Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Molecular and structural basis of an ATPase-nuclease dual-enzyme anti-phage defense complex.
Journal, issue, pages	Cell Res, Vol. 34, Issue 8, Page 545-555, Year 2024
Publish date	Jun 4, 2024
Authors	Qiyin An / Yong Wang / Zhenhua Tian / Jie Han / Jinyue Li / Fumeng Liao / Feiyang Yu / Haiyan Zhao / Yancheng Wen / Heng Zhang / Zengqin Deng /
PubMed Abstract	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.
External links	Cell Res / PubMed:38834762 / PubMed Central
Methods	EM (single particle)
Resolution	2.73 - 3.14 Å
Structure data	38203 8xau EMDB-38203, PDB-8xau: Cryo-EM structure of HerA Method: EM (single particle) / Resolution: 3.14 Å 38204 8xav EMDB-38204, PDB-8xav: Cryo-EM structure of an anti-phage defense complex Method: EM (single particle) / Resolution: 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 Method: EM (single particle) / Resolution: 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 Method: EM (single particle) / Resolution: 2.92 Å 38207 8xay EMDB-38207, PDB-8xay: Cryo-EM structure of an anti-phage defense complex bound to ATPrS and DNA Method: EM (single particle) / Resolution: 2.81 Å
Chemicals	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogueYM ChemComp-AGS: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM
Source	escherichia coli (E. coli)
Keywords	DNA BINDING PROTEIN / HerA / Helicase / DUF4297-HerA / Nuclease / Helicase DUF4297 / Endonuclease