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8ZSF

CryoEM Helical Structure of KomC

Summary for 8ZSF
Entry DOI10.2210/pdb8zsf/pdb
EMDB information60413
DescriptorSir2 family NAD-dependent protein deacetylase (1 entity in total)
Functional Keywordsnadase, filament, cryoem, immune system
Biological sourceEscherichia coli
Total number of polymer chains12
Total formula weight367870.67
Authors
Feng, H.,Shao, K.,Luo, M. (deposition date: 2024-06-05, release date: 2025-12-10, Last modification date: 2026-06-24)
Primary citationFeng, H.,Shao, K.,Zeng, Z.,Tan, E.Y.J.,Hu, Z.,Zhao, R.,Rao, J.,Shi, J.,Chen, Z.,Redondo, R.P.,Wu, B.,Han, W.,Luo, M.
Filament-mediated repurposing of toxic dITP for immunity in the Kongming system.
Mol.Cell, 86:1148-1163.e5, 2026
Cited by
PubMed Abstract: Abortive infection systems protect bacteria by triggering self-destruction in response to phage attack. Most known systems rely on stable cyclic nucleotides that accumulate to stoichiometric levels to activate effectors; the Kongming (Kom) system employs the toxic metabolite deoxyinosine triphosphate (dITP) as its signaling molecule. Here, we show that the Escherichia coli KomB-KomC (KomBC) complex forms a preassembled filament that remains inactive until dITP binding induces cooperative allosteric activation. KomB, a homolog of the nucleotide-hydrolyzing enzyme HAM1, has lost catalytic activity but evolved a high-affinity, hydrolysis-resistant binding pocket for dITP. Interestingly, substoichiometric dITP binding is sufficient to activate adjacent KomC NADase domains, which propagate activation cooperatively along the filament. This filament-based architecture enables ultrasensitive, long-range allosteric signaling in response to a low-abundance and short-lived metabolite. Our findings reveal an ultrasensitive immune strategy that transforms a toxic byproduct into a robust antiviral trigger, expanding the known repertoire of bacterial defense strategies.
PubMed: 41638214
DOI: 10.1016/j.molcel.2026.01.027
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.24 Å)
Structure validation

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