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TitleActivation of Thoeris antiviral system via SIR2 effector filament assembly.
Journal, issue, pagesNature, Vol. 627, Issue 8003, Page 431-436, Year 2024
Publish dateFeb 21, 2024
AuthorsGiedre Tamulaitiene / Dziugas Sabonis / Giedrius Sasnauskas / Audrone Ruksenaite / Arunas Silanskas / Carmel Avraham / Gal Ofir / Rotem Sorek / Mindaugas Zaremba / Virginijus Siksnys /
PubMed AbstractTo survive bacteriophage (phage) infections, bacteria developed numerous anti-phage defence systems. Some of them (for example, type III CRISPR-Cas, CBASS, Pycsar and Thoeris) consist of two modules: ...To survive bacteriophage (phage) infections, bacteria developed numerous anti-phage defence systems. Some of them (for example, type III CRISPR-Cas, CBASS, Pycsar and Thoeris) consist of two modules: a sensor responsible for infection recognition and an effector that stops viral replication by destroying key cellular components. In the Thoeris system, a Toll/interleukin-1 receptor (TIR)-domain protein, ThsB, acts as a sensor that synthesizes an isomer of cyclic ADP ribose, 1''-3' glycocyclic ADP ribose (gcADPR), which is bound in the Smf/DprA-LOG (SLOG) domain of the ThsA effector and activates the silent information regulator 2 (SIR2)-domain-mediated hydrolysis of a key cell metabolite, NAD (refs. ). Although the structure of ThsA has been solved, the ThsA activation mechanism remained incompletely understood. Here we show that 1''-3' gcADPR, synthesized in vitro by the dimeric ThsB' protein, binds to the ThsA SLOG domain, thereby activating ThsA by triggering helical filament assembly of ThsA tetramers. The cryogenic electron microscopy (cryo-EM) structure of activated ThsA revealed that filament assembly stabilizes the active conformation of the ThsA SIR2 domain, enabling rapid NAD depletion. Furthermore, we demonstrate that filament formation enables a switch-like response of ThsA to the 1''-3' gcADPR signal.
External linksNature / PubMed:38383786
MethodsEM (helical sym.) / X-ray diffraction
Resolution2.75 - 3.1 Å
Structure data

16233

8bto

EMDB-16233, PDB-8bto:
Helical structure of BcThsA in complex with 1''-3'gcADPR
Method: EM (helical sym.) / Resolution: 2.96 Å

16234

8btp

EMDB-16234, PDB-8btp:
Helical structure of BcThsA in complex with 1''-3'gc(etheno)ADPR
Method: EM (helical sym.) / Resolution: 2.75 Å

PDB-8btn:
Crystal structure of BcThsB
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Chemicals

ChemComp-OJC:
(2R,3R,3aS,5S,6R,7S,8R,11R,13S,15aR)-2-(6-amino-9H-purin-9-yl)-3,6,7,11,13-pentahydroxyoctahydro-2H,5H,11H,13H-5,8-epoxy-11lambda~5~,13lambda~5~-furo[2,3-g][1,3,5,9,2,4]tetraoxadiphosphacyclotetradecine-11,13-dione

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM / Nicotinamide adenine dinucleotide


ChemComp, No image

ChemComp-RK3:
Unknown entry

ChemComp-ENA:
ETHENO-NAD

Source
  • Bacillus cereus (bacteria)
  • bacillus cereus msx-d12 (bacteria)
KeywordsHYDROLASE / Thoeris / ThsB / TIR domain / SIR2 domain / SLOG domain / 3'cADPR

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