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8J4U

Structure of HerA-Sir2 complex from Escherichia coli Nezha system

This is a non-PDB format compatible entry.
Summary for 8J4U
Entry DOI10.2210/pdb8j4u/pdb
EMDB information35978
DescriptorSIR2-like domain-containing protein, Nucleoside triphosphate hydrolase, [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE, ... (5 entities in total)
Functional Keywordsdefense system hera sir2, immune system
Biological sourceEscherichia coli
More
Total number of polymer chains18
Total formula weight981756.25
Authors
Chen, Q.,Yu, Y. (deposition date: 2023-04-20, release date: 2024-01-03, Last modification date: 2025-06-18)
Primary citationTang, D.,Chen, Y.,Chen, H.,Jia, T.,Chen, Q.,Yu, Y.
Multiple enzymatic activities of a Sir2-HerA system cooperate for anti-phage defense.
Mol.Cell, 83:4600-4613.e6, 2023
Cited by
PubMed Abstract: 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 ∼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.
PubMed: 38096825
DOI: 10.1016/j.molcel.2023.11.010
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.97 Å)
Structure validation

237735

数据于2025-06-18公开中

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