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Title | Molecular basis of Gabija anti-phage supramolecular assemblies. |
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Journal, issue, pages | Nat Struct Mol Biol, Year 2024 |
Publish date | Apr 16, 2024 |
Authors | Xiao-Yuan Yang / Zhangfei Shen / Jiale Xie / Jacelyn Greenwald / Ila Marathe / Qingpeng Lin / Wen Jun Xie / Vicki H Wysocki / Tian-Min Fu / |
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 ...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. |
External links | Nat Struct Mol Biol / PubMed:38627580 |
Methods | EM (single particle) |
Resolution | 2.79 - 3.23 Å |
Structure data | EMDB-41314, PDB-8tjy: EMDB-41319, PDB-8tk0: EMDB-41321, PDB-8tk1: |
Source |
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Keywords | IMMUNE SYSTEM / Anti-phage defense / Tetramer / DNA recognition and cleavage / Viral infection / Bacterial immune system |