7EBD
Bacterial STING in complex with c-di-GMP
Summary for 7EBD
| Entry DOI | 10.2210/pdb7ebd/pdb |
| Descriptor | TIR-like domain-containing protein, ACETATE ION, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one), ... (4 entities in total) |
| Functional Keywords | second messenger, complex, cyclic dinucleotide, antiviral pathway, signaling protein |
| Biological source | Prevotella corporis |
| Total number of polymer chains | 2 |
| Total formula weight | 38070.75 |
| Authors | Ko, T.-P.,Wang, Y.-C.,Yang, C.-S.,Hou, M.-H.,Chen, Y. (deposition date: 2021-03-09, release date: 2021-09-15, Last modification date: 2024-10-16) |
| Primary citation | Ko, T.-P.,Wang, Y.-C.,Yang, C.-S.,Hou, M.-H.,Chen, C.-J.,Chiu, Y.-F.,Chen, Y. Crystal structure and functional implication of bacterial STING. Nat Commun, 13:26-26, 2022 Cited by PubMed Abstract: 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 β-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. PubMed: 35013136DOI: 10.1038/s41467-021-26583-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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