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TitleInsights into the modulation of bacterial NADase activity by phage proteins.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 2692, Year 2024
Publish dateMar 27, 2024
AuthorsHang Yin / Xuzichao Li / Xiaoshen Wang / Chendi Zhang / Jiaqi Gao / Guimei Yu / Qiuqiu He / Jie Yang / Xiang Liu / Yong Wei / Zhuang Li / Heng Zhang /
PubMed AbstractThe Silent Information Regulator 2 (SIR2) protein is widely implicated in antiviral response by depleting the cellular metabolite NAD. The defense-associated sirtuin 2 (DSR2) effector, a SIR2 domain- ...The Silent Information Regulator 2 (SIR2) protein is widely implicated in antiviral response by depleting the cellular metabolite NAD. The defense-associated sirtuin 2 (DSR2) effector, a SIR2 domain-containing protein, protects bacteria from phage infection by depleting NAD, while an anti-DSR2 protein (DSR anti-defense 1, DSAD1) is employed by some phages to evade this host defense. The NADase activity of DSR2 is unleashed by recognizing the phage tail tube protein (TTP). However, the activation and inhibition mechanisms of DSR2 are unclear. Here, we determine the cryo-EM structures of DSR2 in multiple states. DSR2 is arranged as a dimer of dimers, which is facilitated by the tetramerization of SIR2 domains. Moreover, the DSR2 assembly is essential for activating the NADase function. The activator TTP binding would trigger the opening of the catalytic pocket and the decoupling of the N-terminal SIR2 domain from the C-terminal domain (CTD) of DSR2. Importantly, we further show that the activation mechanism is conserved among other SIR2-dependent anti-phage systems. Interestingly, the inhibitor DSAD1 mimics TTP to trap DSR2, thus occupying the TTP-binding pocket and inhibiting the NADase function. Together, our results provide molecular insights into the regulatory mechanism of SIR2-dependent NAD depletion in antiviral immunity.
External linksNat Commun / PubMed:38538592 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.9 Å
Structure data

36980

8k98

EMDB-36980, PDB-8k98:
Cryo-EM structure of DSR2-TTP
Method: EM (single particle) / Resolution: 2.9 Å

36982

8k9a

EMDB-36982, PDB-8k9a:
Cryo-EM structure of DSR2-DSAD1 state 2
Method: EM (single particle) / Resolution: 3.9 Å

37272

8w56

EMDB-37272, PDB-8w56:
Cryo-EM structure of DSR2-DSAD1 state 1
Method: EM (single particle) / Resolution: 3.59 Å

37603

8wkn

EMDB-37603, PDB-8wkn:
Cryo-EM structure of DSR2-DSAD1
Method: EM (single particle) / Resolution: 3.4 Å

38421

8xkn

EMDB-38421, PDB-8xkn:
Cryo-EM structure of tail tube protein
Method: EM (single particle) / Resolution: 3.11 Å

Source
  • bacillus halotolerans (bacteria)
  • bacillus subtilis (bacteria)
KeywordsANTIVIRAL PROTEIN / cryo-EM structure of a protein

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