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Publication Abstract from PubMed

Mammalian innate immune sensor STING (STimulator of INterferon Gene) was recently found to originate from bacteria. During phage infection, bacterial STING sense c-di-GMP generated by the CD-NTase (cGAS/DncV-like nucleotidyltransferase) encoded in the same operon and signal suicide commitment as a defense strategy that restricts phage propagation. However, the precise binding mode of c-di-GMP to bacterial STING and the specific recognition mechanism are still elusive. Here, we determine two complex crystal structures of bacterial STING/c-di-GMP, which provide a clear picture of how c-di-GMP is distinguished from other cyclic dinucleotides. The protein-protein interactions further reveal the driving force behind filament formation of bacterial STING. Finally, we group the bacterial STING into two classes based on the conserved motif in beta-strand lid, which dictate their ligand specificity and oligomerization mechanism, and propose an evolution-based model that describes the transition from c-di-GMP-dependent signaling in bacteria to 2'3'-cGAMP-dependent signaling in eukaryotes.

Crystal structure and functional implication of bacterial STING.,Ko TP, Wang YC, Yang CS, Hou MH, Chen CJ, Chiu YF, Chen Y Nat Commun. 2022 Jan 10;13(1):26. doi: 10.1038/s41467-021-26583-3. PMID:35013136^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.