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TitleStructures and mechanism of E2-CBASS anti-phage system.
Journal, issue, pagesmLife, Vol. 5, Issue 1, Page 99-9107, Year 2026
Publish dateFeb 13, 2026
AuthorsJun Xiao / Yan Yan / Jing Li / Greater Kayode Oyejobi / Dongyang Lan / Bin Zhu / Zhiming Wang / Longfei Wang /
PubMed AbstractBacteria deploy diverse innate immune systems to combat bacteriophage infections. The cyclic-oligonucleotide-based anti-phage signaling system (CBASS) is a type of innate prokaryotic immune system. ...Bacteria deploy diverse innate immune systems to combat bacteriophage infections. The cyclic-oligonucleotide-based anti-phage signaling system (CBASS) is a type of innate prokaryotic immune system. CBASS synthesizes cyclic-oligonucleotide through cGAS/DncV-like nucleotidyltransferases (CD-NTases) to activate downstream effectors, which kill bacteriophage-infected bacteria, thereby stopping phage spread. One major class of CBASS contains a homolog of eukaryotic ubiquitin-conjugating enzymes, either as an E1-E2 fusion or a single E2 enzyme. Both enzymes function by regulating CD-NTase activity. Currently, many structures of CD-NTases have been reported, but there are only a few reports of structures where CD-NTases form complexes with the associated E2. In this study, we analyzed the length and classification of the CD-NTase in two types of type II CBASS-E1E2/JAB-CBASS and E2-CBASS. We found that the CD-NTase in E2-CBASS is longer and predominantly belongs to clade G. We also present the structure of the CdnG-E2 complex with the bound GTP substrate, which indicates the conservation of the donor binding pattern. Interestingly, we discovered that CdnG contains a conserved C-terminal α-helix and β-sheet structure, which is uniquely involved in forming a complex with E2. We also found that the structure of the E2 protein in the E2-CBASS system is highly conserved. Altogether, we provide mechanistic insights into the E2-CBASS system.
External linksmLife / PubMed:41767953 / PubMed Central
MethodsEM (single particle)
Resolution3.36 Å
Structure data

62384

9kkb

EMDB-62384, PDB-9kkb:
Cryo-EM Structure of CdnG-E2 complex with GTP from Serratia marcescens
Method: EM (single particle) / Resolution: 3.36 Å

Chemicals

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

Source
  • serratia marcescens (bacteria)
KeywordsANTIVIRAL PROTEIN / cGAS / CdnG / E2 / CBASS

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