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<p>Several antiviral immune systems based on nucleotide signaling have been identified in bacteria. One of them is the Kongming system, which includes an effector complex (KomBC), composed of a non-canonical purine NTP pyrophosphatase (KomB) and a SIR2 domain-containing protein (KomC). The Kongming system is activated by an atypical signaling nucleotide, dITP, generated upon phage infection. Here, we use structural and functional analyses to show that KomBC assembles into a helical filament, built from vertically stacked 4:4 KomB–KomC repeating units. Binding of dITP to KomB initiates progressive conformational rearrangements within the filament, ultimately remodeling the filament into a distinct architecture in which KomC adopts an active conformation with NADase activity. We further identify a key residue potentially involved in the acquisition of NADase activity in SIR2 family proteins. Thus, our results elucidate the activation mechanism of KomBC, revealing a distinct mode of effector activation by a signaling molecule.</p>

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dITP-induced remodeling activates the filamentous effector complex in Kongming anti-phage defense

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年6月26日

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  • Xia Li,
  • Min Liu,
  • Wenxue Jiang,
  • Guangbo Yan,
  • Dujuan Shi,
  • Qiong Xing,
  • Lixin Ma,
  • Fengtao Huang

摘要

Several antiviral immune systems based on nucleotide signaling have been identified in bacteria. One of them is the Kongming system, which includes an effector complex (KomBC), composed of a non-canonical purine NTP pyrophosphatase (KomB) and a SIR2 domain-containing protein (KomC). The Kongming system is activated by an atypical signaling nucleotide, dITP, generated upon phage infection. Here, we use structural and functional analyses to show that KomBC assembles into a helical filament, built from vertically stacked 4:4 KomB–KomC repeating units. Binding of dITP to KomB initiates progressive conformational rearrangements within the filament, ultimately remodeling the filament into a distinct architecture in which KomC adopts an active conformation with NADase activity. We further identify a key residue potentially involved in the acquisition of NADase activity in SIR2 family proteins. Thus, our results elucidate the activation mechanism of KomBC, revealing a distinct mode of effector activation by a signaling molecule.