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8TK0

Structure of Gabija AB complex

Summary for 8TK0
Entry DOI10.2210/pdb8tk0/pdb
EMDB information41314 41319 41321
DescriptorEndonuclease GajA (1 entity in total)
Functional Keywordsanti-phage defense, tetramer, dna recognition and cleavage, viral infection, bacterial immune system, immune system
Biological sourceBacillus cereus
Total number of polymer chains4
Total formula weight268317.88
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 citationYang, 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: 38627580
DOI: 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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