8j4u | pdb_00008j4u

Structure of HerA-Sir2 complex from Escherichia coli Nezha system

spinqualitylabelsall models 8j4u, resolution 2.97Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8j4u is a 18 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.97Å Ligands: AGS, AR6, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A7B5N0T7_ECOLX Publication Abstract from PubMed In response to the persistent exposure to phage infection, bacteria have evolved diverse antiviral defense mechanisms. In this study, we report a bacterial two-component defense system consisting of a Sir2 NADase and a HerA helicase. Cryo-electron microscopy reveals that Sir2 and HerA assemble into a approximately 1 MDa supramolecular octadecamer. Unexpectedly, this complex exhibits various enzymatic activities, including ATPase, NADase, helicase, and nuclease, which work together in a sophisticated manner to fulfill the antiphage function. Therefore, we name this defense system "Nezha" after a divine warrior in Chinese mythology who employs multiple weapons to defeat enemies. Our findings demonstrate that Nezha could sense phage infections, self-activate to arrest cell growth, eliminate phage genomes, and subsequently deactivate to allow for cell recovery. Collectively, Nezha represents a paradigm of sophisticated and multifaceted strategies bacteria use to defend against viral infections. Multiple enzymatic activities of a Sir2-HerA system cooperate for anti-phage defense.,Tang D, Chen Y, Chen H, Jia T, Chen Q, Yu Y Mol Cell. 2023 Dec 21;83(24):4600-4613.e6. doi: 10.1016/j.molcel.2023.11.010. , Epub 2023 Dec 13. PMID:38096825 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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