DNA 手法: EM (単粒子) / 解像度: 2.81 Å
化合物	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP / AMP-PNP, エネルギー貯蔵分子類似体YM ChemComp-AGS: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-γ-S / ATP-gamma-S, エネルギー貯蔵分子類似体*YM
由来	escherichia coli (大腸菌)
キーワード	DNA BINDING PROTEIN / HerA / Helicase / DUF4297-HerA / Nuclease / Helicase DUF4297 / Endonuclease