8TK0
Structure of Gabija AB complex
Summary for 8TK0
Entry DOI | 10.2210/pdb8tk0/pdb |
EMDB information | 41314 41319 41321 |
Descriptor | Endonuclease GajA (1 entity in total) |
Functional Keywords | anti-phage defense, tetramer, dna recognition and cleavage, viral infection, bacterial immune system, immune system |
Biological source | Bacillus cereus |
Total number of polymer chains | 4 |
Total formula weight | 268317.88 |
Authors | Shen, Z.F.,Yang, X.Y.,Fu, T.M. (deposition date: 2023-07-24, release date: 2024-04-24, Last modification date: 2024-09-04) |
Primary citation | Yang, X.Y.,Shen, Z.,Xie, J.,Greenwald, J.,Marathe, I.,Lin, Q.,Xie, W.J.,Wysocki, V.H.,Fu, T.M. Molecular basis of Gabija anti-phage supramolecular assemblies. Nat.Struct.Mol.Biol., 31:1243-1250, 2024 Cited by PubMed Abstract: As one of the most prevalent anti-phage defense systems in prokaryotes, Gabija consists of a Gabija protein A (GajA) and a Gabija protein B (GajB). The assembly and function of the Gabija system remain unclear. Here we present cryo-EM structures of Bacillus cereus GajA and GajAB complex, revealing tetrameric and octameric assemblies, respectively. In the center of the complex, GajA assembles into a tetramer, which recruits two sets of GajB dimer at opposite sides of the complex, resulting in a 4:4 GajAB supramolecular complex for anti-phage defense. Further biochemical analysis showed that GajA alone is sufficient to cut double-stranded DNA and plasmid DNA, which can be inhibited by ATP. Unexpectedly, the GajAB displays enhanced activity for plasmid DNA, suggesting a role of substrate selection by GajB. Together, our study defines a framework for understanding anti-phage immune defense by the GajAB complex. PubMed: 38627580DOI: 10.1038/s41594-024-01283-w PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.23 Å) |
Structure validation
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